biofiles v5 n5 - enzymes and reagents for alternative energy · biodiesel ethanol h 3c–ch 2 oh o...
TRANSCRIPT
Volume 5, Number 5
Metabolic strategies in alternative energy
Enzyme-based fuel cells
Lignocellulosic depolymerization
Enzymes for biofuel research
Reagents for ethanol and biodiesel analysis
Enzymes and Reagents for Alternative Energy
Biofiles
Biofilescontents
Introduction 3
Advancements in Enzyme-BasedFuel Cell Batteries, Sensors andEmissions Reduction Strategies 8
Selected Enzymes for Biofuel Cell Research 10
Enzymes and Reagents for Ethanol Research 12Enzymes for Lignocellulosic Ethanol Research 12Enzymes for Starch Hydrolysis 20
Ethanol Analysis 23
Enzymes for BioDiesel Research 24
Lipase 24Phospholipase C 24BioDiesel Analysis 25
Metabolic Standards for Mevalonate and Isoprenoid Pathway Analysis 30
BiofilesonlineYour gateway to Biochemicals and Reagents for
Life Science Research
BioFiles Online allows you to:
Easily navigate the content of •the current BioFiles issue
Access any issue of BioFiles •Subscribe for email notifications •
of future eBioFiles issues
Register today for upcoming issues and eBioFiles announcements at
sigma.com/biofiles
Greener ProductsSigma-Aldrich is committed to doing our
part to minimize our footprint on the environment. As a life science and high
technology company, we recognize your need for high quality chemicals comes
first. In cases where it becomes possible to consider alternatives, we have made it
easier for you to find greener options through our new “Greener Alternatives
and Technologies” product lists.
Products Including:
Quality Environmentally-Friendly Enzymes•Ionic Liquids•
Greener Alternatives: Solvents•Greener Alternatives: Reagents•
sigma-aldrich.com/green
Life Science Labware CenterThe Life Science Labware Center allows
easy browsing of labware products, including disposables, books,
and equipment
Features Include:Corning® cell culture selection guide•
Products by top manufacturers•New products by research areas •
New lab start-up programs•Start using the Life Science Labware center at
sigma-aldrich.com/lslabwareTechnical content: Robert Gates, M. S. M.
Order sigma.com/order Technical service sigma.com/techinfo sigma.com/lifescience 3
Leveraging nature’s metabolic strategies for tomorrow’s energy resources.Although most of the world’s population understands that carbon dioxide is the predominant end product of energy production from combustible fuels, most of us forget that the “raw material” for most of our combustible fuel sources is also atmospheric carbon dioxide. Photosynthetic carbon dioxide fixation is most often the first step in the synthesis of both our renewable fuels and non-renewable fossil fuels. Even much of our hydrogen production is an indirect product of carbon dioxide fixation as it is often derived from fossil fuels.
The basic differences between non-renewable fossil fuels and our “new generation” renewable fuels is time, energy input and mass. Our non-renewable fuels, such as petroleum and coal required thousands of years of collection of solar energy to power carbon fixation for the biosynthesis of enormous amounts of biomass. That biomass then underwent millions of years of anaerobic decomposition to yield today’s fossil fuels. In our attempt to circumvent or speed up this process, we are finding natural “renewable analogs” to some of our fossil fuels, i.e., ethanol and butanol to replace or supplement gasoline and fatty acid esters to replace diesel.
However, we have not advanced far enough in our manufacturing technology to divest ourselves of the need for biological systems to do the complicated work for us. Current processes for ethanol production rely on plants to fix carbon dioxide, synthesize a “common currency” molecule such as
IntroductionRobert GatesMarket Segment [email protected]
glucose, and then needlessly polymerize this glucose into starch or cellulose. Then we often rely on microbial and enzymatic hydrolysis of these biopolymers to give back glucose and then ferment it to yield ethanol. Sugarcane ethanol employs a slightly simpler path via sucrose.
Our challenge for the future may be to find the “straightest metabolic line” between carbon dioxide and ethanol, butanol, fatty acids or even hydrogen. The ideal route to ethanol production might be to devise an enzymatic or cellular system to fix carbon dioxide and take the direct route from ribose-1,5-bis-phosphate to pyruvate to ethanol and bypass glucose biosynthesis, polymerization and depolymerization. We have included the Nicholson/IUBMB Metabolic Pathway chart on the following pages illustrating the specific pathways related to carbon dioxide fixation and glucose, cellulose, pectin, starch, lignin and ethanol production highlighted in yellow.
Enzymes and their metabolic pathways enter the energy equation from other directions. Microbial strains are being discovered that can ferment cellulosic biomass to yield hydrogen. Some photosynthetic microbes, such as algae, are capable of splitting water to produce hydrogen utilizing solar energy. Hydrogenases are being targeted not only for hydrogen production but also for the oxidation of H2 in fuel cells. Immobilized enzyme-based fuel cell batteries can utilize multi-enzyme systems that mimic in vivo glycolytic and Krebs Cycle pathways. Immobilized enzymes are also being studied for the sequestration of carbon dioxide emissions.
4
Engineering organisms and enzyme systems to maximize biofuel production could require insertion of exogenous enzymatic pathways from various organisms into a new host. In addition, alternative metabolic pathways such as the mevalonate and isoprenoid pathways are being studied as sources of biofuel.
This issue of BioFiles is devoted to how Sigma-Aldrich enzymes and reagents are involved in many of these areas of research. As summarized above and illustrated
Hydrogen
O
OH
OH
O
O
H
O
O CH3O
HO
O
CH3O
OH
OH
H
HO
CH3O
O
CH3O
CH 3O
HO OHO
O CH3O CH3O
O
CH3OHO
HOHO
O
O
CH3O
CH3OO
O O
OH
O
CH3O
OCH3
HO
O
OCH3
HO
HO
HO
HO
HO
O
OO
OH
OH
O
O
O
H
OH
OH
OH CH 3O
CH3O
CH3O
O
HO
CH3O
O
OCH2OH
OH
OHO
CH2OH
OH
OH
OH
O
OCH2OH
OH
OH
O
OCH2OH
OH
OH
O
OCH2OH
OH
OHO
OH
CH2OH
OH
OH
O
n
OCH2OH
OH
OH
O
OCH2OH
OH
OHO
OCH2O
OH
OH
O
OCH2OH
OH
OHO O
n
OO
OH
CH2OH
OH
OH
C
H
H
H
H
C
H
H
H
C
H
H
C
H
H
H
CH
H
HCH
H
H
CH
H
CH
H
CH
H
CH
H
CH
H
CH
H
CH
H
H
CH
H
CH
H
CH
H
CH
H
CH
H
CH
H
HCH
H
CH
H
CH
H
CH
H
CH
H
CH
H
O S O
OH
OH OH
OH NH2 OCOOH S
SO
S
HO H
ON
OH HO
HO O OH
OH
CH3
H2
CH3H2
H3CCH2
CH2C
CH2CH2
CH2CH2
CH2CH2
CH2CH2
CH2CH2
C
O
O
CH3H2
H3CCH2
CH2C
CH2CH2
CH2CH2
CH2CH2
CH2CH2
CH2CH2
C
O
O
CHH2
H3CCH2
CH2C
CH2CH2
CH2CH2
CH2CH2
CH2CH2
CH2CH2
2C
O
O
CH3H2
H3CCH2
CH2C
CH2CH2
CH2CH2
CH2CH2
CH2CH2
CH2CH2
C
O
O
Solar Energy
CO2
Carbon Dioxide
CO2
Fixation
Biomass
Cellulose
Starch
Lipids
Glucose
Anabolic InVivo Enzymatic Conversions
FuelsNon-Renewable
Fossil Fuels
Renewable Fuels
Combustion
Microbial, Enzymatic andChemical Conversions
AnaerobicDecomposition
CO2
Carbon Dioxide
Methane (Natural Gas)
Propane
Gasoline
Diesel
Coal
BioDiesel
Ethanol
H3C–CH2 OH
OO
OH
CH2OH
OH
OH
Glucose
Lignin
Todays fuel sources originate primarily from the biosythesis of hydrocarbons originating from photosynthetic carbon dioxide fixation. The combustion of these fuels results in production of carbon dioxide. Ideally, this might someday be a “closed-CO2-loop” system with solar power as the only energy input. Many of the structures shown are basic examples of simple unbranched molecules intended to represent heterogeneous mixtures.
below, many of these areas require an understanding of metabolic pathways and enzymatic processes.
References
(1) S. Atsumi, J. C. Liao, Metabolic Engineering for Ad-vanced Biofuels Production from Escherichia coli, Curr. Opin. Biotechnol., 19, 414–419 (2008).
(2) H. Alper, G. Stephanopoulos, Engineering for biofuels: exploiting innate microbial capacity or importing biosynthetic potential?, Nature Reviews, Microbiology, 7, 715–723 (2009).
(3) P. P. Peralta-Yahya, J. D. Keasling, Advanced biofuel pro-duction in microbes, Biotechnol. J., 5, 147–162 (2010).
(4) J. M. Clomburg, R. Gonzalez, Biofuel production in Escherichia coli: the role of metabolic engineering and synthetic biology, Appl. Microbiol. Biotechnpl., 86, 419–434 (2010).
(5) D. Klein-Marcuschamer, V. G. Yadav, A. Ghaderi, G. Stephanopoulos, De Novo Metabolic Engineering and the Promise of Synthetic DNA, Adv. Biochem. Eng. Biotech-nol. in press (2010).
(6) J. L. Fortman, S. Chhabra, A. Mukhopadhyay, H. Chou, T. S. Lee, E. Steen, J. D. Keasling, Biofuel alternatives to etha-nol: pumping the microbial well, Trends in Biotechnol., 26 375–381 (2010).
(7) D. B. Levin, R. Islam, N. Cicek, R. Sparling, Hydrogen production by Clostridium thermocellum 27405 from cellulosic biomass substrates., Int. J. Hydrogen Energy, 31, 1496–1503 (2006)
(8) M. L. Ghirardi, S. Kosourov, A. Tsygankov1, A. Rubin, M. Seibert, Cyclic Photobiological Algal H2 Production, Proceedings of the 2002 U. S. DOE Hydrogen Program Review
(9) A. A. Karyakin, S. V. Morozov, E. E. Karyakina, N. A. Zorin V. V. Perelygin, S. Cosnie, Hydrogenase Electrodes for Fuel Cells, International Hydrogenases Conference 2004.
Order sigma.com/order Technical service sigma.com/techinfo sigma.com/lifescience 5
The New Enzyme ExplorerRedesigned Format and Expanded Resources.
The Enzyme Explorer Indices provide paths to find more than 3,000:
Enzyme/proteins•Inhibitors•Substrates•Cofactors•
The Enzyme Explorer Product Features include enzyme and protein related products for Cell Biology, Diagnostics and industrial scale manufacturing.
The Enzyme Explorer Learning Center
includes:IUBMB Metabolic Pathways•Proteolytic Enzyme Resources•Enzyme Assay Library•Carbohydrate Analysis Enzyme Resource•Product Guides and Protocols•The New Protease Finder•
Allow the New Protease Finder to help you locate both the endo and exoproteases needed for precision protein cleavage.
Request Enzyme Literature•Proteolytic Enzymes•Protease Inhibition•Diagnostic and Metabolic Research•Detection Substrates•Metabolomics and Dietary Research•Cell Dissociation and Lysis•Plasma Proteins•Carbohydrate Analysis•Proteomics and Protein Expression•
sigma-aldrich.com/enzymeexplorer
6
2H+
H+
OX
ALO
AC
ETA
TE
PYR
UVA
TE
SU
CC
INY
L-C
oA
GLU
TAR
ATE
CIT
RAT
E
MA
LATE
2-O
XO-
ASP
AR
TATE
NO
2-
NO
3- N2
NH
4
CH
3CO
SC
oA
AC
ETYL
- CoAHO
H
CO
2
NA
D
TRANSAMINAT
ION
2H+
2H+
+
CO
2
5-A
min
o-le
vulin
ate
Gly
cine
H+
H+H+
H+
H+H+
c
H+
H+
a
F0
F1
F1
β 2
1α
β
α
γ
10c-
sub-
units
A D
P+
Pi
aaH
+
3.6.
1.34
H+-tra
nspo
rting
ATP
synt
hase
α
δF 6
oscp
ATP
ADP
+Pi
FUM
AR
ATE
UQ
H2
UQ
UQ
H2
NA
DH
+H+
CH
2CO
O-
C(O
H)C
OO
-C
H2C
OO
-
CH
(OH
)CO
O-
CH
CO
O-
CH
2CO
O-
- OO
CC
OC
H2C
H2C
OO
-
- OO
CC
H2C
H2C
O.S
CoA
- OO
CC
OC
H2C
OO
-
CH
3CH
(OH
)CH
2CO
.SC
oA
- OO
CC
H=C
HC
OO
-
CCCCC
Gly
oxyl
ate
C
ycle
-OO
CC
HO
GTP
GD
PAT
P
+
HEM
EPr
otop
orph
yrin
ogen
Cop
ropo
rphy
rinog
enU
ropo
rphy
rinog
enPo
rpho
bilin
ogen
5-A
min
o-le
vulin
ate
CO
O-
CH
2C
H2
H2N
CH
2C=O
FAD
H2 FA
DC
yt.bFe-S
SU
CC
INAT
EII
CH
3CO
CO
O-
PYR
UVA
TE
P i
XY
Cyt.c
1
Fe-S
2e-
2e-
1e- 1e
-
III
2UQ
UQ
UQ
H2
2UQ
H2
2UQ
._
UQ
._
Cyt
.bL
Cyt
.bH
Cyt.c
IV
Cu A
CuB
Cu A 1.9.
3.1
2e-
Hem
e a
Hem
e a 3
2H+
2H+
4H+
4H+
2H+
NAD
+
NA
DH
+H+
NA
D+
1.1.
1.39
1.2.
4.1
2.3.
1.12
3.1.
3.43
4.1.
1.32
4.1.
3.7
4.2.
1.3
1.1.
1.41
1.2.
4.2
2.3.
1.61
6.2.
1.4
- OO
CC
H2C
H2C
OO
-
1.3.
5.1
4.2.
1.2
1.1.
1.37
6.4.
1.1
4.1.
3.8
4.1.
3.1
4.1.
3.2
ISO
CIT
RAT
E
2.6.
1.1
2.3.
1.16
4.1.
1.71
1.2.
1.16
5.1.
99.1
5.4.
99.2
4.3.
1.1
1.4.
1.2
1.4.
1.14
6.3.
5.4
1.6.
6.1
1.7.
99.4
1.7.
7.1
1.6.
6.4
1.18.6
.1
2.3.
1.37
1.10
.2.2
1.10
.2.2
γ
εδ
β
H++
33β
AT
P
AD
P
END
ERG
ON
ICR
EAC
TIO
N
1.6.5.3I
FMN
H2
FMN
I
1.6.
5.3
2Fe
-S
(5 C
luste
rs)
H+
H+
H+
H+AT
P
4H+
2H+
2H+or
H+
PHO
TO-
SYST
EM l
O2
3.6.
1.34
NA
DP
+
Gly
cera
ldeh
yde
Rib
ulos
e-1,
5-bi
s-P
2β
8 8
H+
c
3 2
ε
a
3 2
α1α
ε
α
β2
1
3
α
αβ
3
α
β
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
Tran
sloc
ated
pro
tons
H+
H+
H+
H+
Pi
Ferre
doxi
n
4H+
PCPC
PC
PQ
H2 2P
QH
2
PQ
_ .
2PQ
_ . Fe-S
Cyt
.f
PQ
2PQ
Cyt
bf2e-
1e-
1e-
2e-
2e-
2e-
2e-
Cycli
cPh
otop
hosp
hory
latio
n
PQ
PH
OTO
-S
YS
TEM
I
I
Cyt
bc
Non-
cycl
icel
ectro
nflo
w
2e-
2e-
Mn
2e-
*
Prot
ons
from
Wat
er
H2O
H+
H+
2H+
2H+
γ
ATP
synt
hase
CO
2Fi
xatio
n
H+
AD
PP
i
H+ NA
DPH
+H+
eeeAT
PTH
YLA
KO
ID M
EM
BR
AN
E
CH
LOR
OP
LAS
T O
UTE
R M
EM
BR
AN
E
THY
LAK
OID
LU
ME
N
STR
OM
A
(ele
ctric
curre
nt)
P680
Chl
.a
QA
QB
Pheo
phyt
in
P700
Chl
.A0
A 1Fe-S
ATP
AD
P
ATP
1 / 2O
2 H2O
PQ
H2
To B
rain
-
A M I N O A C I D SP Y R I M I D I N E SP U R I N E SC A T E C H O L A M I N E SA R O M A T I C A M I N O A C I D S
hvVI
SIO
N
L I P I DP H O T O S Y N T H E S I S P O R P H Y R I N SS T E R O I D SI S O P R E N O I D SP H O S P H O L I P I D SD E G R A D A T I O NL I P I D B I O S Y N T H E S I SP E N T O S E SH E X O S E SP O L Y S A C C H A R I D E S
CO
CH
CH
(NH
)CO
O2
3+
FOLI
CAC
IDC
1PO
OL
VALI
NE
ATPAT
P
4.1.
1.4
1.1.
1.30
CH
CO
CH
33 CH
CO
CH
CO
O3
2
CH
CH
(OH
)CH
CO
O3
23-
OH
-But
yrat
eA
ceto
ne Ace
toac
etat
e
KET
ON
E B
OD
IES
HYA
LUR
ON
IC A
CID
DER
MAT
AN
BLO
OD
GR
OU
PSU
BST
AN
CES
PEPT
IDO
-G
LYC
AN
N-A
c-N
eura
min
ate
(Sia
late
)
UD
P-Id
uron
ate
UD
P-N
-Ac-
Gal
acto
sam
ine
UD
P-G
alac
turo
nateG
DP-
Fuco
se
TDP-
Rha
mno
se
AD
P-G
luco
se
UD
P-G
luco
se
TDP-
4-O
xo-
6-de
oxyg
luco
se
MA
NN
OSE
CH
ITIN
CH
ON
DR
OIT
INP
EC
TIN
ALG
INAT
ES
INU
LIN
CEL
LULO
SE
O-A
NTI
GEN
SST
AR
CH
GLY
CO
GEN
LAC
TOSE
GA
LAC
TOSE
O
OH
HO
OH
OH
CH
3O
OPP
TO
OH
OH
O
OHAC
NH
HO
OH
O
OH
HO
OP
PU
NH
AC
OH
OH
OH O
H
HO
OH
NH
CO
CH
OH
HOO
OP
PG
CH
OH
2
HO
P
UD
P-N
-Ac-
Glu
cosa
min
epy
ruva
teN
-Ac-
Man
nosa
min
e-6-P
UD
P-G
lucu
rona
te
GD
P-M
anno
se
N-A
c-M
anno
sam
ine
UD
P-N
-Ac-
Glu
cosa
min
eN
-Ac-
Glu
cosa
min
e-6-P
Sorb
itol
Fruc
tose
-1-P
Eryt
hros
e-4-P
3-D
ehyd
rogu
lona
te
L-Xy
lose
L-Ly
xose
D-X
ylul
ose
D-R
ibos
e
Rib
itol
L-A
rabi
tol
L-Xy
lulo
se
L-R
ibul
ose
L-R
ibul
ose-
5-P
L-Xy
lulo
se-5
-P
L-A
rabi
nose
Xylit
olD
-Xyl
ose
D-A
rabi
nose
D-R
ibul
ose
ASC
OR
BATE
2, 3
-Dio
xogu
lona
te
N-A
c-G
luco
sam
ine-
1-P
Inos
itol-P
Inos
itol
Glu
curo
nate
Gul
onat
e
Gul
onol
acto
ne2-
Oxo
gulo
nola
cton
e
Fruc
tose 6-P-
Glu
cona
te
D-R
ibul
ose-
5-P D
-Xyl
ulos
e-5-P
Man
nose
-1-P
GD
P-G
luco
se
TDP-
Glu
cose
UD
P-G
alac
tose
Gal
acto
se-P
Glu
cose
-1-P
Glu
cose
-6-P
Fruc
tose
-6-P
Fruc
tose
-1:
6-bi
s-P
OH
HH
HO
HO
CH
2C
CC
CC
O
OH
OH
HO
H
HH
O
HO
CH
2C
CC
CO
CO
OH
H
H OH
H
CCO
H
CO
P-R
ibos
ylam
ine
Gly
cera
te2,
3-D
ipho
spho
-gl
ycer
ate3-P-
Gly
cera
ldeh
yde
1:3-
bis-P-
Gly
cera
te
3-P-
Gly
cera
te
2-P-
Gly
cera
te
P-en
olpy
ruva
te
Inos
itol
CH
OH
2
CH
OH
2
HO
CH
CH
OH
2
CH
O 2
HO
CH
P
Gly
cero
l
UD
P-G
alac
tose
UD
P-Su
gars
CH
CH
OH
32
ETH
AN
OL
Dih
ydro
xy-
acet
one-P
(Gly
cero
ne-P
)
Glu
cosa
min
e-6-P
Phos
pho-
serin
e
Cha
in e
long
atio
nM
itoch
ondr
ial
Ser
ine
Ser
ine
Indo
le-3
-gly
cero
l-P
3-D
eoxy
-D-a
rabi
no-
hept
ulos
onat
e-7-P
Indo
leac
etat
e(A
uxin
)In
doxy
l Form
ylky
nure
nine
Kynu
reni
ne3-
Hyd
roxy
kynu
reni
ne3-
Hyd
roxy
anth
rani
late
2-A
min
o-3-
carb
oxy
muc
onat
e se
mia
ldeh
yde
NH
OH
Tryp
tam
ine
1-(o
-Car
boxy
phe
nyla
min
o)1-
deox
yrib
ulos
e-5-P
N-(5
-P-R
ibos
yl)
anth
rani
late
Ant
hran
ilate
Cat
echo
l
NH
Indo
le-
acet
alde
hyde
NH
CH
CH
O2
Indo
lepy
ruva
te
NHC
-CH
(OH
)CH
(OH
)CH
O 2P
CH
2-A
min
omuc
onat
e-6-
sem
iald
ehyd
e
CH
CH
NH
22
2
NH
1.2.
3.7
4.1.
1.43
3.5.
1.9
3.7.
1.3
4.2.
1.20
1.13
.11.
64.
1.1.
45
2.4.
2.18
4.6.
1.4
4.1.
1.48
1.14
.13.
9
4.6.
1.3
Deh
ydro
-qu
inat
e4.2.
1.10
1.1.
1.25
2.5.
1.19
Shik
imat
e-3-P
Shik
imat
e-5
enol
pyru
vate
3-P
Cho
rism
ate
PEP
2.7.
1.71
1.4.1.
19
Hom
ogen
tisat
ePh
enyl
pyru
vate
Cin
nam
ate
Cou
mar
ate
Prep
hena
te
2-A
min
om
ucon
ate
Fum
arat
eA
spar
tate
GLY
CIN
E
Sarc
osin
e
Hyd
roxy
-py
ruva
te
P-H
ydro
xy-
pyru
vateSE
RIN
E
Imid
azol
egl
ycer
ol-P
P-R
ibos
yl-A
TPP-
Rib
osyl
form
imin
o5-
amin
oim
idaz
ole-
carb
oxam
ide-
RP
Form
imin
ogl
utam
ate
Imid
azol
one
prop
iona
teU
roca
nate
Cys
tath
ioni
neH
omoc
yste
ine
Phos
phoa
deny
lyl-
sulp
hate
(PA
PS)
CH
(NH
)CO
OH
23
+
His
tidin
ol-P
His
tidin
olH
istid
inal
3.1.
3.15
2.6.
1.9
1.1.
1.23
3.6.
1.31
5.3.
1.16
2.4.
2.17
Asp
arag
ine
ALA
NIN
E
3-Su
lphi
nyl
pyru
vate
Oxo
buty
rate
2-A
ceto
-2-
hydr
oxy-
buty
rate
O-P
hosp
ho-
hom
oser
ineH
OS
CH
CH
NH
22
22
Hyp
otau
rine
HO
SC
HC
HN
H3
22
2
Taur
ine
Glu
tam
ate
γ-G
luta
myl
cyst
eine
Glu
tath
ione
Gly
cine
Cys
tein
e
ß-A
lani
ne
Cys
teat
eS-
Ade
nosy
lho
moc
yste
ine
4.2.
99.2
1.1.
1.86
4.2.
1.9
1.1.
1.86
4.2.
1.9
2.6.
1.32
4.1.
3.18
S-A
deno
syl
met
hion
ine
(SA
M)
2-M
ethy
lace
to-
acet
yl-C
oA
2-A
ceto
lact
ate
2-3-
Dih
ydro
xyis
oval
erat
e2-
Oxo
-is
oval
erat
e
3-H
ydro
xy-
isob
utyr
ate
3-H
ydro
xy-
Isob
utyr
yl-C
oAM
ethy
lac
ryly
l-CoA
2-M
ethy
l-3-
hydr
oxy-
buty
ryl-C
oA
Tigl
yl-C
oA2
Met
hylb
utyr
yl-
CoA
2:3-
Di-O
H-
3-m
ethy
lval
erat
e2-
Oxo
-3-m
ethy
lva
lera
te
Isob
utyr
yl-C
oA
Cys
tein
esu
lphi
nate
4.2.
99.9
2-Is
opro
pyl-
mal
ate
CH
CH
CO
CO
O3
2
+C
HC
H(N
H)C
OO
33
CH
CH
(OH
)CO
O3
HO
SC
HC
OC
OO
22
OC
HC
OC
OO
2P
OC
HC
H(N
H)C
OO
23
P
HO
CH
CO
CO
O2
HO
CH
CH
(NH
)CO
O2
3+
+
OH
CH
CO
CO
O2
CO
O OH
OH
O
CO
O OH
OH
HO
P
CO
O
OH
OH
O
CH
2
P
CO
O
O-C
-CO
OO
HO
OH
OO
CC
HC
OC
OO
2
NH
HO
C-C
H(O
H)C
H(O
H)C
H2O
PC
H
CO
O
NH
2
CO
O
OH
NH
2C
OO
CO
O
OC
H
OO
CC
HN
HC
H2
3
CH
(CH
)C
OS
-AC
P3
214
CH
(CH
)C
OS
CoA
32
14
CH
(CH
)C
H=C
HC
O-S
-AC
P3
22
CH
CH
=CH
CO
-S-A
CP
3C
HC
H(O
H)C
HC
OS
-AC
P3
2
CO
SC
oA
Lino
leat
e
Ole
oyl-C
oA
Stea
royl
-CoA
Deh
ydro
stea
royl
-CoA
OH
-Ste
aroy
l-CoA
Oxo
stea
royl
-CoA
Palm
itoyl
-AC
PPa
lmito
yl-C
oA
ACYL
-AC
P2,
3-E
noyl
-AC
P
3, 4
-Dec
enoy
l-AC
P
2, 3
-Dec
enoy
l-AC
P
3-O
H-A
cyl-A
CP
3-O
xoac
yl-A
CP
3-O
xo-D
ecan
oyl-A
CP
3-O
xo-H
exan
oyl-A
CP
3-O
H-H
exan
oyl-A
CP
2, 3
-Hex
enoy
l-AC
P
But
anoy
l-AC
PC
roto
noyl
-AC
P3-
OH
-But
anoy
l-AC
PA
ceto
acet
yl-A
CP
Hex
anoy
l-AC
P
3-O
H-D
ecan
oyl-A
CP
Dec
anoy
l-AC
P
Palm
itole
oyl-A
CP
γ-Li
nole
nate
Ara
chid
onat
eLe
ukot
riene
B4
CO
SC
oA
CO
-S-A
CP
Thro
mbo
xane
B2
HO
OC
CH
CO
-S-A
CP
2M
alon
yl-A
CP
HO
OC
CH
CO
-SC
oA2
Mal
onyl
-Co-
A
CH
CO
-S-A
CP
3
Ace
tyl-A
CP
CH
O-C
O-R
2
CH
OH
2
R’-C
O-O
CH
FATT
Y AC
IDAC
YL-C
oA(C
ytos
ol)
CH
O-C
O-R
2
CH
O 2
R’-C
O-O
CH
P
Car
diol
ipin
Phos
phat
idyl
glyc
erol
Ace
tylc
holin
eG
lyce
roph
osph
ocho
line
Lyso
leci
thin
Cho
line
plas
mal
ogen
CD
P-ch
olin
eC
holin
e-P
Mev
alda
te
CH
(CH
)C
H=C
HC
H(O
H)C
HC
HO
H3
212
2
Deh
ydro
sphi
ngan
inSp
hing
anin
4-Sp
hing
enin
Psyc
hosi
ne
Acy
l-CoA
Acy
l-CoA
Cer
ebro
side
Gal
acto
seC
H(C
H)
CH
=CH
CH
(OH
)CH
CH
O-
32
122
NH
CO
R
Isop
ente
nyl-PP
(C5)
Dim
ethy
lally
l-PP
(C5)
Ger
anyl
-ger
anyl
-PP
(C20
)
Farn
esyl
-PP
(C15
)
Squa
lene
(C30
)
Ger
anyl
-PP
(C10
)
Des
mos
tero
lZy
mos
tero
lLa
nost
erol
CH
C =
CH
CH
O3
2P
P
CH
3
Cer
amid
e
Gan
glio
side
sN
HC
OR
CH
O 2P
P
OP
PC
H2
CH
OLE
STER
OL
CH
C(O
H)C
HC
HO
H3
22
CH
CO
O2
CH
C(O
H)C
HC
HO
32
CH
CO
O2
NA
DP
+D
ehyd
roas
corb
ate
OH
HO
HO
CH
2C
CC
CC
O
OH
HO
H
OH
HO
HO
CH
2C
CC
OC
OC
O
H
NA
D+
Pi
AD
PA
DP
Phyt
oene
(C40
)Ly
cope
ne(C
40)
ß-C
AR
OTE
NE
(C40
)R
hodo
psin
Met
arho
dops
in
Ret
inoa
te
trans-
Ret
inal
11-cis
-Ret
inol
trans-
Ret
inol
(Vita
min
A)
Ret
inol
est
ers
Dar
k
Ligh
t
Ubi
quin
one
(Coe
nzym
e Q
)
Men
aqui
none
Plas
toqu
inon
e
Phyl
loqu
inon
e(V
itam
in K
)
Ops
inC
HO
CH
OH
2
CH
O
CH
OH
2
CH
3C
HO 3
CH
O 3n
O O
OO
Phyt
ol(C
20)
α-To
coph
erol
(Vita
min
E)
Qui
nolin
ate
Qui
nolin
ate-
nucl
eotid
eN
icot
inat
e-nu
cleo
tide
Des
amin
o-N
AD
5-H
ydro
xy-
tryp
toph
an5-
Hyd
roxy
tryp
tam
ine
(SER
OTO
NIN
)N-
Acet
yl-5
-O-m
ethy
l-ser
oton
in(M
ELAT
ON
IN)
NH
CH
CH
NH
CO
CH
22
3H
O
NH
CH
CH
NH
CO
CH
22
3C
HO 3
+N
AD
(P)
NIC
OTI
NAT
E
N-A
cety
l-ser
oton
in
2.4.
2.19
Dop
amin
eD
opa
Dop
aqui
none
THYR
OXI
NE
MEL
AN
IN
OH
OH
CH
OH
CH
NH
CH
23
OH
OH
CH
OH
CH
NH
22
4-O
H-3
-Met
hoxy
-ph
enyl
glyc
ol
CH
OH
CH
NH
22
OH
OC
H3
OC
H3
CH
OH
CH
OH
2
OH
OC
H3
4-O
H-3
-Met
hoxy
-D
-man
dela
te
Cyc
lic A
MP
ATP
Dep
hosp
ho-C
oenz
yme
A
4-P-
Pant
ethe
ine
4-P-
Pant
othe
nylc
yste
ine
4-P-
Pant
othe
nate
Pant
oate
6.3.
2.1
1.1.
1.16
9
3.5.
1.22
2.7.
1.33
NH
NH
O O
O O
CH
OH
2
OH
OC
H3
CH
(OH
)CO
O
H2 NH
3+
CH
-CO
OC
O O
CO
O
NR
ibos
e-P
N+
CO
O
NH
CH
CO
O2
O
OH
CH
O 2P
NH
CO
CH
NH
22
OH
Form
ylgl
ycin
amid
e-RP
Ure
a
Form
ylgl
ycin
amid
ine-
RP
Alla
ntoa
teA
llant
oin
UR
ATE
AD
P
Xant
hine
Hyp
oxan
thin
e
Inos
ine
Ade
nine
Ade
nylo
-su
ccin
ate
5-A
min
oim
idaz
ole-
RP
5-A
min
o-4-
imid
azol
eca
rbox
ylat
e-RP
5-A
min
o-4-
imid
azol
e(N
-suc
ciny
lcar
boxa
mid
e)-RP
5-A
min
oim
idaz
ole
carb
oxam
ide-
RP Fo
rmyl
amid
o-im
idaz
ole-
carb
oxam
ide-
RP
HN
CO
NH
22
HNH
C 2C
HO
NH
RP
NH
C
CCO
CC
OO
CN
H
NH
HN
HN
H
CCO
CC
HO
CN
H
N
N
HN
Car
bam
oyl
ß-al
anin
eD
ihyd
ro-
urac
ilU
raci
l
d-A
DP
d-AT
P
GTP
GD
P
XAN
THO
SIN
E-P
(XM
P)
TTP
TDP
ß-U
reid
ois
obut
yrat
eD
ihyd
roth
ymin
eTh
ymin
ed-
UM
Pd-
CM
Pd-
CD
P
CD
P
Car
bam
oyl
aspa
rtat
eD
ihyd
roor
otat
eO
rota
teO
rotid
ine-P
Urid
ine-P
(UM
P)U
DP
3-A
min
o-is
obut
yrat
eC
HCNH
2 CH
OC
NH
NC
HCO
CH
OC
NH
HN
CH
-CH
3CO
OC
NH
HN
CH
2
CH
2C
H2
CO
OC
NH
HNCO
CH
OC
NH
HN
CC
H3
Met
hylm
alon
ylse
mia
ldeh
yde
OH
CC
HC
OO
CH
3
CH
2CO
CH
-CO
OO
CN
H
HN
CH
CO
C-C
OO
OC
NH
HN
HN
CO
NH
CH
CH
CO
O2
22
CC
CC
H RP
HC
NH
NH
OO
C-C
H-C
HC
OO
2 N
N
N
CH
O
NH
RP
NH
OC
HC 2
2.7.
7.43
3.1.
3.29
1.1.
1.15
8
5.1.
3.13
2.7.
1.38
3.2.
1.23
3.1.
3.29
4.1.
3.20
2.7.
1.60
5.1.
3.14
5.1.
3.7
5.1.
3.1
2.7.
1.4
5.4.
2.3
3.1.
1.17
1.1.
1.49
1.1.
1.21
2.7.
7.23
3.1.
3.25
1.13
.99.
11.
1.1.
19
1.1.
3.8
5.3.
1.3
2.7.
1.53
1.1.
1.9
2.7.
1.15
2.7.
1.17
5.1.
3.4
5.1.
3.1
2.2.
1.2
4.1.
2.13
2.7.
1.11
2.7.
1.47
2.2.
1.1
1.2.
1.12
1.1.
1.29
1.1.
1.95
1.3.
1.35
1.14
.99.
25
2.3.
1.41
2.3.
1.41
2.3.
1.41
1.1.
1.10
0
5.3.
99.5
4.2.
1.60
5.3.
99.3
1.14
.99.
11.13
.11.
34
1.3.
1.10
1.3.
1.9
1.14
.99.
5
1.3.
1.9
4.2.
1.61
4.2.
1.60
4.2.
1.60
4.2.
1.59
4.2.
1.58
1.3.
1.9
1.3.
1.9
6.2.
1.3
3.1.
2.20
1.1.
1.10
0
5.3.
1.1
HO
OC
-CO
OH
Oxa
late
Gly
cola
te
HO
CH
CH
O2
Gly
col
alde
hyde
Etha
nola
min
e-P2.
7.1.
30
2.3.
1.7
3.7.
1.2
4.1.
3.5
2.7.
8.8
2.1.
1.17
2.1.
1.71
1.3.
1.35
2.7.
8.2
3.1.
4.3
3.1.
4.4
2.7.
7.15
3.1.
1.5
3.1.
4.2
2.7.
1.32
2.7.
1.82
1.2.
4.1
2.3.
1.12
1.8.
1.4
2.6.
1.2
1.4.
1.1
4.1.
1.1
2.3.
1.50
1.1.
1.10
2
3.1.
4.12
2.7.
8.3
2.4.
1.62
3.2.
1.46
5.2.
1.3
1.2.
1.36
2.3.
1.76
3.1.
1.21
5.2.
1.7
5.4.
99.7
1.14
.99.
7
4.3.
1.8
4.2.
1.75
4.1.
1.37
1.3.
3.3
1.3.
3.4
4.99
.1.1
2.5.
1.29
2.4.
1.47
4.1.
1.28
2.3.
1.5
2.1.
1.4
6.3.
5.1
6.3.
1.5
2.4.
2.11
2.7.
7.18
2.6.
1.5
1.2.
1.32
1.13
.11.
5
2.1.
1.28
2.1.
2.2
6.3.
3.1
3.5.
2.5
1.4.
1.10
1.7.
3.3
1.1.
1.20
41.
1.3.
221.
1.3.
22
4.1.
1.28
4.1.
1.21
2.1.
2.3
2.4.
2.1
1.5.
99.2
2.1.
1.5
2.6.
1.22
3.5.
2.3
2.6.
1.51
1.4.
1.7
3.1.
3.3
2.6.
1.52
2.1.
3.2
ACET
ATE
2.4.
2.4
2.1.
1.45
RP
CH
CO
CH
OC
N
HN
1.3.
1.14
2.4.
2.10
4.1.
1.23
2.7.
7.7
2.7.
7.7
2.7.
7.7
1.17
.4.1
2.7.
7.7
2.7.
4.14
4.4.
1.1
1.6.
4.1 1.
13.1
1.20
4.4.
1.8
4.2.
1.22
1.1.
1.27
4.1.
1.29
6.3.
2.3
6.3.
2.2
1.8.
1.3
LAC
TATE
Ace
tald
ehyd
e
2.7.
1.24
2.7.
7.3
4.1.
1.36
Bile
Aci
ds
CH
CH
CO
SC
oA3
2Pr
opan
oyl-C
oA
1.1.
1.31
2.1.
3.1
4.1.
1.41
5.1.
99.1
6.4.
1.3
6.3.
2.5
2.1.
1.14
2.1.
1.13
4.6.
1.1
CD
P-Et
hano
lam
ine
1.1.
1.35
4.2.
1.17
+H
OS
CH
CH
(NH
)CO
O2
23
3.5.
2.7
NH
HN
CH
OO
CC
HC
HC
HC
OO
22
CM
P-N
-Ace
tyl
neur
amin
ate
CD
P-di
acyl
glyc
erol
CH
OLI
NE
Etha
nola
min
e
Gly
oxyl
ate
HIS
TAM
INE
2.3.
1.46
Hom
oser
ine
Tyra
min
e
Plan
t Pig
men
tsTa
nnin
s
Mal
eyl
acet
oace
tate
Fum
aryl
acet
oace
tate
5.2.
1.2
CH
CO
O2
OH
OH
OHCH
CH
NH
22
2
OH
OH
CH
CH
NH
22
2Hyd
roxy
phen
ylpy
ruva
te
α-To
coph
erol
(Vita
min
E)
LIG
NIN
d-G
TP
OH
OH
OH O
HO
OH
P
OP
PT
CH
3H
O
OH
OH
O
NA
DPH
2.2.
1.1
2.7.
1.3
1.1.
1.45
1.1.
1.13
0
1.10
.3.3
1.10
.2.1
1.1.
1.10
ATP
CH
CH
NH
22
2
NH
HO
5.4.
99.5
1.14
.16.
12.
6.1.
51.
13.1
1.27
Indo
le
4.1.
99.1
1.13
.11.
11
OH O
OH
NH
CC
CH
CH
O 2P
HH
CO
O
NH
2
CO
O
6.3.
5.3
6.3.
2.6
4.3.
2.2 G
uani
neD
NA
6.3.
4.4
4.3.
2.2
CCO
CC
HH
CN
H
N
N
HN
CCO
CC
HH
CN
H
N
N
HN
3.5.
3.4
2.4.
2.1
2.7.
7.6
2.7.
7.6
2.7.
7.6
2.7.
7.6
2.7.
4.6
2.7.
4.3
2.7.
4.4
2.7.
4.6
2.4.
2.15
1.1.
1.20
5
6.3.
4.1
6.3.
5.2
2.7.
4.4
3.5.
4.3
3.2.
2.2
2.4.
2.1
3.1.
3.5
3.1.
4.6
6.3.
4.2
1.17
.4.1
1.17
.4.1
3.5.
4.12
2.7.
4.8
2.7.
4.9
2.7.
4.6 2.4.
2.4
1.3.
1.2
3.5.
2.2
3.5.
1.6
3.5.
1.6
3.5.
2.2
3.5.
4.1
Dip
hosp
ho-
mev
alon
ate
Mev
alon
ate
3-O
xope
ntan
oyl-C
oA
3-O
xoac
yl-C
oA3-
OH
-Acy
l-CoA
2, 3
-Eno
yl-C
oA
2, 3
-Hex
enoy
l-CoA
3-O
H-H
exan
oyl-C
oA
Ace
toac
etyl
-CoA
3-O
H-B
utan
oyl-C
oAC
roto
noyl
-CoA
Pent
anoy
l-CoA
3-O
H-P
enta
noyl
-CoA
1.1.
1.35
1.1.
1.35
1.1.
1.15
7
1.3.
99.3
1.3.
99.3
1.3.
99.2
1.1.
1.35
Odd
C F
atty
aci
ds
Succ
inyl
hom
oser
ine
CO
2
2-O
XO A
CID
Glu
tam
yl-P
Glu
tam
ine
UR
EA
P-C
reat
ine
Cre
atin
eC
reat
inin
e
Gly
cine
CIT
RU
LLIN
E
Glu
tam
icse
mia
ldeh
yde
2-A
MIN
O A
CID
Pyrr
olin
e-5-
carb
oxyl
ate
Gly
oxyl
ate
Pyru
vate
4-H
ydro
xy-
2-ox
oglu
tara
te
4-H
ydro
xy-
glut
amat
e
3-H
ydro
xy-
pyrr
olin
e-5-
carb
oxyl
ate
Putr
esci
neH
NC
HC
HC
HC
HN
H2
22
22
2
Sper
mid
ine
Sper
min
e
N -T
rimet
hylly
sine
66
N -T
rimet
hyl-
3-O
H-ly
sine
Car
nitin
e
Glu
tary
l-CoA
Sacc
haro
pine
2-A
min
oadi
pate
sem
iald
ehyd
e2-
Amin
oadi
pate
2-O
xoad
ipat
e
Arg
inin
o-su
ccin
ate
Gua
nido
acet
ate
Met
hylm
alon
yl-C
oA
4.1.
2.12
Asp
arty
lSe
mia
ldeh
yde
2, 3
-Dih
ydro
-di
pico
linat
e
1.2.
1.11
4.2.
1.52
1.3.
1.26
Pipe
ridei
ne-
2, 6
-dic
arbo
xyla
teN
-Suc
ciny
l-2-
amin
o-6-
oxo-
pim
elat
e
2.6.
1.17
N-S
ucci
nyl-2
, 6di
amin
opim
elat
eD
iam
ino-
pim
elat
e3.
5.1.
18
3-M
ethy
l-gl
utac
onyl
-CoA
(CH
)C
HC
HC
OS
CoA
32
2(C
H)
CH
CH
CO
SC
oA3
22
3-M
ethy
l-cr
oton
yl-C
oAIs
oval
eryl
-CoA
Oxo
pant
oate
HC
HO
OO
CC
HC
= C
HC
OS
CoA
2CH
3
CH
CO
CH
CO
SC
oA3
CH
3C
HC
H=C
HC
OS
CoA
3
CH
3C
HC
H(O
H)C
HC
OS
CoA
3
CH
3
C(O
H)C
H(O
H)C
OO
CH
CH
32
CH
3
CH
= C
CO
SC
oA2
CH
3H
OC
HC
HC
OS
-CoA
-2C
H3
CH
CH
CO
-SC
oA3
CH
3
C (O
H)C
H(O
H)C
OO
CH
3
CH
3
CH
CH
CH
CO
SC
oA3
2CH
3
CH
C =
CH
CO
SC
oA3C
H3
ATP
4-A
min
obut
yrat
e(G
ABA
)
1.3.
99.7
1.5.
1.2
1.14
.11.
2
2.6.
1.39
1.2.
1.31
1.14
.11.
8
2.5.
1.16
2.5.
1.22
4.1.
3.16
2.6.
1.23
1.5.
99.8
1.5.
1.2
6.4.
1.4
1.3.
99.1
0
4.2.
1.33
2.6.
1.6
1.1.
1.85
Oxo
leuc
ine
CO
OH
(CH
)C
HC
HC
H(O
H)C
OO
32
S-A
deno
sylm
ethy
lth
iopr
opyl
amin
e(D
ecar
boxy
late
d SA
M)
PRO
LIN
E
Coe
nzym
e A
CH
C=
CH
CH
32
CH
3
OC
H
CH
3
3H
OC
H3
CH
3
CH
3
CH
C-C
HH
O3
22
CP
P
CH
2
CH
C=
CH
CH
O2
2P
P
CH
3
3-P-
Gly
cero
l
Phos
phat
idyl
etha
nola
min
eC
EPH
ALI
N
3.1.
4.12
2.7.
8.3
Prog
este
rone
1.5.
1.12
2.7.
3.2
4.2.
1.17
3.1.
2.4
2.6.
1.32
4.4.
1.15
Ace
tyls
erin
e2.
7.7.
42.
7.1.
251.
8.99
.1A
deny
lyls
ulph
ate
(APS
)
2.7.
1.39
4.4.
1.15
4.1.
1.29
4.2.
99.8
2.3.
1.30
P-R
ibos
yl-PP
1.1.
1.1
1.2.
1.4
Asp
arty
l-P
5.1.
1.7
2.7.
1.40
4.1.
3.18
4.1.
3.18
1.5.
1.9
1.14
.11.
1
CH
OLI
NE
2.1.
1.13
1.3.
1.2
NH
CH
CH
SH
22
N
HC
HC
HC
O2
2O
CH
C(C
H)
CH
(OH
)CO
23
2P
AD
P-
NH
CH
CH
SH
22
N
HC
HC
HC
O2
2O
CH
C(C
H)
CH
(OH
)CO
23
2
P-A
DP
-N
HC
HC
HS
H2
2
NH
CH
CH
CO
22
OC
H C
(CH
)C
H(O
H)C
O2
32
1.4.
1.8
1.3.
99.3
1.3.
99.3 1.
4.1.
9
4.2.
1.18
4.1.
1.20
1.3.
99.7
1.8.
99.2
+C
HC
O-O
CH
CH
(NH
)CO
O2
23
2.5.
1.6
2.1.
1.10
2.1.
1.20
1.1.
1.3
1.1.
1.3
4.2.
1.18
4.1.
2.5
4.3.
1.5
4.2.
1.20
2.1.
2.1
2.1.1.
20
Gly
oxyl
ate
2.1.
1.6
1.4.3.
41.
14.1
8.11.14
.16.
2
Hex
anoy
l-CoA
But
anoy
l-CoA
6.3.
4.16
6.3.
5.5
2.7.
2.11
2.1.
3.3
NO
1.14
.13.
39
3.5.
3.6
3.5.
3.1
4.3.
2.1
4.1.
1.17
2.7.
7.41
2.6.
1.4
1.1.
1.10
0
1.1.
1.8
2.3.
1.51
2.3.
1.15
2.7.
8.5
SO- 42
1.14
.16.
4
NH
2 O
OC
O
OC
4.1.
1.25
1.3.
1.13
1.3.
1.13
2.7.
4.6
CYT
IDIN
E-tr
ipho
spha
te(C
TP)
Cyt
osin
e
2.4.
2.9
4.1.
1.11
2.6.
1.18
4.3.
1.3
4.2.
1.49
3H
SO-
1.1.
1.10
5
2.3.
1.41N
AD
PH
1.1.
1.22
2.3.
1.4
5.5.
1.4
3.2.
1.26
3.2.
1.48 2.
6.1.
16
1.1.
1.14
2.7.
7.34
4.2.
1.47
2.4.
1.68
2.4.
1.69
2.4.
1.9
5.3.
1.8
2.4.
1.11
O
OP
PU
CH
OH
2
CH
OH
2
HO
OHO
H HO
2.4.
1.21
4.2.1.
521.
2.1.
18
4.2.
1.18
O
CH
C
CH
OC
N
HN
DP CH
CO
CH
OC
N
HN
RP
PP
OC
H2
H CCH O
HO
H
CH
NH
NC H
CP
H
O
OC
H2
CCH O
H
H OH
C
H CC
CNH
2 CC
HH
CN
RP
(PP
)
N
N
N+P
NH
2H
O
OC
H2
CCH O
H
H OH
C
H CC
OC
CC
HH
CN
RP
N
N
NH
P
H
OC
H2
CCH O
HO
H
CO
CH
2C
CO
NH
2 CC
HH
CN
RP
N
N
NH
P
+O
OC
CH
N(C
H)
23
3B
etai
ne
Bet
aine
alde
hyde
2.4.
1.16
5.1.
3.6
2.4.
1.33
2.7.
7.13
5.4.
2.8
5.3.
1.8
O
OH
CH
OH
2 HO
OP
HO
2.7.
1.28
2.7.
1.31
6.3.
4.13
5.3.
1.1
2.2.
1.1
4.1.
1.9
3.1.
2.11
ß-O
H-ß
-Met
hyl-
glut
aryl
-CoA
6.3.
4.5
5.3.
1.6
2.5.
1.21
2.1.
1.2
3.5.
2.10
6.3.
2.13
6.3.
2.7-
10
2.7.
7.27
2.7.
7.9
3.5.
4.10
CCO
CC
HO
CN
RP
N
NH
HN
CCO
CC
H
NN
N
HN
RP
HN 2
C
2.7.
4.6
1.17
.4.1
2.7.
4.6
2.6.
1.13
Car
bam
oyl-P
2.3.
1.9
Car
nitin
e
2.6.
1.4
2.6.
1.44
CH
C(O
H)C
HC
OS
CoA
32
CH
CO
O2
1.2.
3.5
1.1.
1.34
2.3.
1.16
4.1.
3.5
2.3.
1.16
4.1.
3.4
Men
aqui
none
4.1.1.
15
2.6.
1.19
4.2.
1.16
Car
nosi
ne
CH
CH
NH
22
2C N
HN
C
HC
H
4.1.
1.22
4.3.
1.3
Ubi
quin
one
Plas
toqu
inon
e
D-R
ibos
e-5-P
NH
CH
CH
(NH
)CO
O2
3H
O+
O
OH
OH
HO
OP
PU
CO
O-
O
OH
OH
HO
OP
PU
CO
O-
OH
HO
H
HO
CH
2C
CC
O
H
CO
CO
O-
OC
HO
HC
HO
HA
cNH
HO
OP
COC
O-
CH
OH
2
OC
HO
HC
HO
HA
cNH
HO
OHCO
OC
HO
H2
O
OH
OH
HO
HO
CH
O 2P
O
OHAC
NH
HO
OH
CH
O 2P
O
OO
HH
OH
OP
CH
OH
2
O
OH
OH
HO
HO
CH
OH
2
O
OH
HO
OH
3
CH
O 2P
O
OH
HO
O
NH
CO
CH
3
P
CH
OH
2C
HO
H2
CH
OH
2
O
OH
HO
OH
NH
2
CH
O 2P
O
OH
HO
OHO
PP
U
CH
OH
2
O
O
HO
OH
OH
HO
P
CH
OH
2
CH
OH
2O
OH
O
OH
OH
O
OH
OH
OH
CH
OH
2
O
OH
HO
OHO
H
CH
2C
HO
P2
OH
HH
HO
H
CC
CC
OH
OH
H
CO
O-
HO
CH
2
H OH
OH
OH
CC
CC
HO
HH
HO
CH
2
H OH
OH
H
CC
CC
HO
HO
H
HO
CH
2
OH
HO
HH
CC
CC
HO
HO
H
HO
CH
2
H OH
HO
H
CC
CC
HO
OH
H
HO
CH
2
OH
HH
OH
CC
CC
HO
OH
H
HO
CH
2
OH
HO
HO
H
CC
CC
HO
HH
HO
CH
2
H OH
HO
H
CC
CC
OH
HH O
HCO
O-
PO
CH
2
OH
HO
H
CC
CO
H
PO
CH
2C
HO
H2
H OH
H
CC
CO
OH
HO
CH
2C
HO
H2
CH
OH
2P
OC
H2
H OH
OH
CC
CO
H
CH
OH
2P
OC
H2
OH
HH
CC
CO
OH
CH
OH
2P
OC
H2
H OH
OH
CC
CO
H
HO
CH
2C
HO
H2
OH
HO
H
CC
CO
H
HO
CH
2C
HO
H2
OH
HH
CC
CO
OH
HO
CH
2C
HO
H2
H OH
OH
H
CC
CHO
H
HO
CH
2C
HO
H2
OH
HO
HO
H
CC
CHH
HO
CH
2C
HO
H2
H OH
HO
H
CC
CC
OH
HH O
HCH
OH
2H
OC
H2
H OH
OH
CC
CH
OH
POC
H2
H OH
HO
H
CC
CC
O
OH
H
HO
CH
2C
HO 2
P
H OH
OH
OH
CC
CHH
HO
CH
2C
HO
H2
H OH
OH
CC
C
H
CO
HHO
PO
CH
2C
HO
H2
P
H OH
OH
CC
C
H
CO
HHO
CH
O 2P
OC
H2
H OH
OH
CCH
CC
HO
OH
H
POC
H2
POC
H2
O
OH
NH
2
OH
CH
O 2P
C
HO
HC
HO
POC
H2
HO
CH
2CO
CH
2OP
O
OH
OO
PP
OH
CH
O 2P
CH
OH
CO
OP
POC
H2
C
HO
HP
OC
H 2C
OO
CO
O
OH
OH
OO
H
CO
O
CH
(CH
)C
H(O
H)C
HC
OS
-CoA
32
142
CH
(CH
)C
H(O
H)C
HC
OS
32
142
CH
(CH
)C
OC
HC
OS
-CoA
32
142
CH
(CH
)C
OC
HC
OS
-CoA
32
142
CH
(CH
)C
OS
-CoA
32
n+2
CH
(CH
)C
H=C
HC
OS
-CoA
32
14
CH
(CH
)3
2nC
H=C
HC
OS
-CoA
CH
(CH
)3
25
2C
H=C
HC
HC
OS
ACP
CH
(CH
)3
26C
H=C
HC
OS
ACP
CH
(CH
)3
26C
OC
HC
OS
ACP
2C
H(C
H)
32
62
2C
HC
HC
OS
ACP
CH
(CH
)3
22
22
CH
CH
CO
SAC
P
CH
CH
CH
CO
SAC
P3
22
CH
(CH
)3
26C
H(O
H)C
HC
OS
ACP
2
CH
CH
=CH
CO
.S-A
CP
3
CH
(CH
)3
22
2C
OC
HC
OS
ACP
CH
3CO
CH
CO
SAC
P2
CH
(CH
)3
2n
2C
OC
HC
OS
ACP
CH
(CH
)3
2n
2C
H(O
H)C
HC
OS
ACP
CH
(CH
)3
22
2C
H(O
H)C
HC
OS
ACP
AC
YL-
CoA
(Mito
chon
dria
)
CH
(CH
)C
HC
HC
OS
CoA
32
22
n
CH
(CH
)C
H=C
HC
OS
CoA
32
nC
H(C
HC
H(O
H)C
HC
OS
CoA
32
n
CH
(CH
)C
HC
HC
OS
CoA
32
22
2C
H(C
H)
CH
=CH
CO
SC
oA3
22
CH
(CH
)C
OC
HC
OS
CoA
32
2n
CH
CO
CH
CO
SC
oA3
2
CH
(CH
)C
H(O
H)C
HC
OS
CoA
32
22
CH
CH
(OH
)CH
CO
SC
oA3
2C
HC
H=C
HC
OS
CoA
3C
HC
HC
HC
OS
CoA
32
2
CH
CH
CH
CH
CO
SC
oA3
22
2Pe
nten
oyl-C
oAC
HC
HC
H=C
HC
OS
CoA
32
CH
CH
CH
(OH
)CH
CO
SC
oA3
22
CH
(CH
)C
OC
HC
OS
CoA
32
22
CH
CH
CO
CH
CO
SC
oA3
22
OH
OH
HO
OH
O O-
CH
O-P
O2
CH
CH
OH
CH
OH
22
O
CH
2
CH
2
R'-C
O-O
CH
O-C
O-R
O-P
OO-
HO
CH
CH
22N
H3
+P
OC
HC
H2
2NH
3+
CP
P-O
CH
CH
22N
H3
+
O
-
CH
O-C
O-R
2
CH
O P
2O
CH
CH
22N
H3
+
CH
CO
CH
CH
N(C
H)
32
23
3
HO
CH
CH
N(C
H)
22
33
+
CH
CH
2C
OO
(NH
) 3+
OH
OH
CH
CH
2C
OO
-(N
H) 3
+
CO
NH
2CH
CH
(NH
)CO
O2
3+
NH
OC
CO
NH
OC
N H
C H
HN 2
HC
CH
NN
CR
PH
N 2
CH
C
CH
OC
N
N
DP
NH
2
RP
PP
CH
C
CH
OC
N
N
NH
2
CC
CC
H RP
(P)
HC
NN
N
NN
H2
HN
CO
O2
P
(CH
)N
H2
32
HN
(CH
)N
H2
23
(CH
)N
H2
4 (CH
)N
H2
32
HN
(CH
)N
H2
24
CH
-SC
HC
HC
HN
H3
22
2
Ade
nosy
l
+
+C
H3
CH
3CH
CH
(NH
)CO
O3
++C N
HN
C
HC
H
CH
CH
(NH
)CH
OH
23
2+
C NH
NC
HC
H
CH
CH
(NH
)CH
OP
23
2C N
HN
C H
HC
CH
CO
CH
OP
22
+H
SC
HC
HC
H(N
H)C
OO
22
3
+
+S
CH
CH
CH
(NH
)CO
O2
23
CH
CH
(NH
)CO
O2
3
RP
CO
C-C
OO
OC
N
HN
CH
2.4.
1.23
CH
(CH
)C
H=C
HC
H(O
H)C
HC
HO
H3
212
2
NH
3+
CH
(CH
)C
H(O
H)C
HC
HO
H3
214
2
NH
3+
CH
(CH
)C
OC
HC
HO
H3
214
2
NH
3+
Gal
acto
seC
H(C
H)
CH
=CH
CH
(OH
)CH
CH
O-
32
122
NH
3+
4.1.
1.70
HN
CO
NH
22
OH
CC
HN
(CH
)2
33
+
C-C
H3
CO
CH
OC
ND
P
HN
DP
CP
P-O
CH
CH
N(C
H)
22
33
+O
CH
CH
N(C
H)
22
33
+
1.2.
1.41
UD
P-N
-Ac-
Mur
amat
e
O
OC
HC
H3 C
OO
-
NH
AC
HO
OPP
U
CH
OH
2 4.1.
3.20
O
OH
CH
3
HO
HO
OP
PG
2.7.
7.24
2.4.
1.22
2.7.
7.125.
1.3.
2
5.3.
1.4
Sedo
hept
ulos
e-PP
3.1.
1.28
4.2.
1.24
N
CH
2
CH
2
N
N N
CH
3 CH
3
CH
CH
CO
O
CH
CH
CH
2
HC 3 HC 3
HC 3H
C
CC HH Fe
CH
2C
H2
CO
O-
-
CH
3
CH
3
CH
2
CH
2CH
2
HC 3HC 3
N H NH
N H NH
CH
CH
HC 2
CCH2
H2
-
CH
2C
H2
CO
O
CH
2C
H2
CO
O-
HC 2
HC 2
CH
2
CH
2
OO
C
CO
O
HN 2
N H
-
-
CH
2
HC 2
HC 2
HC 2
H2
H2
CH
2C
H2
CH
2
CH
2
CH
2
CH
2 N H NH
N H NH
CO
O
CO
O
CO
OC
OO
CC
--
CH
2C
H2
CO
O
CH
2C
H2
CO
O-
-
--
OO
C- O
OC
-
CH
3
CH
3
HC 3
HC 3H
C 2
H2
H2
N H NH
N H NH
CH
2
CH
2
CH
2
CH
2
CH
2
CC
CO
O-
CH
2C
H2
CO
O
CH
2C
H2
CO
O-
-CO
O-
CO
O-
CH
C(O
H)C
HC
HO
32
2P
P
CH
CO
O2
OH
CC
OO
HO
CH
CO
O2
NH
2
HN
CN
HC
HC
OO
22
+N
H2
HN
CN
(CH
)CH
CO
O2
32
+N
H2
HN
CN
(CH
)CH
CO
O3
2P
-
+H
NC
NH
CO
NC
H2
CH
3
OO
CC
HC
HC
OO
2
HN
CN
HC
HC
HC
HC
H2
22
2
N(N
H) 3
+C
OO
CH
CO
OH
C
CH
2H
OC
H N
OO
CC
H(O
H)C
HC
H(N
H)C
OO
23
+
CH
CO
O
CH
2H
OC
H
HC 2
N H
NH
CH
CO
O
CH
2C
H2
CH
2
OO
CC
H(O
H)C
HC
OC
OO
2
NC
HC
OO
CH
2C
H2
CH
CH
CO
CO
O3
OH
CC
OO
+H
NC
ON
HC
HC
HC
HC
H2
22
2(N
H) 3C
OO
HN
OC
CH
CH
CH
22
2C
OO
(NH
) 3+
R-C
O-C
OO
+
CO
OR
-CH
(NH
) 3+
CO
OH
NO
CC
HC
H2
2(N
H3
+
OO
C-C
H-C
OS
CoA
CH
3
PO
OC
CH
CH
2C
OO
(NH
) 3+
OO
CC
HC
HC
HO
22
OH
CC
HC
H2
CO
O(N
H) 3
+
(CH
)N
CH
CH
(OH
)CH
CO
O3
32
2+
OH
CC
HC
HC
H2
2+
CO
O(N
H) 3
PO
OC
CH
CH
CH
22
+C
OO
(NH
) 3
OH
CC
HC
HC
HC
H2
22
CO
O(N
H) 3
+N
HC
HC
HC
HC
OO
22
CO
O
CH
CH
CH
CH
CH
22
22
CO
O(N
H) 3
+
HN
(CH
)2
42
CH
(NH
)CO
O3
CH
(NH
3++
(CH
)N
(CH
)3
32
3CH
CH
(NH
)CO
O2
3+
+
CH
2CH
OO
CC
N
HC
CH
-CO
OC
H2
CH2
CH
-CO
O O
OC
CN
HC 2
OO
CC
OC
HC
HC
HC
H-C
OO
22
2C
HC
H2
22
OO
CC
HC
HC
ON
H2
2O
OC
CH
CH
CH
CH
CH
-CO
O2
22
OO
CC
HC
HC
ON
H2
2C
H2
2
NH
3+
OO
CC
H-C
HC
HC
HC
HC
OO
22
2N
H3
+
NH
3+
(CH
)C
HC
(OH
)CH
32
2
CO
OH
CO
O(C
H)
CH
CH
CO
CO
O3
22
+(C
H)
CH
CH
32
2C
H(N
H)C
OO
3
HO
CH
CH
CO
O2C
H3
CH
CO
CO
OC
H3
CH
3C
HC
OC
(OH
)CH
33
CO
O
+P
OC
HC
HC
H(N
H)C
OO
22
3+
HO
CH
CH
CH
(NH
)CO
O2
23
+C
HC
HC
H(N
H)C
OO
22
3 O
OC
CH
CH
2CO
O2
+C
HS
H2
OO
CC
H(N
H)C
HC
HC
ON
HC
HC
ON
HC
HC
OO
32
22
HO
CH
C(C
H)
CO
CO
O2
32
HO
CH
C(C
H)
CH
(OH
)CO
O2
32
N
HC
HC
HC
OO
22
HO
CH
C(C
H)
CH
(OH
)CO
32)
23
2
N
HC
HC
HC
OO
22
OC
HC
(CH
)C
H(O
H)C
O2
32
P
CH
CH
32
CH
3 CH
+C
H(N
H)C
OO
3
CH
CO
C(O
H)C
HC
H3
23
CO
OC
HC
OC
OO
CH
CH
32
CH
3
NH
CH
CH
SH
2
CO
O
NH
CH
CH
CO
22
OC
H C
(CH
)C
H(O
H)C
O2
32
P
+C
HS
H2
OO
CC
H(N
H)C
HC
HC
ON
HC
HC
OO
32
2
+A
deno
syl
SC
HC
HC
H(N
H)C
OO
22
3
+S
CH
CH
CH
(NH
)CO
O2
23
+H
OS
CH
CH
(NH
)CO
O3
23
+ +S
-CH
CH
(NH
)CO
O2
3
S-C
HC
H(N
H)C
OO
23
+H
SC
HC
H(N
H)C
OO
23
1.1.
1.23
H
C NH
NC
HC
CH
CH
CO
O2 N
HC
OC
HC
HN
H2
22
+
H
C NH
NC
HC
CH
CH
(NH
)CO
O2
3
CH
CH
CH
CO
O2
2
NH
NC
H
OC
CC
HC
HC
OO
NH
NC
H
CH
CH
CO
O3
N H
OO
C
CH
-CO
OO
CNH
2C
H2
HN
CH
CH
CO
O2
22
HN
CH
22C
H3
CH
CO
OH
NC
ON
HC
HC
HC
OO
22
CH
3
CCO
CH RP
HC
NN
N
HN
CCCO
CH
HC
ONN
NR
P
CC
H
NNH
N 2
HC
CCO
CH
NNC
CC
H
NN
RP
HN 2 H
N 2C
O O
OP~
~ PO
O OOP
O
O
CH
2
N
N
N
N
O
OH
OHNH
2
HC
CH
N
N
N
N O
O PO
O
O
CH
2
OH
NH
2
HC
CH
CO
OC
O
NH
OC
N HC H
HN 2
NH
2
OO
C-C
H-C
HC
OO
2
HN
CO
CC
HNN
CR
PR
PH
N 2
OO
CC
CH
NR
P
N
CH
N 2
CH
=CH
CO
O
OH
CH
=CH
CO
OCH
CO
CO
O2
CH
2
P
CO
O
OH
O
O
O CO
O
O
CH
CO
O2
O CH
CO
O2
-OO
C
OC
H2
CH
2
OH
HC
P HO
CH
HC
OH
OC
CO
O
CO
OH
O
OH
OH
O
NH
2C
OO
OC
H
NH
CH
CO
CO
O2
NH
CH
O
CO
NH
2O
H
CH
CH
(NH
)CO
O2
3+
N
CO
OC
OO
N+C
OO
CO
OR
P
O
OH
OH
HO
OP
PU
CO
O
O
OH
NH
CO
CH
3
HO
OP
PU
CO
OC
HO
H2
O
OC
CH 2
NH
AC
HO
OP
PU
CO
OCH
OH
2
O
OH
HO
OH
OH
CO
O
OO
CC
HN
(CH
)2
32
Dim
ethy
lgly
cine
1.1.
99.1
1.2.
1.8
CO
OH
OH
OC
OO
O
HO
OH
CO
O
CH
(O)
PP
OC
H 2C
OO
CH
(OH
)H
OC
H 2C
OO
CO
O
C
H(O
)P
HO
CH 2
CO
O
CH
=C(O
)2
PC
OO
CO
NH
2
Rib
ose
-O -
P - O
- P
- O- A
deno
sine
(P)
+ NO O
O O
+
CO
O
NR
ibos
e - O
- P
- O -
P - O
-A
deno
sine
O O
O O
II
II
OHOCH
CH
2C
OO
(NH
) 3+
Epin
ephr
ine
(Adr
enal
ine)
Nor
epin
ephr
ine
(Nor
adre
nalin
e)
Nor
met
epin
ephr
ine
(Nor
met
adre
nalin
e)
HO
CH
CH
N(C
H)
22
33
+
Ade
nosy
l+
+SC
HC
HC
H(N
H)C
OO
22
3C
H3
(CH
)N
(CH
)3
32
3CH
CH
(NH
)CO
O2
3+
+O
H
OO
CC
HC
HC
HC
OS
CoA
22
2
OO
CC
HC
HC
HN
H2
22
2
OO
CC
HC
HC
HC
OC
OO
22
2 O
OC
CH
CH
CH
CH
22
2C
OO
CO
O(N
H) 3
++
HO
H
HO
H
HH
OH
HO
H
Pros
tagl
andi
n PG
E2
OH
HO
CH
2C
CC
OC
CO
O
OH
H OH
HH
-
CO
O
OR'
-CO
-OCHC
HO
-CO
-R2
CH
O P
OC
MP
2O
CH
CH
N(C
H)
22
3+
OH
OC
H
CH
OP
O2
CH
OH
2
O-
CH
OP
O2
OC
HO
CH
=CH
R2
CH
CH
N(C
H)
22
33
+
O-
CH
OP
O2
OR
'-CO
-OC
HC
HO
-CO
-R2
3.1.
1.32
CH
CH
N(C
H)
22
33
+
O-
OH
OC
H
CH
OP
O2
CH
O-C
O-R
2
CH
CH
N(C
H)
22
33
+
O-
CH
CH
(NH
)CO
O2
3+
+C N
HN
C
HC
H
CH
CH
(NH
)CH
O2
3
HS
11-cis
-Ret
inal
Pi
AD
P
NA
DP
+
GD
P-M
annu
rona
te
Man
nose
-6-P
Deh
ydro
-sh
ikim
ate
Shik
imat
e
RN
A
d-G
DP
d-C
TP
GUA
NO
SIN
E-P
(GM
P)
ß-A
lani
ne
P-R
ibos
yl-A
MP
P-R
ibul
osyl
form
imin
o5-
amin
oim
idaz
ole-
carb
oxam
ide-
RP
Imid
azol
eac
etol
-P
HS
HSO
-
PAN
TOTH
ENAT
E
3-Is
opro
pyl-
mal
ate
Succ
inic
sem
iald
ehyd
e
2.4.
1.17
Dia
cyl
glyc
erol
2.3.
1.6
1.14
.12.
1
1.4.
4.2
CH
CH
O3
3.5.
4.19
4.2.
1.19
3.3.
1.1
4.1.
1.12
4.1.
2.5
CO
O-
2O
HC
CH
2.1.
4.1
2.4.
99.7
5.1.
3.12
1.1.
1.13
2
4.2.
1.46
2.7.
1.7
2.4.
1.29
2.4.
1.21
2.4.
1.13
2.4.
1.1
etc.
5.4.
2.2
2.7.
1.6
2.7.
7.10
3.1.
1.18
4.1.
1.34
2.7.
1.47
2.7.
1.16
3.1.
3.9
AD
P
P-G
luco
nola
cton
e
1.1.
1.44
O
OO
HH
O
OH
CH
O 2P
PHEN
YLA
LAN
INE
TYR
OSI
NE
TRYP
TOPH
AN
INO
SIN
E-P
(IMP)
THYM
IDIN
E-P
HIS
TID
INE
UR
IDIN
E-tr
ipho
spha
te(U
TP)
CYS
TIN
EC
YSTE
INE
ISO
LEU
CIN
E
LEU
CIN
E
LYSI
NE
OR
NIT
HIN
E
AR
GIN
INE
HYD
RO
XYPR
OLI
NE
PH
OS
PH
ATID
YL
SE
RIN
EPh
osph
atid
ylin
osito
l
LEC
ITH
IN
SPH
ING
OM
YELI
N
STER
OID
S
Preg
neno
lone
2.7.
6.1
2.4.
2.14
6.3.
4.7
5.3.
1.9
3.1.
3.11
1.2.
1.13
2.7.
2.3
H OH
OH
CC
C
H
CO
OH
CH
HOH
PO
CH
2C
HO 2
P
5.4.
2.1
AD
P4.2.
1.11
Endo
plas
mic
Ret
icul
um
1.1.
1.10
0
3.1.
1.3
Phos
phat
idat
e
2.3.
1.39
4.2.
1.17
4.2.
1.17
4.2.
1.55
1.1.
1.79
1.2.
1.21
1.4.
3.8
1.1.
1.32
2.7.
1.36
2.7.
4.2
4.1.
1.33
2.5.
1.1
2.5.
1.10
2.7.
8.5
2.7.
8.1
4.1.
1.65
2.7.
7.14
1.3.
99.7
PO
OC
H(C
H)
CH
=CH
CH
(OH
)CH
CH
O3
212
2
NH
Acy
l
CH
CH
N(C
H)
22
33
+
O-
3.5.
1.23
1.13
.11.
21
2.5.
1.32
1.1.
1.10
5
2.4.
2.19
1.2.
1.32
MET
HIO
NIN
E
4.1.
3.27
4.2.
1.51
1.14
.17.
1
1.14
.18.
1
1.14
.13.
11
Gly
cina
mid
e-rib
osyl
-P
4.2.
1.22
3-O
xohe
xano
yl-C
oA
THR
EON
INE
1.2.
1.25
1.2.
1.25
1.2.
1.25
1.5.
1.7
- 10
GLU
TAM
ATE
2.3.
1.38
ATP
NA
DH
SUC
RO
SE
AD
ENO
SIN
E-P
(AM
P)
Tria
cylg
lyce
rol
FAT
RN
A
CH
3
CH
2
OC
-CO
OO
H
CO
O
CH
CH
2C
OO
(NH
) 3+
GLY
CO
PRO
TEIN
SG
AN
GLI
OSI
DES
MU
CIN
S
4.1.
2.-
2.6.
1.-
GLU
CO
SE
O-A
cyl-c
arni
tine
O-A
cyl-c
arni
tine
OH
O-
-
R-CO
-OCH
R'-C
O-O
CH
R'-C
O-O
CH
OH
CO
-CO
-R
C
HC
H(O
H)C
HO
-P-O
CH
22
2
CH
O-C
O-R
’2
OR'
-CO
-OCH
O-
CH
O-C
O-R
2
CH
O-P
O2
O-
2.7.
8.11
HN
CH
CH
CH
CH
22
22
CO
O(N
H) 3
+
2.3.
1.20
3.1.
3.4
2.7.
1.10
7
NH
2+
+H
NC
NH
CH
CH
CH
CH
22
22
CO
O(N
H) 3
H OH
HO
H
CC
CC
O
OH
H
HO
CH
2C
HO
H2
R-C
H2C
OO
CH
O-C
O-R
2
CH
O-C
O-R
"2
R’-C
O-O
CH
OH
O
C
HC
HN
H2
3+
OR'
-CO
-OCH
O-
CH
O-C
O-R
2
CH
O P
O2
CO
O
OO
CC
HC
HC
H2
2C
OO
(NH
) 3
+C
HC
H(O
H)C
H(N
H)C
OO
33
O
OH
HO
OH
OH
CH
OH
2C
HO
H2
NH
CH
O-C
O-R
2
1.3.
1.13
4.1.
1.28
Mal
onic
sem
i-al
dehy
de
2.7.
2.4
2.1.
3.3
3.5.
1.2
6.3.
1.2
6.3.5.
5
Car
bohy
drat
esB
iosy
nthe
sis
Deg
rada
tion
Am
ino
Aci
dsB
iosy
nthe
sis
Deg
rada
tion
Lipi
ds Bio
synt
hesi
sD
egra
datio
n
Purin
es &
Pyrim
idin
esB
iosy
nthe
sis
Deg
rada
tion
Bio
synt
hesi
sD
egra
datio
nVi
tam
ins
Co-
enzy
mes
& H
orm
ones
Pent
ose
Phos
phat
e Pa
thw
ay
Phot
osyn
thes
is D
ark
Rea
ctio
ns
CO
MPA
RTM
ENTA
TIO
NTh
e "B
ackb
one"
of m
etab
olis
m in
volv
esG
LYC
OLY
SIS
in th
e C
YTO
PLA
SM
,th
eTC
A C
YC
LE (m
ainl
y) in
the
Mito
chon
dria
l mat
rixan
d AT
P F
OR
MAT
ION
spa
nnin
g th
eM
ITO
CH
ON
DR
IAL
INN
ER
ME
MB
RA
NE
An
elec
tron
flow
(an
elec
tric
curr
ent)
gene
rate
d fro
mN
AD
H a
nd U
QH
2dr
ives
the
trans
loca
tion
of p
roto
nsfro
m th
e m
atrix
to th
e in
term
embr
ane
spac
e.Th
ere
trolo
catio
n of
thes
e pr
oton
s th
roug
h th
e F0
sub
units
ofAT
P sy
ntha
se to
the
mat
rix th
en s
uppl
ies
the
ener
gyne
eded
to fo
rm A
TP fr
om A
DP
and
phos
phat
e
Ele
ctro
n Fl
owP
roto
n Fl
ow
Sm
all N
umbe
rs (
eg. 2
.4.6
.7) r
efer
to th
e IU
BM
BE
nzym
eC
omm
issi
on (E
C) R
efer
ence
Num
bers
of E
nzym
es
LEG
END
Hum
an M
etab
olis
m is
iden
tifie
d as
far p
ossi
ble
by b
lack
arr
ows
Bio
synt
hesi
sD
egra
datio
n
HEM
OG
LOB
INC
HLO
RO
PHYL
L
ATP
TRANSLOCATED
PRO
TON
S
2.7.
1.1AT
P2.
7.1.
2
Met
abol
ic O
rigin
s of
Fuel
7
© 2
003
Inte
rnat
iona
l Uni
on o
f Bio
chem
istry
and
M
olec
ular
Bio
logy
w
ww
.iubm
b.or
g22
nd E
ditio
n D
esig
ned
by D
onal
d E.
Nic
holso
n, D
.Sc.
, Th
e U
nive
rsity
of L
eeds
, Eng
land
– a
nd S
igm
a-Al
dric
h C
at. N
o. M
3782
2H+
H+
OX
ALO
AC
ETA
TE
PYR
UVA
TE
SU
CC
INY
L-C
oA
GLU
TAR
ATE
CIT
RAT
E
MA
LATE
2-O
XO-
ASP
AR
TATE
NO
2-
NO
3- N2
NH
4
CH
3CO
SC
oA
AC
ETYL
- CoAHO
H
CO
2
NA
D
TRANSAMINAT
ION
2H+
2H+
+
CO
2
5-A
min
o-le
vulin
ate
Gly
cine
H+
H+H+
H+
H+H+
c
H+
H+
a
F0
F1
F1
β 2
1α
β
α
γ
10c-
sub-
units
A D
P+
Pi
aaH
+
3.6.
1.34
H+-tra
nspo
rting
ATP
synt
hase
α
δF 6
oscp
ATP
ADP
+Pi
FUM
AR
ATE
UQ
H2
UQ
UQ
H2
NA
DH
+H+
CH
2CO
O-
C(O
H)C
OO
-C
H2C
OO
-
CH
(OH
)CO
O-
CH
CO
O-
CH
2CO
O-
- OO
CC
OC
H2C
H2C
OO
-
- OO
CC
H2C
H2C
O.S
CoA
- OO
CC
OC
H2C
OO
-
CH
3CH
(OH
)CH
2CO
.SC
oA
- OO
CC
H=C
HC
OO
-
CCCCC
Gly
oxyl
ate
C
ycle
-OO
CC
HO
GTP
GD
PAT
P
+
HEM
EPr
otop
orph
yrin
ogen
Cop
ropo
rphy
rinog
enU
ropo
rphy
rinog
enPo
rpho
bilin
ogen
5-A
min
o-le
vulin
ate
CO
O-
CH
2C
H2
H2N
CH
2C=O
FAD
H2 FA
DC
yt.bFe-S
SU
CC
INAT
EII
CH
3CO
CO
O-
PYR
UVA
TE
P i
XY
Cyt.c
1
Fe-S
2e-
2e-
1e- 1e
-
III
2UQ
UQ
UQ
H2
2UQ
H2
2UQ
._
UQ
._
Cyt
.bL
Cyt
.bH
Cyt.c
IV
Cu A
CuB
Cu A 1.9.
3.1
2e-
Hem
e a
Hem
e a 3
2H+
2H+
4H+
4H+
2H+
NAD
+
NA
DH
+H+
NA
D+
1.1.
1.39
1.2.
4.1
2.3.
1.12
3.1.
3.43
4.1.
1.32
4.1.
3.7
4.2.
1.3
1.1.
1.41
1.2.
4.2
2.3.
1.61
6.2.
1.4
- OO
CC
H2C
H2C
OO
-
1.3.
5.1
4.2.
1.2
1.1.
1.37
6.4.
1.1
4.1.
3.8
4.1.
3.1
4.1.
3.2
ISO
CIT
RAT
E
2.6.
1.1
2.3.
1.16
4.1.
1.71
1.2.
1.16
5.1.
99.1
5.4.
99.2
4.3.
1.1
1.4.
1.2
1.4.
1.14
6.3.
5.4
1.6.
6.1
1.7.
99.4
1.7.
7.1
1.6.
6.4
1.18.6
.1
2.3.
1.37
1.10
.2.2
1.10
.2.2
γ
εδ
β
H++
33β
AT
P
AD
P
END
ERG
ON
ICR
EAC
TIO
N1.6.5.3I
FMN
H2
FMN
I
1.6.
5.3
2Fe
-S
(5 C
luste
rs)
H+
H+
H+
H+AT
P
4H+
2H+
2H+or
H+
PHO
TO-
SYST
EM l
O2
3.6.
1.34
NA
DP
+
Gly
cera
ldeh
yde
Rib
ulos
e-1,
5-bi
s-P
2β
8 8
H+
c
3 2
ε
a
3 2
α1α
ε
α
β2
1
3
α
αβ
3
α
β
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
H+
Tran
sloc
ated
pro
tons
H+
H+
H+
H+
Pi
Ferre
doxi
n
4H+
PCPC
PC
PQ
H2 2P
QH
2
PQ
_ .
2PQ
_ . Fe-S
Cyt
.f
PQ
2PQ
Cyt
bf2e-
1e-
1e-
2e-
2e-
2e-
2e-
Cycli
cPh
otop
hosp
hory
latio
n
PQ
PH
OTO
-S
YS
TEM
I
I
Cyt
bc
Non-
cycl
icel
ectro
nflo
w
2e-
2e-
Mn
2e-
*
Prot
ons
from
Wat
er
H2O
H+
H+
2H+
2H+
γ
ATP
synt
hase
CO
2Fi
xatio
n
H+
AD
PP
i
H+ NA
DPH
+H+
eeeAT
PTH
YLA
KO
ID M
EM
BR
AN
E
CH
LOR
OP
LAS
T O
UTE
R M
EM
BR
AN
E
THY
LAK
OID
LU
ME
N
STR
OM
A
(ele
ctric
curre
nt)
P680
Chl
.a
QA
QB
Pheo
phyt
in
P700
Chl
.A0
A 1Fe-S
ATP
AD
P
ATP
1 / 2O
2 H2O
PQ
H2
To B
rain
-
A M I N O A C I D SP Y R I M I D I N E SP U R I N E SC A T E C H O L A M I N E SA R O M A T I C A M I N O A C I D S
hvVI
SIO
N
L I P I DP H O T O S Y N T H E S I S P O R P H Y R I N SS T E R O I D SI S O P R E N O I D SP H O S P H O L I P I D SD E G R A D A T I O NL I P I D B I O S Y N T H E S I SP E N T O S E SH E X O S E SP O L Y S A C C H A R I D E S
CO
CH
CH
(NH
)CO
O2
3+
FOLI
CAC
IDC
1PO
OL
VALI
NE
ATPAT
P
4.1.
1.4
1.1.
1.30
CH
CO
CH
33 CH
CO
CH
CO
O3
2
CH
CH
(OH
)CH
CO
O3
23-
OH
-But
yrat
eA
ceto
ne Ace
toac
etat
e
KET
ON
E B
OD
IES
HYA
LUR
ON
IC A
CID
DER
MAT
AN
BLO
OD
GR
OU
PSU
BST
AN
CES
PEPT
IDO
-G
LYC
AN
N-A
c-N
eura
min
ate
(Sia
late
)
UD
P-Id
uron
ate
UD
P-N
-Ac-
Gal
acto
sam
ine
UD
P-G
alac
turo
nateG
DP-
Fuco
se
TDP-
Rha
mno
se
AD
P-G
luco
se
UD
P-G
luco
se
TDP-
4-O
xo-
6-de
oxyg
luco
se
MA
NN
OSE
CH
ITIN
CH
ON
DR
OIT
INP
EC
TIN
ALG
INAT
ES
INU
LIN
CEL
LULO
SE
O-A
NTI
GEN
SST
AR
CH
GLY
CO
GEN
LAC
TOSE
GA
LAC
TOSE
O
OH
HO
OH
OH
CH
3O
OPP
TO
OH
OH
O
OHAC
NH
HO
OH
O
OH
HO
OP
PU
NH
AC
OH
OH
OH O
H
HO
OH
NH
CO
CH
OH
HOO
OP
PG
CH
OH
2
HO
P
UD
P-N
-Ac-
Glu
cosa
min
epy
ruva
teN
-Ac-
Man
nosa
min
e-6-P
UD
P-G
lucu
rona
te
GD
P-M
anno
se
N-A
c-M
anno
sam
ine
UD
P-N
-Ac-
Glu
cosa
min
eN
-Ac-
Glu
cosa
min
e-6-P
Sorb
itol
Fruc
tose
-1-P
Eryt
hros
e-4-P
3-D
ehyd
rogu
lona
te
L-Xy
lose
L-Ly
xose
D-X
ylul
ose
D-R
ibos
e
Rib
itol
L-A
rabi
tol
L-Xy
lulo
se
L-R
ibul
ose
L-R
ibul
ose-
5-P
L-Xy
lulo
se-5
-P
L-A
rabi
nose
Xylit
olD
-Xyl
ose
D-A
rabi
nose
D-R
ibul
ose
ASC
OR
BATE
2, 3
-Dio
xogu
lona
te
N-A
c-G
luco
sam
ine-
1-P
Inos
itol-P
Inos
itol
Glu
curo
nate
Gul
onat
e
Gul
onol
acto
ne2-
Oxo
gulo
nola
cton
e
Fruc
tose 6-P-
Glu
cona
te
D-R
ibul
ose-
5-P D
-Xyl
ulos
e-5-P
Man
nose
-1-P
GD
P-G
luco
se
TDP-
Glu
cose
UD
P-G
alac
tose
Gal
acto
se-P
Glu
cose
-1-P
Glu
cose
-6-P
Fruc
tose
-6-P
Fruc
tose
-1:
6-bi
s-P
OH
HH
HO
HO
CH
2C
CC
CC
O
OH
OH
HO
H
HH
O
HO
CH
2C
CC
CO
CO
OH
H
H OH
H
CCO
H
CO
P-R
ibos
ylam
ine
Gly
cera
te2,
3-D
ipho
spho
-gl
ycer
ate3-P-
Gly
cera
ldeh
yde
1:3-
bis-P-
Gly
cera
te
3-P-
Gly
cera
te
2-P-
Gly
cera
te
P-en
olpy
ruva
te
Inos
itol
CH
OH
2
CH
OH
2
HO
CH
CH
OH
2
CH
O 2
HO
CH
P
Gly
cero
l
UD
P-G
alac
tose
UD
P-Su
gars
CH
CH
OH
32
ETH
AN
OL
Dih
ydro
xy-
acet
one-P
(Gly
cero
ne-P
)
Glu
cosa
min
e-6-P
Phos
pho-
serin
e
Cha
in e
long
atio
nM
itoch
ondr
ial
Ser
ine
Ser
ine
Indo
le-3
-gly
cero
l-P
3-D
eoxy
-D-a
rabi
no-
hept
ulos
onat
e-7-P
Indo
leac
etat
e(A
uxin
)In
doxy
l Form
ylky
nure
nine
Kynu
reni
ne3-
Hyd
roxy
kynu
reni
ne3-
Hyd
roxy
anth
rani
late
2-A
min
o-3-
carb
oxy
muc
onat
e se
mia
ldeh
yde
NH
OH
Tryp
tam
ine
1-(o
-Car
boxy
phe
nyla
min
o)1-
deox
yrib
ulos
e-5-P
N-(5
-P-R
ibos
yl)
anth
rani
late
Ant
hran
ilate
Cat
echo
l
NH
Indo
le-
acet
alde
hyde
NH
CH
CH
O2
Indo
lepy
ruva
te
NHC
-CH
(OH
)CH
(OH
)CH
O 2P
CH
2-A
min
omuc
onat
e-6-
sem
iald
ehyd
e
CH
CH
NH
22
2
NH
1.2.
3.7
4.1.
1.43
3.5.
1.9
3.7.
1.3
4.2.
1.20
1.13
.11.
64.
1.1.
45
2.4.
2.18
4.6.
1.4
4.1.
1.48
1.14
.13.
9
4.6.
1.3
Deh
ydro
-qu
inat
e4.2.
1.10
1.1.
1.25
2.5.
1.19
Shik
imat
e-3-P
Shik
imat
e-5
enol
pyru
vate
3-P
Cho
rism
ate
PEP
2.7.
1.71
1.4.1.
19
Hom
ogen
tisat
ePh
enyl
pyru
vate
Cin
nam
ate
Cou
mar
ate
Prep
hena
te
2-A
min
om
ucon
ate
Fum
arat
eA
spar
tate
GLY
CIN
E
Sarc
osin
e
Hyd
roxy
-py
ruva
te
P-H
ydro
xy-
pyru
vateSE
RIN
E
Imid
azol
egl
ycer
ol-P
P-R
ibos
yl-A
TPP-
Rib
osyl
form
imin
o5-
amin
oim
idaz
ole-
carb
oxam
ide-
RP
Form
imin
ogl
utam
ate
Imid
azol
one
prop
iona
teU
roca
nate
Cys
tath
ioni
neH
omoc
yste
ine
Phos
phoa
deny
lyl-
sulp
hate
(PA
PS)
CH
(NH
)CO
OH
23
+
His
tidin
ol-P
His
tidin
olH
istid
inal
3.1.
3.15
2.6.
1.9
1.1.
1.23
3.6.
1.31
5.3.
1.16
2.4.
2.17
Asp
arag
ine
ALA
NIN
E
3-Su
lphi
nyl
pyru
vate
Oxo
buty
rate
2-A
ceto
-2-
hydr
oxy-
buty
rate
O-P
hosp
ho-
hom
oser
ineH
OS
CH
CH
NH
22
22
Hyp
otau
rine
HO
SC
HC
HN
H3
22
2
Taur
ine
Glu
tam
ate
γ-G
luta
myl
cyst
eine
Glu
tath
ione
Gly
cine
Cys
tein
e
ß-A
lani
ne
Cys
teat
eS-
Ade
nosy
lho
moc
yste
ine
4.2.
99.2
1.1.
1.86
4.2.
1.9
1.1.
1.86
4.2.
1.9
2.6.
1.32
4.1.
3.18
S-A
deno
syl
met
hion
ine
(SA
M)
2-M
ethy
lace
to-
acet
yl-C
oA
2-A
ceto
lact
ate
2-3-
Dih
ydro
xyis
oval
erat
e2-
Oxo
-is
oval
erat
e
3-H
ydro
xy-
isob
utyr
ate
3-H
ydro
xy-
Isob
utyr
yl-C
oAM
ethy
lac
ryly
l-CoA
2-M
ethy
l-3-
hydr
oxy-
buty
ryl-C
oA
Tigl
yl-C
oA2
Met
hylb
utyr
yl-
CoA
2:3-
Di-O
H-
3-m
ethy
lval
erat
e2-
Oxo
-3-m
ethy
lva
lera
te
Isob
utyr
yl-C
oA
Cys
tein
esu
lphi
nate
4.2.
99.9
2-Is
opro
pyl-
mal
ate
CH
CH
CO
CO
O3
2
+C
HC
H(N
H)C
OO
33
CH
CH
(OH
)CO
O3
HO
SC
HC
OC
OO
22
OC
HC
OC
OO
2P
OC
HC
H(N
H)C
OO
23
P
HO
CH
CO
CO
O2
HO
CH
CH
(NH
)CO
O2
3+
+
OH
CH
CO
CO
O2
CO
O OH
OH
O
CO
O OH
OH
HO
P
CO
O
OH
OH
O
CH
2
P
CO
O
O-C
-CO
OO
HO
OH
OO
CC
HC
OC
OO
2
NH
HO
C-C
H(O
H)C
H(O
H)C
H2O
PC
H
CO
O
NH
2
CO
O
OH
NH
2C
OO
CO
O
OC
H
OO
CC
HN
HC
H2
3
CH
(CH
)C
OS
-AC
P3
214
CH
(CH
)C
OS
CoA
32
14
CH
(CH
)C
H=C
HC
O-S
-AC
P3
22
CH
CH
=CH
CO
-S-A
CP
3C
HC
H(O
H)C
HC
OS
-AC
P3
2
CO
SC
oA
Lino
leat
e
Ole
oyl-C
oA
Stea
royl
-CoA
Deh
ydro
stea
royl
-CoA
OH
-Ste
aroy
l-CoA
Oxo
stea
royl
-CoA
Palm
itoyl
-AC
PPa
lmito
yl-C
oA
ACYL
-AC
P2,
3-E
noyl
-AC
P
3, 4
-Dec
enoy
l-AC
P
2, 3
-Dec
enoy
l-AC
P
3-O
H-A
cyl-A
CP
3-O
xoac
yl-A
CP
3-O
xo-D
ecan
oyl-A
CP
3-O
xo-H
exan
oyl-A
CP
3-O
H-H
exan
oyl-A
CP
2, 3
-Hex
enoy
l-AC
P
But
anoy
l-AC
PC
roto
noyl
-AC
P3-
OH
-But
anoy
l-AC
PA
ceto
acet
yl-A
CP
Hex
anoy
l-AC
P
3-O
H-D
ecan
oyl-A
CP
Dec
anoy
l-AC
P
Palm
itole
oyl-A
CP
γ-Li
nole
nate
Ara
chid
onat
eLe
ukot
riene
B4
CO
SC
oA
CO
-S-A
CP
Thro
mbo
xane
B2
HO
OC
CH
CO
-S-A
CP
2M
alon
yl-A
CP
HO
OC
CH
CO
-SC
oA2
Mal
onyl
-Co-
A
CH
CO
-S-A
CP
3
Ace
tyl-A
CP
CH
O-C
O-R
2
CH
OH
2
R’-C
O-O
CH
FATT
Y AC
IDAC
YL-C
oA(C
ytos
ol)
CH
O-C
O-R
2
CH
O 2
R’-C
O-O
CH
P
Car
diol
ipin
Phos
phat
idyl
glyc
erol
Ace
tylc
holin
eG
lyce
roph
osph
ocho
line
Lyso
leci
thin
Cho
line
plas
mal
ogen
CD
P-ch
olin
eC
holin
e-P
Mev
alda
te
CH
(CH
)C
H=C
HC
H(O
H)C
HC
HO
H3
212
2
Deh
ydro
sphi
ngan
inSp
hing
anin
4-Sp
hing
enin
Psyc
hosi
ne
Acy
l-CoA
Acy
l-CoA
Cer
ebro
side
Gal
acto
seC
H(C
H)
CH
=CH
CH
(OH
)CH
CH
O-
32
122
NH
CO
R
Isop
ente
nyl-PP
(C5)
Dim
ethy
lally
l-PP
(C5)
Ger
anyl
-ger
anyl
-PP
(C20
)
Farn
esyl
-PP
(C15
)
Squa
lene
(C30
)
Ger
anyl
-PP
(C10
)
Des
mos
tero
lZy
mos
tero
lLa
nost
erol
CH
C =
CH
CH
O3
2P
P
CH
3
Cer
amid
e
Gan
glio
side
sN
HC
OR
CH
O 2P
P
OP
PC
H2
CH
OLE
STER
OL
CH
C(O
H)C
HC
HO
H3
22
CH
CO
O2
CH
C(O
H)C
HC
HO
32
CH
CO
O2
NA
DP
+D
ehyd
roas
corb
ate
OH
HO
HO
CH
2C
CC
CC
O
OH
HO
H
OH
HO
HO
CH
2C
CC
OC
OC
O
H
NA
D+
Pi
AD
PA
DP
Phyt
oene
(C40
)Ly
cope
ne(C
40)
ß-C
AR
OTE
NE
(C40
)R
hodo
psin
Met
arho
dops
in
Ret
inoa
te
trans-
Ret
inal
11-cis
-Ret
inol
trans-
Ret
inol
(Vita
min
A)
Ret
inol
est
ers
Dar
k
Ligh
t
Ubi
quin
one
(Coe
nzym
e Q
)
Men
aqui
none
Plas
toqu
inon
e
Phyl
loqu
inon
e(V
itam
in K
)
Ops
inC
HO
CH
OH
2
CH
O
CH
OH
2
CH
3C
HO 3
CH
O 3n
O O
OO
Phyt
ol(C
20)
α-To
coph
erol
(Vita
min
E)
Qui
nolin
ate
Qui
nolin
ate-
nucl
eotid
eN
icot
inat
e-nu
cleo
tide
Des
amin
o-N
AD
5-H
ydro
xy-
tryp
toph
an5-
Hyd
roxy
tryp
tam
ine
(SER
OTO
NIN
)N-
Acet
yl-5
-O-m
ethy
l-ser
oton
in(M
ELAT
ON
IN)
NH
CH
CH
NH
CO
CH
22
3H
O
NH
CH
CH
NH
CO
CH
22
3C
HO 3
+N
AD
(P)
NIC
OTI
NAT
E
N-A
cety
l-ser
oton
in
2.4.
2.19
Dop
amin
eD
opa
Dop
aqui
none
THYR
OXI
NE
MEL
AN
IN
OH
OH
CH
OH
CH
NH
CH
23
OH
OH
CH
OH
CH
NH
22
4-O
H-3
-Met
hoxy
-ph
enyl
glyc
ol
CH
OH
CH
NH
22
OH
OC
H3
OC
H3
CH
OH
CH
OH
2
OH
OC
H3
4-O
H-3
-Met
hoxy
-D
-man
dela
te
Cyc
lic A
MP
ATP
Dep
hosp
ho-C
oenz
yme
A
4-P-
Pant
ethe
ine
4-P-
Pant
othe
nylc
yste
ine
4-P-
Pant
othe
nate
Pant
oate
6.3.
2.1
1.1.
1.16
9
3.5.
1.22
2.7.
1.33
NH
NH
O O
O O
CH
OH
2
OH
OC
H3
CH
(OH
)CO
O
H2 NH
3+
CH
-CO
OC
O O
CO
O
NR
ibos
e-P
N+
CO
O
NH
CH
CO
O2
O
OH
CH
O 2P
NH
CO
CH
NH
22
OH
Form
ylgl
ycin
amid
e-RP
Ure
a
Form
ylgl
ycin
amid
ine-
RP
Alla
ntoa
teA
llant
oin
UR
ATE
AD
P
Xant
hine
Hyp
oxan
thin
e
Inos
ine
Ade
nine
Ade
nylo
-su
ccin
ate
5-A
min
oim
idaz
ole-
RP
5-A
min
o-4-
imid
azol
eca
rbox
ylat
e-RP
5-A
min
o-4-
imid
azol
e(N
-suc
ciny
lcar
boxa
mid
e)-RP
5-A
min
oim
idaz
ole
carb
oxam
ide-
RP Fo
rmyl
amid
o-im
idaz
ole-
carb
oxam
ide-
RP
HN
CO
NH
22
HNH
C 2C
HO
NH
RP
NH
C
CCO
CC
OO
CN
H
NH
HN
HN
H
CCO
CC
HO
CN
H
N
N
HN
Car
bam
oyl
ß-al
anin
eD
ihyd
ro-
urac
ilU
raci
l
d-A
DP
d-AT
P
GTP
GD
P
XAN
THO
SIN
E-P
(XM
P)
TTP
TDP
ß-U
reid
ois
obut
yrat
eD
ihyd
roth
ymin
eTh
ymin
ed-
UM
Pd-
CM
Pd-
CD
P
CD
P
Car
bam
oyl
aspa
rtat
eD
ihyd
roor
otat
eO
rota
teO
rotid
ine-P
Urid
ine-P
(UM
P)U
DP
3-A
min
o-is
obut
yrat
eC
HCNH
2 CH
OC
NH
NC
HCO
CH
OC
NH
HN
CH
-CH
3CO
OC
NH
HN
CH
2
CH
2C
H2
CO
OC
NH
HNCO
CH
OC
NH
HN
CC
H3
Met
hylm
alon
ylse
mia
ldeh
yde
OH
CC
HC
OO
CH
3
CH
2CO
CH
-CO
OO
CN
H
HN
CH
CO
C-C
OO
OC
NH
HN
HN
CO
NH
CH
CH
CO
O2
22
CC
CC
H RP
HC
NH
NH
OO
C-C
H-C
HC
OO
2 N
N
N
CH
O
NH
RP
NH
OC
HC 2
2.7.
7.43
3.1.
3.29
1.1.
1.15
8
5.1.
3.13
2.7.
1.38
3.2.
1.23
3.1.
3.29
4.1.
3.20
2.7.
1.60
5.1.
3.14
5.1.
3.7
5.1.
3.1
2.7.
1.4
5.4.
2.3
3.1.
1.17
1.1.
1.49
1.1.
1.21
2.7.
7.23
3.1.
3.25
1.13
.99.
11.
1.1.
19
1.1.
3.8
5.3.
1.3
2.7.
1.53
1.1.
1.9
2.7.
1.15
2.7.
1.17
5.1.
3.4
5.1.
3.1
2.2.
1.2
4.1.
2.13
2.7.
1.11
2.7.
1.47
2.2.
1.1
1.2.
1.12
1.1.
1.29
1.1.
1.95
1.3.
1.35
1.14
.99.
25
2.3.
1.41
2.3.
1.41
2.3.
1.41
1.1.
1.10
0
5.3.
99.5
4.2.
1.60
5.3.
99.3
1.14
.99.
11.13
.11.
34
1.3.
1.10
1.3.
1.9
1.14
.99.
5
1.3.
1.9
4.2.
1.61
4.2.
1.60
4.2.
1.60
4.2.
1.59
4.2.
1.58
1.3.
1.9
1.3.
1.9
6.2.
1.3
3.1.
2.20
1.1.
1.10
0
5.3.
1.1
HO
OC
-CO
OH
Oxa
late
Gly
cola
te
HO
CH
CH
O2
Gly
col
alde
hyde
Etha
nola
min
e-P2.
7.1.
30
2.3.
1.7
3.7.
1.2
4.1.
3.5
2.7.
8.8
2.1.
1.17
2.1.
1.71
1.3.
1.35
2.7.
8.2
3.1.
4.3
3.1.
4.4
2.7.
7.15
3.1.
1.5
3.1.
4.2
2.7.
1.32
2.7.
1.82
1.2.
4.1
2.3.
1.12
1.8.
1.4
2.6.
1.2
1.4.
1.1
4.1.
1.1
2.3.
1.50
1.1.
1.10
2
3.1.
4.12
2.7.
8.3
2.4.
1.62
3.2.
1.46
5.2.
1.3
1.2.
1.36
2.3.
1.76
3.1.
1.21
5.2.
1.7
5.4.
99.7
1.14
.99.
7
4.3.
1.8
4.2.
1.75
4.1.
1.37
1.3.
3.3
1.3.
3.4
4.99
.1.1
2.5.
1.29
2.4.
1.47
4.1.
1.28
2.3.
1.5
2.1.
1.4
6.3.
5.1
6.3.
1.5
2.4.
2.11
2.7.
7.18
2.6.
1.5
1.2.
1.32
1.13
.11.
5
2.1.
1.28
2.1.
2.2
6.3.
3.1
3.5.
2.5
1.4.
1.10
1.7.
3.3
1.1.
1.20
41.
1.3.
221.
1.3.
22
4.1.
1.28
4.1.
1.21
2.1.
2.3
2.4.
2.1
1.5.
99.2
2.1.
1.5
2.6.
1.22
3.5.
2.3
2.6.
1.51
1.4.
1.7
3.1.
3.3
2.6.
1.52
2.1.
3.2
ACET
ATE
2.4.
2.4
2.1.
1.45
RP
CH
CO
CH
OC
N
HN
1.3.
1.14
2.4.
2.10
4.1.
1.23
2.7.
7.7
2.7.
7.7
2.7.
7.7
1.17
.4.1
2.7.
7.7
2.7.
4.14
4.4.
1.1
1.6.
4.1 1.
13.1
1.20
4.4.
1.8
4.2.
1.22
1.1.
1.27
4.1.
1.29
6.3.
2.3
6.3.
2.2
1.8.
1.3
LAC
TATE
Ace
tald
ehyd
e
2.7.
1.24
2.7.
7.3
4.1.
1.36
Bile
Aci
ds
CH
CH
CO
SC
oA3
2Pr
opan
oyl-C
oA
1.1.
1.31
2.1.
3.1
4.1.
1.41
5.1.
99.1
6.4.
1.3
6.3.
2.5
2.1.
1.14
2.1.
1.13
4.6.
1.1
CD
P-Et
hano
lam
ine
1.1.
1.35
4.2.
1.17
+H
OS
CH
CH
(NH
)CO
O2
23
3.5.
2.7
NH
HN
CH
OO
CC
HC
HC
HC
OO
22
CM
P-N
-Ace
tyl
neur
amin
ate
CD
P-di
acyl
glyc
erol
CH
OLI
NE
Etha
nola
min
e
Gly
oxyl
ate
HIS
TAM
INE
2.3.
1.46
Hom
oser
ine
Tyra
min
e
Plan
t Pig
men
tsTa
nnin
s
Mal
eyl
acet
oace
tate
Fum
aryl
acet
oace
tate
5.2.
1.2
CH
CO
O2
OH
OH
OHCH
CH
NH
22
2
OH
OH
CH
CH
NH
22
2Hyd
roxy
phen
ylpy
ruva
te
α-To
coph
erol
(Vita
min
E)
LIG
NIN
d-G
TP
OH
OH
OH O
HO
OH
P
OP
PT
CH
3H
O
OH
OH
O
NA
DPH
2.2.
1.1
2.7.
1.3
1.1.
1.45
1.1.
1.13
0
1.10
.3.3
1.10
.2.1
1.1.
1.10
ATP
CH
CH
NH
22
2
NH
HO
5.4.
99.5
1.14
.16.
12.
6.1.
51.
13.1
1.27
Indo
le
4.1.
99.1
1.13
.11.
11
OH O
OH
NH
CC
CH
CH
O 2P
HH
CO
O
NH
2
CO
O
6.3.
5.3
6.3.
2.6
4.3.
2.2 G
uani
neD
NA
6.3.
4.4
4.3.
2.2
CCO
CC
HH
CN
H
N
N
HN
CCO
CC
HH
CN
H
N
N
HN
3.5.
3.4
2.4.
2.1
2.7.
7.6
2.7.
7.6
2.7.
7.6
2.7.
7.6
2.7.
4.6
2.7.
4.3
2.7.
4.4
2.7.
4.6
2.4.
2.15
1.1.
1.20
5
6.3.
4.1
6.3.
5.2
2.7.
4.4
3.5.
4.3
3.2.
2.2
2.4.
2.1
3.1.
3.5
3.1.
4.6
6.3.
4.2
1.17
.4.1
1.17
.4.1
3.5.
4.12
2.7.
4.8
2.7.
4.9
2.7.
4.6 2.4.
2.4
1.3.
1.2
3.5.
2.2
3.5.
1.6
3.5.
1.6
3.5.
2.2
3.5.
4.1
Dip
hosp
ho-
mev
alon
ate
Mev
alon
ate
3-O
xope
ntan
oyl-C
oA
3-O
xoac
yl-C
oA3-
OH
-Acy
l-CoA
2, 3
-Eno
yl-C
oA
2, 3
-Hex
enoy
l-CoA
3-O
H-H
exan
oyl-C
oA
Ace
toac
etyl
-CoA
3-O
H-B
utan
oyl-C
oAC
roto
noyl
-CoA
Pent
anoy
l-CoA
3-O
H-P
enta
noyl
-CoA
1.1.
1.35
1.1.
1.35
1.1.
1.15
7
1.3.
99.3
1.3.
99.3
1.3.
99.2
1.1.
1.35
Odd
C F
atty
aci
ds
Succ
inyl
hom
oser
ine
CO
2
2-O
XO A
CID
Glu
tam
yl-P
Glu
tam
ine
UR
EA
P-C
reat
ine
Cre
atin
eC
reat
inin
e
Gly
cine
CIT
RU
LLIN
E
Glu
tam
icse
mia
ldeh
yde
2-A
MIN
O A
CID
Pyrr
olin
e-5-
carb
oxyl
ate
Gly
oxyl
ate
Pyru
vate
4-H
ydro
xy-
2-ox
oglu
tara
te
4-H
ydro
xy-
glut
amat
e
3-H
ydro
xy-
pyrr
olin
e-5-
carb
oxyl
ate
Putr
esci
neH
NC
HC
HC
HC
HN
H2
22
22
2
Sper
mid
ine
Sper
min
e
N -T
rimet
hylly
sine
66
N -T
rimet
hyl-
3-O
H-ly
sine
Car
nitin
e
Glu
tary
l-CoA
Sacc
haro
pine
2-A
min
oadi
pate
sem
iald
ehyd
e2-
Amin
oadi
pate
2-O
xoad
ipat
e
Arg
inin
o-su
ccin
ate
Gua
nido
acet
ate
Met
hylm
alon
yl-C
oA
4.1.
2.12
Asp
arty
lSe
mia
ldeh
yde
2, 3
-Dih
ydro
-di
pico
linat
e
1.2.
1.11
4.2.
1.52
1.3.
1.26
Pipe
ridei
ne-
2, 6
-dic
arbo
xyla
teN
-Suc
ciny
l-2-
amin
o-6-
oxo-
pim
elat
e
2.6.
1.17
N-S
ucci
nyl-2
, 6di
amin
opim
elat
eD
iam
ino-
pim
elat
e3.
5.1.
18
3-M
ethy
l-gl
utac
onyl
-CoA
(CH
)C
HC
HC
OS
CoA
32
2(C
H)
CH
CH
CO
SC
oA3
22
3-M
ethy
l-cr
oton
yl-C
oAIs
oval
eryl
-CoA
Oxo
pant
oate
HC
HO
OO
CC
HC
= C
HC
OS
CoA
2CH
3
CH
CO
CH
CO
SC
oA3
CH
3C
HC
H=C
HC
OS
CoA
3
CH
3C
HC
H(O
H)C
HC
OS
CoA
3
CH
3
C(O
H)C
H(O
H)C
OO
CH
CH
32
CH
3
CH
= C
CO
SC
oA2
CH
3H
OC
HC
HC
OS
-CoA
-2C
H3
CH
CH
CO
-SC
oA3
CH
3
C (O
H)C
H(O
H)C
OO
CH
3
CH
3
CH
CH
CH
CO
SC
oA3
2CH
3
CH
C =
CH
CO
SC
oA3C
H3
ATP
4-A
min
obut
yrat
e(G
ABA
)
1.3.
99.7
1.5.
1.2
1.14
.11.
2
2.6.
1.39
1.2.
1.31
1.14
.11.
8
2.5.
1.16
2.5.
1.22
4.1.
3.16
2.6.
1.23
1.5.
99.8
1.5.
1.2
6.4.
1.4
1.3.
99.1
0
4.2.
1.33
2.6.
1.6
1.1.
1.85
Oxo
leuc
ine
CO
OH
(CH
)C
HC
HC
H(O
H)C
OO
32
S-A
deno
sylm
ethy
lth
iopr
opyl
amin
e(D
ecar
boxy
late
d SA
M)
PRO
LIN
E
Coe
nzym
e A
CH
C=
CH
CH
32
CH
3
OC
H
CH
3
3H
OC
H3
CH
3
CH
3
CH
C-C
HH
O3
22
CP
P
CH
2
CH
C=
CH
CH
O2
2P
P
CH
3
3-P-
Gly
cero
l
Phos
phat
idyl
etha
nola
min
eC
EPH
ALI
N
3.1.
4.12
2.7.
8.3
Prog
este
rone
1.5.
1.12
2.7.
3.2
4.2.
1.17
3.1.
2.4
2.6.
1.32
4.4.
1.15
Ace
tyls
erin
e2.
7.7.
42.
7.1.
251.
8.99
.1A
deny
lyls
ulph
ate
(APS
)
2.7.
1.39
4.4.
1.15
4.1.
1.29
4.2.
99.8
2.3.
1.30
P-R
ibos
yl-PP
1.1.
1.1
1.2.
1.4
Asp
arty
l-P
5.1.
1.7
2.7.
1.40
4.1.
3.18
4.1.
3.18
1.5.
1.9
1.14
.11.
1
CH
OLI
NE
2.1.
1.13
1.3.
1.2
NH
CH
CH
SH
22
N
HC
HC
HC
O2
2O
CH
C(C
H)
CH
(OH
)CO
23
2P
AD
P-
NH
CH
CH
SH
22
N
HC
HC
HC
O2
2O
CH
C(C
H)
CH
(OH
)CO
23
2
P-A
DP
-N
HC
HC
HS
H2
2
NH
CH
CH
CO
22
OC
H C
(CH
)C
H(O
H)C
O2
32
1.4.
1.8
1.3.
99.3
1.3.
99.3 1.
4.1.
9
4.2.
1.18
4.1.
1.20
1.3.
99.7
1.8.
99.2
+C
HC
O-O
CH
CH
(NH
)CO
O2
23
2.5.
1.6
2.1.
1.10
2.1.
1.20
1.1.
1.3
1.1.
1.3
4.2.
1.18
4.1.
2.5
4.3.
1.5
4.2.
1.20
2.1.
2.1
2.1.1.
20
Gly
oxyl
ate
2.1.
1.6
1.4.3.
41.
14.1
8.11.14
.16.
2
Hex
anoy
l-CoA
But
anoy
l-CoA
6.3.
4.16
6.3.
5.5
2.7.
2.11
2.1.
3.3
NO
1.14
.13.
39
3.5.
3.6
3.5.
3.1
4.3.
2.1
4.1.
1.17
2.7.
7.41
2.6.
1.4
1.1.
1.10
0
1.1.
1.8
2.3.
1.51
2.3.
1.15
2.7.
8.5
SO- 42
1.14
.16.
4
NH
2 O
OC
O
OC
4.1.
1.25
1.3.
1.13
1.3.
1.13
2.7.
4.6
CYT
IDIN
E-tr
ipho
spha
te(C
TP)
Cyt
osin
e
2.4.
2.9
4.1.
1.11
2.6.
1.18
4.3.
1.3
4.2.
1.49
3H
SO-
1.1.
1.10
5
2.3.
1.41N
AD
PH
1.1.
1.22
2.3.
1.4
5.5.
1.4
3.2.
1.26
3.2.
1.48 2.
6.1.
16
1.1.
1.14
2.7.
7.34
4.2.
1.47
2.4.
1.68
2.4.
1.69
2.4.
1.9
5.3.
1.8
2.4.
1.11
O
OP
PU
CH
OH
2
CH
OH
2
HO
OHO
H HO
2.4.
1.21
4.2.1.
521.
2.1.
18
4.2.
1.18
O
CH
C
CH
OC
N
HN
DP CH
CO
CH
OC
N
HN
RP
PP
OC
H2
H CCH O
HO
H
CH
NH
NC H
CP
H
O
OC
H2
CCH O
H
H OH
C
H CC
CNH
2 CC
HH
CN
RP
(PP
)
N
N
N+P
NH
2H
O
OC
H2
CCH O
H
H OH
C
H CC
OC
CC
HH
CN
RP
N
N
NH
P
H
OC
H2
CCH O
HO
H
CO
CH
2C
CO
NH
2 CC
HH
CN
RP
N
N
NH
P
+O
OC
CH
N(C
H)
23
3B
etai
ne
Bet
aine
alde
hyde
2.4.
1.16
5.1.
3.6
2.4.
1.33
2.7.
7.13
5.4.
2.8
5.3.
1.8
O
OH
CH
OH
2 HO
OP
HO
2.7.
1.28
2.7.
1.31
6.3.
4.13
5.3.
1.1
2.2.
1.1
4.1.
1.9
3.1.
2.11
ß-O
H-ß
-Met
hyl-
glut
aryl
-CoA
6.3.
4.5
5.3.
1.6
2.5.
1.21
2.1.
1.2
3.5.
2.10
6.3.
2.13
6.3.
2.7-
10
2.7.
7.27
2.7.
7.9
3.5.
4.10
CCO
CC
HO
CN
RP
N
NH
HN
CCO
CC
H
NN
N
HN
RP
HN 2
C
2.7.
4.6
1.17
.4.1
2.7.
4.6
2.6.
1.13
Car
bam
oyl-P
2.3.
1.9
Car
nitin
e
2.6.
1.4
2.6.
1.44
CH
C(O
H)C
HC
OS
CoA
32
CH
CO
O2
1.2.
3.5
1.1.
1.34
2.3.
1.16
4.1.
3.5
2.3.
1.16
4.1.
3.4
Men
aqui
none
4.1.1.
15
2.6.
1.19
4.2.
1.16
Car
nosi
ne
CH
CH
NH
22
2C N
HN
C
HC
H
4.1.
1.22
4.3.
1.3
Ubi
quin
one
Plas
toqu
inon
e
D-R
ibos
e-5-P
NH
CH
CH
(NH
)CO
O2
3H
O+
O
OH
OH
HO
OP
PU
CO
O-
O
OH
OH
HO
OP
PU
CO
O-
OH
HO
H
HO
CH
2C
CC
O
H
CO
CO
O-
OC
HO
HC
HO
HA
cNH
HO
OP
COC
O-
CH
OH
2
OC
HO
HC
HO
HA
cNH
HO
OHCO
OC
HO
H2
O
OH
OH
HO
HO
CH
O 2P
O
OHAC
NH
HO
OH
CH
O 2P
O
OO
HH
OH
OP
CH
OH
2
O
OH
OH
HO
HO
CH
OH
2
O
OH
HO
OH
3
CH
O 2P
O
OH
HO
O
NH
CO
CH
3
P
CH
OH
2C
HO
H2
CH
OH
2
O
OH
HO
OH
NH
2
CH
O 2P
O
OH
HO
OHO
PP
U
CH
OH
2
O
O
HO
OH
OH
HO
P
CH
OH
2
CH
OH
2O
OH
O
OH
OH
O
OH
OH
OH
CH
OH
2
O
OH
HO
OHO
H
CH
2C
HO
P2
OH
HH
HO
H
CC
CC
OH
OH
H
CO
O-
HO
CH
2
H OH
OH
OH
CC
CC
HO
HH
HO
CH
2
H OH
OH
H
CC
CC
HO
HO
H
HO
CH
2
OH
HO
HH
CC
CC
HO
HO
H
HO
CH
2
H OH
HO
H
CC
CC
HO
OH
H
HO
CH
2
OH
HH
OH
CC
CC
HO
OH
H
HO
CH
2
OH
HO
HO
H
CC
CC
HO
HH
HO
CH
2
H OH
HO
H
CC
CC
OH
HH O
HCO
O-
PO
CH
2
OH
HO
H
CC
CO
H
PO
CH
2C
HO
H2
H OH
H
CC
CO
OH
HO
CH
2C
HO
H2
CH
OH
2P
OC
H2
H OH
OH
CC
CO
H
CH
OH
2P
OC
H2
OH
HH
CC
CO
OH
CH
OH
2P
OC
H2
H OH
OH
CC
CO
H
HO
CH
2C
HO
H2
OH
HO
H
CC
CO
H
HO
CH
2C
HO
H2
OH
HH
CC
CO
OH
HO
CH
2C
HO
H2
H OH
OH
H
CC
CHO
H
HO
CH
2C
HO
H2
OH
HO
HO
H
CC
CHH
HO
CH
2C
HO
H2
H OH
HO
H
CC
CC
OH
HH O
HCH
OH
2H
OC
H2
H OH
OH
CC
CH
OH
POC
H2
H OH
HO
H
CC
CC
O
OH
H
HO
CH
2C
HO 2
P
H OH
OH
OH
CC
CHH
HO
CH
2C
HO
H2
H OH
OH
CC
C
H
CO
HHO
PO
CH
2C
HO
H2
P
H OH
OH
CC
C
H
CO
HHO
CH
O 2P
OC
H2
H OH
OH
CCH
CC
HO
OH
H
POC
H2
POC
H2
O
OH
NH
2
OH
CH
O 2P
C
HO
HC
HO
POC
H2
HO
CH
2CO
CH
2OP
O
OH
OO
PP
OH
CH
O 2P
CH
OH
CO
OP
POC
H2
C
HO
HP
OC
H 2C
OO
CO
O
OH
OH
OO
H
CO
O
CH
(CH
)C
H(O
H)C
HC
OS
-CoA
32
142
CH
(CH
)C
H(O
H)C
HC
OS
32
142
CH
(CH
)C
OC
HC
OS
-CoA
32
142
CH
(CH
)C
OC
HC
OS
-CoA
32
142
CH
(CH
)C
OS
-CoA
32
n+2
CH
(CH
)C
H=C
HC
OS
-CoA
32
14
CH
(CH
)3
2nC
H=C
HC
OS
-CoA
CH
(CH
)3
25
2C
H=C
HC
HC
OS
ACP
CH
(CH
)3
26C
H=C
HC
OS
ACP
CH
(CH
)3
26C
OC
HC
OS
ACP
2C
H(C
H)
32
62
2C
HC
HC
OS
ACP
CH
(CH
)3
22
22
CH
CH
CO
SAC
P
CH
CH
CH
CO
SAC
P3
22
CH
(CH
)3
26C
H(O
H)C
HC
OS
ACP
2
CH
CH
=CH
CO
.S-A
CP
3
CH
(CH
)3
22
2C
OC
HC
OS
ACP
CH
3CO
CH
CO
SAC
P2
CH
(CH
)3
2n
2C
OC
HC
OS
ACP
CH
(CH
)3
2n
2C
H(O
H)C
HC
OS
ACP
CH
(CH
)3
22
2C
H(O
H)C
HC
OS
ACP
AC
YL-
CoA
(Mito
chon
dria
)
CH
(CH
)C
HC
HC
OS
CoA
32
22
n
CH
(CH
)C
H=C
HC
OS
CoA
32
nC
H(C
HC
H(O
H)C
HC
OS
CoA
32
n
CH
(CH
)C
HC
HC
OS
CoA
32
22
2C
H(C
H)
CH
=CH
CO
SC
oA3
22
CH
(CH
)C
OC
HC
OS
CoA
32
2n
CH
CO
CH
CO
SC
oA3
2
CH
(CH
)C
H(O
H)C
HC
OS
CoA
32
22
CH
CH
(OH
)CH
CO
SC
oA3
2C
HC
H=C
HC
OS
CoA
3C
HC
HC
HC
OS
CoA
32
2
CH
CH
CH
CH
CO
SC
oA3
22
2Pe
nten
oyl-C
oAC
HC
HC
H=C
HC
OS
CoA
32
CH
CH
CH
(OH
)CH
CO
SC
oA3
22
CH
(CH
)C
OC
HC
OS
CoA
32
22
CH
CH
CO
CH
CO
SC
oA3
22
OH
OH
HO
OH
O O-
CH
O-P
O2
CH
CH
OH
CH
OH
22
O
CH
2
CH
2
R'-C
O-O
CH
O-C
O-R
O-P
OO-
HO
CH
CH
22N
H3
+P
OC
HC
H2
2NH
3+
CP
P-O
CH
CH
22N
H3
+
O
-
CH
O-C
O-R
2
CH
O P
2O
CH
CH
22N
H3
+
CH
CO
CH
CH
N(C
H)
32
23
3
HO
CH
CH
N(C
H)
22
33
+
CH
CH
2C
OO
(NH
) 3+
OH
OH
CH
CH
2C
OO
-(N
H) 3
+
CO
NH
2CH
CH
(NH
)CO
O2
3+
NH
OC
CO
NH
OC
N H
C H
HN 2
HC
CH
NN
CR
PH
N 2
CH
C
CH
OC
N
N
DP
NH
2
RP
PP
CH
C
CH
OC
N
N
NH
2
CC
CC
H RP
(P)
HC
NN
N
NN
H2
HN
CO
O2
P
(CH
)N
H2
32
HN
(CH
)N
H2
23
(CH
)N
H2
4 (CH
)N
H2
32
HN
(CH
)N
H2
24
CH
-SC
HC
HC
HN
H3
22
2
Ade
nosy
l
+
+C
H3
CH
3CH
CH
(NH
)CO
O3
++C N
HN
C
HC
H
CH
CH
(NH
)CH
OH
23
2+
C NH
NC
HC
H
CH
CH
(NH
)CH
OP
23
2C N
HN
C H
HC
CH
CO
CH
OP
22
+H
SC
HC
HC
H(N
H)C
OO
22
3
+
+S
CH
CH
CH
(NH
)CO
O2
23
CH
CH
(NH
)CO
O2
3
RP
CO
C-C
OO
OC
N
HN
CH
2.4.
1.23
CH
(CH
)C
H=C
HC
H(O
H)C
HC
HO
H3
212
2
NH
3+
CH
(CH
)C
H(O
H)C
HC
HO
H3
214
2
NH
3+
CH
(CH
)C
OC
HC
HO
H3
214
2
NH
3+
Gal
acto
seC
H(C
H)
CH
=CH
CH
(OH
)CH
CH
O-
32
122
NH
3+
4.1.
1.70
HN
CO
NH
22
OH
CC
HN
(CH
)2
33
+
C-C
H3
CO
CH
OC
ND
P
HN
DP
CP
P-O
CH
CH
N(C
H)
22
33
+O
CH
CH
N(C
H)
22
33
+
1.2.
1.41
UD
P-N
-Ac-
Mur
amat
e
O
OC
HC
H3 C
OO
-
NH
AC
HO
OPP
U
CH
OH
2 4.1.
3.20
O
OH
CH
3
HO
HO
OP
PG
2.7.
7.24
2.4.
1.22
2.7.
7.125.
1.3.
2
5.3.
1.4
Sedo
hept
ulos
e-PP
3.1.
1.28
4.2.
1.24
N
CH
2
CH
2
N
N N
CH
3 CH
3
CH
CH
CO
O
CH
CH
CH
2
HC 3 HC 3
HC 3H
C
CC HH Fe
CH
2C
H2
CO
O-
-
CH
3
CH
3
CH
2
CH
2CH
2
HC 3HC 3
N H NH
N H NH
CH
CH
HC 2
CCH2
H2
-
CH
2C
H2
CO
O
CH
2C
H2
CO
O-
HC 2
HC 2
CH
2
CH
2
OO
C
CO
O
HN 2
N H
-
-
CH
2
HC 2
HC 2
HC 2
H2
H2
CH
2C
H2
CH
2
CH
2
CH
2
CH
2 N H NH
N H NH
CO
O
CO
O
CO
OC
OO
CC
--
CH
2C
H2
CO
O
CH
2C
H2
CO
O-
-
--
OO
C- O
OC
-
CH
3
CH
3
HC 3
HC 3H
C 2
H2
H2
N H NH
N H NH
CH
2
CH
2
CH
2
CH
2
CH
2
CC
CO
O-
CH
2C
H2
CO
O
CH
2C
H2
CO
O-
-CO
O-
CO
O-
CH
C(O
H)C
HC
HO
32
2P
P
CH
CO
O2
OH
CC
OO
HO
CH
CO
O2
NH
2
HN
CN
HC
HC
OO
22
+N
H2
HN
CN
(CH
)CH
CO
O2
32
+N
H2
HN
CN
(CH
)CH
CO
O3
2P
-
+H
NC
NH
CO
NC
H2
CH
3
OO
CC
HC
HC
OO
2
HN
CN
HC
HC
HC
HC
H2
22
2
N(N
H) 3
+C
OO
CH
CO
OH
C
CH
2H
OC
H N
OO
CC
H(O
H)C
HC
H(N
H)C
OO
23
+
CH
CO
O
CH
2H
OC
H
HC 2
N H
NH
CH
CO
O
CH
2C
H2
CH
2
OO
CC
H(O
H)C
HC
OC
OO
2
NC
HC
OO
CH
2C
H2
CH
CH
CO
CO
O3
OH
CC
OO
+H
NC
ON
HC
HC
HC
HC
H2
22
2(N
H) 3C
OO
HN
OC
CH
CH
CH
22
2C
OO
(NH
) 3+
R-C
O-C
OO
+
CO
OR
-CH
(NH
) 3+
CO
OH
NO
CC
HC
H2
2(N
H3
+
OO
C-C
H-C
OS
CoA
CH
3
PO
OC
CH
CH
2C
OO
(NH
) 3+
OO
CC
HC
HC
HO
22
OH
CC
HC
H2
CO
O(N
H) 3
+
(CH
)N
CH
CH
(OH
)CH
CO
O3
32
2+
OH
CC
HC
HC
H2
2+
CO
O(N
H) 3
PO
OC
CH
CH
CH
22
+C
OO
(NH
) 3
OH
CC
HC
HC
HC
H2
22
CO
O(N
H) 3
+N
HC
HC
HC
HC
OO
22
CO
O
CH
CH
CH
CH
CH
22
22
CO
O(N
H) 3
+
HN
(CH
)2
42
CH
(NH
)CO
O3
CH
(NH
3++
(CH
)N
(CH
)3
32
3CH
CH
(NH
)CO
O2
3+
+
CH
2CH
OO
CC
N
HC
CH
-CO
OC
H2
CH2
CH
-CO
O O
OC
CN
HC 2
OO
CC
OC
HC
HC
HC
H-C
OO
22
2C
HC
H2
22
OO
CC
HC
HC
ON
H2
2O
OC
CH
CH
CH
CH
CH
-CO
O2
22
OO
CC
HC
HC
ON
H2
2C
H2
2
NH
3+
OO
CC
H-C
HC
HC
HC
HC
OO
22
2N
H3
+
NH
3+
(CH
)C
HC
(OH
)CH
32
2
CO
OH
CO
O(C
H)
CH
CH
CO
CO
O3
22
+(C
H)
CH
CH
32
2C
H(N
H)C
OO
3
HO
CH
CH
CO
O2C
H3
CH
CO
CO
OC
H3
CH
3C
HC
OC
(OH
)CH
33
CO
O
+P
OC
HC
HC
H(N
H)C
OO
22
3+
HO
CH
CH
CH
(NH
)CO
O2
23
+C
HC
HC
H(N
H)C
OO
22
3 O
OC
CH
CH
2CO
O2
+C
HS
H2
OO
CC
H(N
H)C
HC
HC
ON
HC
HC
ON
HC
HC
OO
32
22
HO
CH
C(C
H)
CO
CO
O2
32
HO
CH
C(C
H)
CH
(OH
)CO
O2
32
N
HC
HC
HC
OO
22
HO
CH
C(C
H)
CH
(OH
)CO
32)
23
2
N
HC
HC
HC
OO
22
OC
HC
(CH
)C
H(O
H)C
O2
32
P
CH
CH
32
CH
3 CH
+C
H(N
H)C
OO
3
CH
CO
C(O
H)C
HC
H3
23
CO
OC
HC
OC
OO
CH
CH
32
CH
3
NH
CH
CH
SH
2
CO
O
NH
CH
CH
CO
22
OC
H C
(CH
)C
H(O
H)C
O2
32
P
+C
HS
H2
OO
CC
H(N
H)C
HC
HC
ON
HC
HC
OO
32
2
+A
deno
syl
SC
HC
HC
H(N
H)C
OO
22
3
+S
CH
CH
CH
(NH
)CO
O2
23
+H
OS
CH
CH
(NH
)CO
O3
23
+ +S
-CH
CH
(NH
)CO
O2
3
S-C
HC
H(N
H)C
OO
23
+H
SC
HC
H(N
H)C
OO
23
1.1.
1.23
H
C NH
NC
HC
CH
CH
CO
O2 N
HC
OC
HC
HN
H2
22
+
H
C NH
NC
HC
CH
CH
(NH
)CO
O2
3
CH
CH
CH
CO
O2
2
NH
NC
H
OC
CC
HC
HC
OO
NH
NC
H
CH
CH
CO
O3
N H
OO
C
CH
-CO
OO
CNH
2C
H2
HN
CH
CH
CO
O2
22
HN
CH
22C
H3
CH
CO
OH
NC
ON
HC
HC
HC
OO
22
CH
3
CCO
CH RP
HC
NN
N
HN
CCCO
CH
HC
ONN
NR
P
CC
H
NNH
N 2
HC
CCO
CH
NNC
CC
H
NN
RP
HN 2 H
N 2C
O O
OP~
~ PO
O OOP
O
O
CH
2
N
N
N
N
O
OH
OHNH
2
HC
CH
N
N
N
N O
O PO
O
O
CH
2
OH
NH
2
HC
CH
CO
OC
O
NH
OC
N HC H
HN 2
NH
2
OO
C-C
H-C
HC
OO
2
HN
CO
CC
HNN
CR
PR
PH
N 2
OO
CC
CH
NR
P
N
CH
N 2
CH
=CH
CO
O
OH
CH
=CH
CO
OCH
CO
CO
O2
CH
2
P
CO
O
OH
O
O
O CO
O
O
CH
CO
O2
O CH
CO
O2
-OO
C
OC
H2
CH
2
OH
HC
P HO
CH
HC
OH
OC
CO
O
CO
OH
O
OH
OH
O
NH
2C
OO
OC
H
NH
CH
CO
CO
O2
NH
CH
O
CO
NH
2O
H
CH
CH
(NH
)CO
O2
3+
N
CO
OC
OO
N+C
OO
CO
OR
P
O
OH
OH
HO
OP
PU
CO
O
O
OH
NH
CO
CH
3
HO
OP
PU
CO
OC
HO
H2
O
OC
CH 2
NH
AC
HO
OP
PU
CO
OCH
OH
2
O
OH
HO
OH
OH
CO
O
OO
CC
HN
(CH
)2
32
Dim
ethy
lgly
cine
1.1.
99.1
1.2.
1.8
CO
OH
OH
OC
OO
O
HO
OH
CO
O
CH
(O)
PP
OC
H 2C
OO
CH
(OH
)H
OC
H 2C
OO
CO
O
C
H(O
)P
HO
CH 2
CO
O
CH
=C(O
)2
PC
OO
CO
NH
2
Rib
ose
-O -
P - O
- P
- O- A
deno
sine
(P)
+ NO O
O O
+
CO
O
NR
ibos
e - O
- P
- O -
P - O
-A
deno
sine
O O
O O
II
II
OHOCH
CH
2C
OO
(NH
) 3+
Epin
ephr
ine
(Adr
enal
ine)
Nor
epin
ephr
ine
(Nor
adre
nalin
e)
Nor
met
epin
ephr
ine
(Nor
met
adre
nalin
e)
HO
CH
CH
N(C
H)
22
33
+
Ade
nosy
l+
+SC
HC
HC
H(N
H)C
OO
22
3C
H3
(CH
)N
(CH
)3
32
3CH
CH
(NH
)CO
O2
3+
+O
H
OO
CC
HC
HC
HC
OS
CoA
22
2
OO
CC
HC
HC
HN
H2
22
2
OO
CC
HC
HC
HC
OC
OO
22
2 O
OC
CH
CH
CH
CH
22
2C
OO
CO
O(N
H) 3
++
HO
H
HO
H
HH
OH
HO
H
Pros
tagl
andi
n PG
E2
OH
HO
CH
2C
CC
OC
CO
O
OH
H OH
HH
-
CO
O
OR'
-CO
-OCHC
HO
-CO
-R2
CH
O P
OC
MP
2O
CH
CH
N(C
H)
22
3+
OH
OC
H
CH
OP
O2
CH
OH
2
O-
CH
OP
O2
OC
HO
CH
=CH
R2
CH
CH
N(C
H)
22
33
+
O-
CH
OP
O2
OR
'-CO
-OC
HC
HO
-CO
-R2
3.1.
1.32
CH
CH
N(C
H)
22
33
+
O-
OH
OC
H
CH
OP
O2
CH
O-C
O-R
2
CH
CH
N(C
H)
22
33
+
O-
CH
CH
(NH
)CO
O2
3+
+C N
HN
C
HC
H
CH
CH
(NH
)CH
O2
3
HS
11-cis
-Ret
inal
Pi
AD
P
NA
DP
+
GD
P-M
annu
rona
te
Man
nose
-6-P
Deh
ydro
-sh
ikim
ate
Shik
imat
e
RN
A
d-G
DP
d-C
TP
GUA
NO
SIN
E-P
(GM
P)
ß-A
lani
ne
P-R
ibos
yl-A
MP
P-R
ibul
osyl
form
imin
o5-
amin
oim
idaz
ole-
carb
oxam
ide-
RP
Imid
azol
eac
etol
-P
HS
HSO
-
PAN
TOTH
ENAT
E
3-Is
opro
pyl-
mal
ate
Succ
inic
sem
iald
ehyd
e
2.4.
1.17
Dia
cyl
glyc
erol
2.3.
1.6
1.14
.12.
1
1.4.
4.2
CH
CH
O3
3.5.
4.19
4.2.
1.19
3.3.
1.1
4.1.
1.12
4.1.
2.5
CO
O-
2O
HC
CH
2.1.
4.1
2.4.
99.7
5.1.
3.12
1.1.
1.13
2
4.2.
1.46
2.7.
1.7
2.4.
1.29
2.4.
1.21
2.4.
1.13
2.4.
1.1
etc.
5.4.
2.2
2.7.
1.6
2.7.
7.10
3.1.
1.18
4.1.
1.34
2.7.
1.47
2.7.
1.16
3.1.
3.9
AD
P
P-G
luco
nola
cton
e
1.1.
1.44
O
OO
HH
O
OH
CH
O 2P
PHEN
YLA
LAN
INE
TYR
OSI
NE
TRYP
TOPH
AN
INO
SIN
E-P
(IMP)
THYM
IDIN
E-P
HIS
TID
INE
UR
IDIN
E-tr
ipho
spha
te(U
TP)
CYS
TIN
EC
YSTE
INE
ISO
LEU
CIN
E
LEU
CIN
E
LYSI
NE
OR
NIT
HIN
E
AR
GIN
INE
HYD
RO
XYPR
OLI
NE
PH
OS
PH
ATID
YL
SE
RIN
EPh
osph
atid
ylin
osito
l
LEC
ITH
IN
SPH
ING
OM
YELI
N
STER
OID
S
Preg
neno
lone
2.7.
6.1
2.4.
2.14
6.3.
4.7
5.3.
1.9
3.1.
3.11
1.2.
1.13
2.7.
2.3
H OH
OH
CC
C
H
CO
OH
CH
HOH
PO
CH
2C
HO 2
P
5.4.
2.1
AD
P4.2.
1.11
Endo
plas
mic
Ret
icul
um
1.1.
1.10
0
3.1.
1.3
Phos
phat
idat
e
2.3.
1.39
4.2.
1.17
4.2.
1.17
4.2.
1.55
1.1.
1.79
1.2.
1.21
1.4.
3.8
1.1.
1.32
2.7.
1.36
2.7.
4.2
4.1.
1.33
2.5.
1.1
2.5.
1.10
2.7.
8.5
2.7.
8.1
4.1.
1.65
2.7.
7.14
1.3.
99.7
PO
OC
H(C
H)
CH
=CH
CH
(OH
)CH
CH
O3
212
2
NH
Acy
l
CH
CH
N(C
H)
22
33
+
O-
3.5.
1.23
1.13
.11.
21
2.5.
1.32
1.1.
1.10
5
2.4.
2.19
1.2.
1.32
MET
HIO
NIN
E
4.1.
3.27
4.2.
1.51
1.14
.17.
1
1.14
.18.
1
1.14
.13.
11
Gly
cina
mid
e-rib
osyl
-P
4.2.
1.22
3-O
xohe
xano
yl-C
oA
THR
EON
INE
1.2.
1.25
1.2.
1.25
1.2.
1.25
1.5.
1.7
- 10
GLU
TAM
ATE
2.3.
1.38
ATP
NA
DH
SUC
RO
SE
AD
ENO
SIN
E-P
(AM
P)
Tria
cylg
lyce
rol
FAT
RN
A
CH
3
CH
2
OC
-CO
OO
H
CO
O
CH
CH
2C
OO
(NH
) 3+
GLY
CO
PRO
TEIN
SG
AN
GLI
OSI
DES
MU
CIN
S
4.1.
2.-
2.6.
1.-
GLU
CO
SE
O-A
cyl-c
arni
tine
O-A
cyl-c
arni
tine
OH
O-
-
R-CO
-OCH
R'-C
O-O
CH
R'-C
O-O
CH
OH
CO
-CO
-R
C
HC
H(O
H)C
HO
-P-O
CH
22
2
CH
O-C
O-R
’2
OR'
-CO
-OCH
O-
CH
O-C
O-R
2
CH
O-P
O2
O-
2.7.
8.11
HN
CH
CH
CH
CH
22
22
CO
O(N
H) 3
+
2.3.
1.20
3.1.
3.4
2.7.
1.10
7
NH
2+
+H
NC
NH
CH
CH
CH
CH
22
22
CO
O(N
H) 3
H OH
HO
H
CC
CC
O
OH
H
HO
CH
2C
HO
H2
R-C
H2C
OO
CH
O-C
O-R
2
CH
O-C
O-R
"2
R’-C
O-O
CH
OH
O
C
HC
HN
H2
3+
OR'
-CO
-OCH
O-
CH
O-C
O-R
2
CH
O P
O2
CO
O
OO
CC
HC
HC
H2
2C
OO
(NH
) 3
+C
HC
H(O
H)C
H(N
H)C
OO
33
O
OH
HO
OH
OH
CH
OH
2C
HO
H2
NH
CH
O-C
O-R
2
1.3.
1.13
4.1.
1.28
Mal
onic
sem
i-al
dehy
de
2.7.
2.4
2.1.
3.3
3.5.
1.2
6.3.
1.2
6.3.5.
5
Car
bohy
drat
esB
iosy
nthe
sis
Deg
rada
tion
Am
ino
Aci
dsB
iosy
nthe
sis
Deg
rada
tion
Lipi
ds Bio
synt
hesi
sD
egra
datio
n
Purin
es &
Pyrim
idin
esB
iosy
nthe
sis
Deg
rada
tion
Bio
synt
hesi
sD
egra
datio
nVi
tam
ins
Co-
enzy
mes
& H
orm
ones
Pent
ose
Phos
phat
e Pa
thw
ay
Phot
osyn
thes
is D
ark
Rea
ctio
ns
CO
MPA
RTM
ENTA
TIO
NTh
e "B
ackb
one"
of m
etab
olis
m in
volv
esG
LYC
OLY
SIS
in th
e C
YTO
PLA
SM
,th
eTC
A C
YC
LE (m
ainl
y) in
the
Mito
chon
dria
l mat
rixan
d AT
P F
OR
MAT
ION
spa
nnin
g th
eM
ITO
CH
ON
DR
IAL
INN
ER
ME
MB
RA
NE
An
elec
tron
flow
(an
elec
tric
curr
ent)
gene
rate
d fro
mN
AD
H a
nd U
QH
2dr
ives
the
trans
loca
tion
of p
roto
nsfro
m th
e m
atrix
to th
e in
term
embr
ane
spac
e.Th
ere
trolo
catio
n of
thes
e pr
oton
s th
roug
h th
e F0
sub
units
ofAT
P sy
ntha
se to
the
mat
rix th
en s
uppl
ies
the
ener
gyne
eded
to fo
rm A
TP fr
om A
DP
and
phos
phat
e
Ele
ctro
n Fl
owP
roto
n Fl
ow
Sm
all N
umbe
rs (
eg. 2
.4.6
.7) r
efer
to th
e IU
BM
BE
nzym
eC
omm
issi
on (E
C) R
efer
ence
Num
bers
of E
nzym
es
LEG
END
Hum
an M
etab
olis
m is
iden
tifie
d as
far p
ossi
ble
by b
lack
arr
ows
Bio
synt
hesi
sD
egra
datio
n
HEM
OG
LOB
INC
HLO
RO
PHYL
L
ATP
TRANSLOCATED
PRO
TON
S
2.7.
1.1AT
P2.
7.1.
2
8
Advancements in Enzyme-Based Fuel Cell Batteries, Sensors and Emissions Reduction Strategies
In addition to synthetic polymer supports, Dr. Minteer and her collaborator, Dr. Michael Cooney of the University of Hawaii, have immobilized dehydrogenases on macroporous chitosan scaffolds. The scaffolds were fabricated from solutions of native and hydrophobically modified chitosan polymers through the process of thermally induced phase separation. The hydrophobically modified chitosan is proposed to possess amphiphilic micelles into which the enzyme can be encapsulated and retained.
One of Dr. Minteer’s basic biofuel cell batteries employs an ethanol/alcohol dehydrogenase system to generate a proton gradient across the conductive membrane. They have also refined these dehydrogenase systems by replacing traditional NAD(H) cofactor-dependent dehydrogenases with pyrroloquinoline quinone(PQQ)-dependent dehydrogenases to improve efficiency. Other multienzyme coupled systems use classical glycolytic and Krebs cycle enzyme systems and corresponding metabolic substrates to generate power.
Dr. Minteer’s lab has also utilized mitochondria to generate current by metabolism of classic cellular energy sources. The resulting electrons are shuffled through the electron transport chain where they reduce oxygen at cytochrome c oxidase and combine with the protons from oxidation to form water. During this metabolic process it is possible for cytochrome c to undergo direct electron transfer to a carbon electrode and complete oxygen reduction at a platinum cathode.
Taking advantage of the fact that nitroaromatics can decouple the inhibition of pyruvate metabolism, mitochondria-modified electrodes have also been used to electrochemically sense the presence of nitroaromatic explosive compounds. These oligomycin inhibited mitochondria-modified electrodes were employed as the bioanode in a pyruvate/air biofuel cell. This concept could be used as a traditional electrochemical sensor or as a self-powered sensor.
Dr. Minteer's Nafion-based immobilization technology is also addressing the reduction of fluegas emissions from coal-fired power plants using carbonic anhydrase to sequester CO
2.
Advancements in Enzyme-Based Fuel Cell Batteries, Sensors and Emissions Reduction StrategiesDr. Shelley Minteer, Ph. D.
Sigma® Life Science and Aldrich Materials Science merge to help researchers completely rethink tomorrow’s immobilized enzyme technologies.
Today’s fuel cells and batteries lack the ability to produce electrical power for the long periods of time we desire and commonly incorporate toxic or precious metals to produce and store their energy.
Enzyme-based fuel cells have potentially higher energy density than traditional batteries using much more environmentally compatible materials. While the idea of enzyme-based biofuel cells is not a new concept, recent developments have captured the interests of the research community. Dr. Shelley Minteer at Saint Louis University Department of Chemistry is one of the pioneers in this area. Dr. Minteer and her team have developed a new enzyme immobilization technology that has begun to revolutionize the way we think about using enzymes for long-term catalytic applications.
Dr. Minteer’s enzyme immobilization strategy encapsulates and stabilizes Sigma enzymes in modified Nafion® polymer matrices from Aldrich. The efficacy of Dr. Minteer’s immobilized enzymes can be measured in years compared to days for other biofuel cell technologies. Dr. Minteer has successfully demonstrated the use of several metabolic fuels such as glycerol, fatty acids, ethanol and other alcohols, pyruvate and glucose to provide the fuel source, while a wide variety of enzymes and coupled multienzyme systems provide the catalytic power to convert the fuel to electrical current.
Enzymes immobilized in Nafion® membrane are encapsulated in the polymer resulting in increased stability while retaining active site availability and optimized orientation.
Order sigma.com/order Technical service sigma.com/techinfo sigma.com/lifescience 9
(10) A.E. Blackwell, M.J. Moehlenbrock, J.R. Worsham, and S.D. Minteer, “Comparison of Electropolymerized Thiazine Dyes as an Electrocatalyst in Enzymatic Biofuel Cells and Self Powered Sensors,” Journal of Nanoscience and Nanotechnology, 2009, 9, 1719–1726.
(11) M. Cooney, V. Svoboda, C. Lau, G. Martin, and S.D. Mint-eer, “Enzymatic Biofuel Cells,” Energy and Environmental Science, 2008, 1, 320–337.
(12) M.J. Cooney, J. Petermann, C. Lau, S.D. Minteer, “Charac-terization and Evaluation of Hydrophobically Modified Chitosan Scaffolds: towards design of enzyme immo-bilized flow-through electrodes,” Carbohydrate Polymers, 2009, 75, 428–435.
(13) G. Martin, S. Minteer, and M.J. Cooney, “Spatial distribu-tion of malate dehydrogenase in amphiphilic chitosan scaffolds,” Applied Materials and Interfaces, 2009, 1(2) 367–372.
(14) C. Hettige, S.D. Minteer, and S. Calabrese Barton, “Simula-tion of Multi-Step Enzyme Electrodes,” ECS Transactions, 2008, 13/21, 99–109.
(15) K. Sjoholm, M.J. Cooney, and S.D. Minteer, “Effects of Degree of Deacetylation on Enzyme Immobilization in Hydrophobically Modified Chitosan,” Carbohydrate Polymers, 2009, 77, 420–424.
(16) G. Martin, S.D. Minteer, and M.J. Cooney, “Fluorescence characterization of chemical microenvironments in hy-drophobically modified chitosan,” Carbohydrate Polymers, 2009, 77, 695–702.
(17) D. Sokic-Lazic and S.D. Minteer, “Pyruvate/air enzymatic biofuel cell capable of complete oxidation,” Electrochemi-cal and Solid-State Letters, 2009, 12(9), F26–F28.
(18) M.C. Beilke, T.L. Klotzbach, B.L. Treu, D. Sokic-Lazic, J. Wildrick, E.R. Amend, L.M. Gebhart, R.L. Arechederra, M.N. Germain, M.J. Moehlenbrock, Sudhanshu, and S.D. Mint-eer, “Enzymatic Biofuel Cells,” in Micro-Fuel Cells: Principles and Applications, Elsevier, 2009, 179–241.
Acetyl CoA
Pyruvate Deh.
Citrate Synthase
Aconitase
Isocitrate Deh.
α-Ketoglutarate Deh.
Succinyl-CoA SynthetaseSuccinate Dehydrogenase
Fumarase
Malate Dehydrogenase
Oxa
loac
etat
e Isocitrate
α-Ketoglutarate
Succinyl-CoA
Succinate
Fumarate
Malate
Citrate
GDP
GTP
FAD
FADH
NADH
NAD+
NADH
NAD+
NADPH
NADP+
NADPH
NADP+
2CO
2CO
2
p
Mo
dified
Nafio
n® M
emb
rane an
d En
zymes
Poly(m
ethylen
e green
)
Carb
on
Paper
Platinum
Potentiostat
FuelSolution
Pyru
vate
Anode NRE 212Nafion®
Cathode
O2
H2O
An an example of one of Dr Minteer’s fuel cells; utilizing pyruvate as the initial fuel source, this fuel cell incorporates a multi-enzyme coupled system that generates a proton gradient source of energy analogous to that produced in vivo in the Kreb’s Cycle.
References(1) S.D. Minteer, B.Y. Liaw, and M.J. Cooney, “Enzyme-based
biofuel cells,” Current Opinions in Biotechnology, 2007, 18, 228–234.
(2) C.M. Moore, N.L. Akers, and S.D. Minteer, “Improving the Environment for Immobilized Dehydrogenase Enzymes by Modifying Nafion with Tetraalkylammonium Bro-mides,” Biomacromolecules, 5, 2004, 1241–1247.
(3) M.J. Cooney, M. Windmeisser, B.Y. Liaw, C. Lau, T. Klotz-bach, and S.D. Minteer, “Design of Chitosan Gel Pore Structure: Towards Enzyme Catalyzed Flow-Through Electrodes,” Journal of Materials Chemistry, 2008, 18, 667–674.
(4) P. Atanassov, C. Apblett, S. Banta, S. Brozik, S. Calabrese Barton, M. Cooney, B.Y. Liaw, S. Mukerjee, and S.D. Minteer, “Enzymatic Biofuel Cells,” Electrochemical Society Interface, 16, 2007, 28–31.
(5) T.L. Klotzbach, M. Watt, Y. Ansari, and S.D. Minteer, “Improving the microenvironment for enzyme immo-bilization at electrodes by hydrophobically modifying chitosan and Nafion polymers,” Journal of Membrane Science, 2008, 311, 81–88.
(6) V. Svoboda, M. Cooney, B.Y. Liaw, S. Minteer, E. Piles, D. Lehnert, S.C. Barton, R. Rincon, and P. Atanassov, “Stan-dardized characterization of biocatalytic electrodes,” Electroanalysis, 2008, 20, 1099–1109.
(7) B.L. Treu, R. Arechederra, and S.D. Minteer, “Bioelectroca-talysis of Ethanol via PQQ-Dependent Dehydrogenases Utilizing Carbon Nanomaterial Supports,” Journal of Nanoscience and Nanotechnology, 2009, 9, 2374–2380.
(8) B.L. Treu and S.D. Minteer, “Isolation and Purification of PQQ-dependent Lactate Dehydrogenase from Gluconobacter and Use for Direct Electron Transfer at Carbon and Gold Electrodes,” Bioelectrochemistry, 2008, 74, 71–77.
(9) D. Sokic-Lazic and S.D. Minteer, “Citric acid cycle biomim-ic on a carbon electrode,” Biosensors and Bioelectronics, 2008, 24, 945–950.
(19) M. J. Moehlenbrock, R. L. Arechederra, K. H. Sjoholm, and S.D. Minteer, “Analytical Techniques for Character-izing Enzymatic Biofuel Cells,” Analytical Chemistry, 2009, 81(23), 9538–9545.
(20) P. Addo, R. Arechederra, and S. D. Minteer, “Evaluating En-zyme Cascades for Methanol/Air Biofuel Cells Based on NAD-dependent Enzymes,” Electroanalysis, 2010, 22(7-8), 807–812.
(21) R. Rincoln, M. Germain, K. Artyushkova, M. Mojica, M. Germaine, P. Atanassov, and S.D. Minteer, “Structure and Electrochemical Properties of Electrocatalysts for NADH Oxidation,” Electroanalysis, 2010, 22(7–8), 799–806.
(22) W. Gellett, M. Kesmez, J. Schumacher, N. Akers, and S.D. Minteer, “Biofuel Cells for Portable Power,” Electroanalysis, 2010, 22(7–8), 727–731.
(23) D. Sokic-Lazic, R.L. Arechederra, B.L. Treu, and S.D. Minteer, “Oxidation of Biofuels: Fuel Diversity and Ef-fectiveness of Fuel Oxidation through Multiple Enzyme Cascades,” Electroanalysis, 2010, 22(7–8), 757–764.
(24) C. Lau, G. Martin, S.D. Minteer, and M.J. Cooney, “Devel-opment of a Chitosan Scaffold Electrode for Fuel Cell Applications,” Electroanalysis, 2010, 22(7–8), 793–798.
(25) R. Arechederra, B.L. Treu, and S.D. Minteer, “Develop-ment of Glycerol/Oxygen Biofuel Cells,” Journal of Power Sources, 173, 2007, 156–161.
(26) R. Arechederra and S.D. Minteer, “Organelle-Based Bio-fuel Cells: Immobilized Mitochondria at Carbon Paper Electrodes,” Electrochimica Acta, 2008, 53, 6698–6703.
(27) M. Germain, R. Arechederra, and S.D. Minteer, “Nitroaro-matic Actuation of Mitochondrial Bioelectrocatalysis for Self Powered Explosive Sensors,” Journal of the American Chemical Society, 2008, 130(46), 15272–15273.
(28) R. Arechederra, K. Boehm, and S.D. Minteer, “ Mitochon-drial Bioelectrocatalysis for Biofuel Cell Applications,” Electrochimica Acta, 2009, 54, 7268–7273.
10
Selected Enzymes for Biofuel Cell ResearchEnzyme-based biofuel cells are incorporating a wide variety of enzymes. Sigma-Aldrich manufactures hundreds of enzymes, many of which may have potential applications in biofuel cells. For a complete list of enzymes, data sheets, assay protocols, and other enzyme-related technical resources visit the web-based Sigma Enzyme Explorer at sigma-aldrich.com/enzymeexplorer. The Enzyme Explorer also features the IUBMB on-line metabolic pathway chart with over 500 links to enzymes, substrates and cofactors.
The following products are only a small sample of the enzymes available from Sigma-Aldrich of potential use in biofuel cell research.
▼ Alcohol Dehydrogenase
ADHAlcohol Dehydro genase fromParvibaculum lavamentivorans
recombinant, expressed in Escherichia coli, activity: ≥40.0 units/mg
One unit corresponds to the amount of enzyme which reduces 1 μmole ethyl acetate per minute at pH 7.0 and 30 °C.75449-1ML 1 mL75449-5ML 5 mL
Alcohol Dehydro genase fromSaccharomyces cerevisiaeAlcohol:NAD+ oxidoreductase; Alcohol Dehydro-genase from yeast [9031-72-5]A 141 kDa tetramer containing 4 equal subunits. The active site of each subunit contains a zinc atom. Each active site also contains 2 reactive sulfhydryl groups and a histidine residue.
Isoelectric point: 5.4–5.8
Optimal pH: 8.6–9.0
Substrates: Yeast ADH is most active with ethanol and its activity decreases as the size of the alcohol increases or decreases. Branched chain alcohols and secondary alcohols also have very low activity.
KM (ethanol) = 2.1 × 10-3 M
KM (methanol = 1.3 × 10-1 M
KM (isopropanol) = 1.4 × 10-1 M
Selected Enzymes for Biofuel Cell Research
Inhibitors: Compounds that react with free sulfhydryls, including N-alkylmaleimides and iodoacetamide.
Zinc chelator inhibitors, including 1,10-phenanthroline, 8-hydroxyquinoline, 2,2’-dipyridyl, and thiourea.
Substrate analogue inhibitors, including β-NAD analogs, purine and pyrimidine derivatives, chloroethanol, and fluoroethanol.
Extinction Coefficient: E1% = 14.6 (water, 280 nm)
One unit will convert 1.0 μmole of ethanol to acetaldehyde per min at pH 8.8 at 25 °C.
�lyophilized powder (contains buffer salts), activity: ≥300 units/mg protein
Solids containing ≤ 2% citrate buffer salts suitable for conventional determination of β-NAD, β-NADH, ethanol and acetaldehyde
Contains bound β-NAD and β-NADH and is not suitable for the recycling microassay of β-NAD and β-NADH. If you require ADH for this purpose, see Cat. No. A3263.
A7011-7.5KU 7500 unitsA7011-15KU 15000 unitsA7011-30KU 30000 unitsA7011-75KU 75000 unitsA7011-150KU 150000 unitsA7011-300KU 300000 units
activity: ≥300 units/mg proteinSolids containing <2% citrate buffer salts suitable for recycling micro-assay of β-NAD and β-NADH
A3263-7.5KU 7500 unitsA3263-15KU 15000 unitsA3263-30KU 30000 unitsA3263-75KU 75000 unitsA3263-150KU 150000 units
Alcohol Dehydro genase, Deinococcusradiodurans, recombinant from E. coliADH[9031-72-5]
activity: ≥10000 units/mLOne unit corresponds to the amount of enzyme which reduces 1 μmole ethyl-2-oxo-4-phenylbutyrate per minute at pH 7.0 and 37 °C
16892-1ML 1 mL16892-5ML 5 mL
Alcohol Dehydro genase, NADP+
dependent from ThermoanaerobiumbrockiiAlcohol:NADP+ oxidoreductase; TBADH[9028-12-0]An extremely thermostable enzyme with broad substrate specificity for alcohols, ketones and acetaldehyde.
One unit will oxidize 1.0 μmole of 2-propanol to acetone per min at pH 7.8 at 40 °C in the presence of NADP+.
lyophilized powder, activity: 5–15 units/mg protein
Contains phosphate buffer salts and dithioerythritolA8435-100UN 100 unitsA8435-250UN 250 units
lyophilized powder, activity: 30–90 units/mg protein
Purified
Contains sodium citrate and dithioerythritol.A9287-100UN 100 units
Alcohol Dehydrogenase ▲
Bilirubin Oxi dase from MyrotheciumverrucariaBilirubin:oxygen oxidoreductase [80619-01-8]
lyophilized powder, activity: 15–65 units/mg protein
One unit will oxidize 1.0 μmole of bilirubin per min at pH 8.4 at 37 °C.
B0390-25UN 25 unitsB0390-100UN 100 units
Order sigma.com/order Technical service sigma.com/techinfo sigma.com/lifescience 11
Cyto chrome c Oxi dase from bovine heartFerro cyto chrome-c:oxygen oxidoreductase, Com plex IV; EC 1.9.3.1[9001-16-5]Cytochrome c oxidase is the principal terminal oxidase of high oxygen affinity in the aerobic metabolism of all animals, plants, yeasts and some bacteria.
Supplied as a solution in 25 mM Tris-HCl buffer, pH 7.8, 5 mM EDTA, and 39 mM sodium dodecyl maltoside.
activity: ≥20 units/mg protein
One unit of cytochrome c oxidase will oxidize 1.0 μmole of ferrocytochrome c per min. at 25 °C at pH 6.0.C5499-250UG 250 μg
d-Fructose Dehydro genase fromGluconobacter industriusd-Fructose:(acceptor) 5-oxidoreductase[37250-85-4]
lyophilized powder, activity: 400–1,200 units/mg protein
Lyophilized powder containing citrate-phosphate buffer salts, TRITON® X-100, and stabilizer
One unit will convert 1.0 μmole d-fructose to 5-ketofructose per min at pH 4.5 at 37 °C.F5152-250UN 250 units
Glucose Dehydro genase from calf liverβ-d-Glucose: NAD[P]+ 1-oxidoreductase[9028-53-9]
activity: ~15 units/g solidCrude powder
One unit will oxidize 1.0 μmole of β-d-glucose to d-glucono-δ-lactone per min at pH 7.6 at 25 °C.G5625 Inquire
Glucose Dehydro genase fromPseudomonas sp.[9028-53-9]
powder, activity: ≥200 units/mgOne unit corresponds to the amount of enzyme which will oxidizes 1 μmole β-D-glucose to D-glucono-δ-lactone per minute at pH 8.0 and 37 °C19359-10MG-F 10 mg
Glucose Dehydro genase fromThermoplasma acidophilumβ-D-Glucose:NAD[P]+ 1-oxidoreductase[9028-53-9]
recombinant, expressed in Escherichia coli, ammonium sulfate suspension, activity: ≥100 units/mg protein (glucose substrate), activity: ≥50 units/mg protein (galactose substrate)
A thermostable enzyme with resistance to organic solvents. Enzyme also shows substantial activity with d-galactose as substrate.
Suspension in 2.8 M (NH4)2SO4, 50 mM phosphate buffer, pH 7.0
One unit will oxidize 1.0 μmole of d-glucose to d-glucono-δ-lactone per min at pH 7.0 at 37 °C in the presence of NADP+.G5909-100UN 100 unitsG5909-500UN 500 units
Glucose Oxi dase from Aspergillus nigerG.Od.; GOx; β-d-Glucose:oxygen 1-oxidoreductase [9001-37-0]Molecular Weight: 160 kDa (gel filtration)pI: 4.2
Extinction coefficient: E1% = 16.7 (280 nm)
Glucose oxidase from Aspergillus niger is a dimer consisting of 2 equal subunits with a molecular mass of 80 kDa each. Each subunit contains one flavin adenine dinulceotide moiety and one iron. The enzyme is a glycoprotein containing ~16% neutral sugar and 2% amino sugars. The enzyme also contains 3 cysteine residues and 8 potential sites for N-linked glycosylation.
Glucose oxidase is capable of oxidizing d-aldohexoses, monodeoxy-d-glucoses, and methyl-d-glucoses at varying rates.
The pH optimum for glucose oxidase is 5.5, while it has a broad activity range of pH 4–7. Glucose oxidase is specific for β-d-glucose with a KM of 33–110 mM.
Glucose oxidase does not require any activators, but it is inhibited by Ag+, Hg2+, Cu2+, phenylmercuric acetate, and p-chloromercuribenzoate. It is not inhibited by the nonmetallic SH reagents: N-ethylmaleimide, iodoacetate, and iodoacetamide.
Glucose oxidase can be utilized in the enzymatic determination of d-glucose in solution. As glucose oxidase oxidizes β-d-glucose to d-gluconolactate and hydrogen peroxide, horseradish peroxidase is often used as the coupling enzyme for glucose determination. Although glucose oxidase is specific for β-d-glucose, solutions of d-glucose can be quantified as α-d-glucose will mutorotate to β-d-glucose as the β-d-glucose is consumed by the enzymatic reaction.
One unit will oxidize 1.0 μmole of β-d-glucose to d-gluconolactone and H2O2 per min at pH 5.1 at 35 °C, equivalent to an O2 uptake of 22.4 μl per min. If the reaction mixture is saturated with oxygen, the activity may increase by up to 100%.
lyophilized powder, activity: 100,000–250,000 units/g solid (without added oxygen)
May contain traces of amylase, maltase, glycogenase, invertase, and galactose oxidase.
Protein determined by biuret
G7141-10KU 10000 unitsG7141-50KU 50000 unitsG7141-250KU 250000 unitsG7141-1MU 1000000 unitsG7141-2.5MU 2500000 units
▼ Laccase[80498-15-3]
Laccase from Rhus verniciferaBen zene diol:oxygen oxidoreductase
crude acetone powder, activity: ≥50 units/mg solid
One unit will produce a ΔA530 of 0.001 per min at pH 6.5 at 30 °C in a 3 mL reaction volume using syringaldazine as substrate.L2157-10KU 10000 units
Laccase from Trametes versicolor
former nomenclature: Coriolus versicolor
powder, activity: >20 units/mgOne unit corresponds to the amount of enzyme which converts 1 μmole of catechol per minute at pH 4.5 and 25 °C53739-100MG-F 100 mg53739-1G-F 1 g
powder, activity: ≥0.5 units/mgOne unit corresponds to the amount of enzyme which converts 1 μmole of catechol per minute at pH 6.0 and 25 °C38429-1G 1 g38429-10G 10 g
Laccase ▲
12
Enzymes and Reagents for Ethanol Research
Enzymes and Reagents for Ethanol ResearchEnzymes for Lignocellulosic Ethanol Research
Middle Lamella
Pectin
Plant Cell Wall
Hemicellulose
Cellulose Microfibril
Cell Wall
Plasma Membrane
Visit the Enzyme Explorer Assay Library
Features over 600 detailed procedures for measuring enzyme activity and related metabolites. The Library is the result of over ten years of in-house work on
analytical procedures developed by Sigma-Aldrich® scientists.
Visit sigma.com/enzymeexplorer
Enzymes for Lignocellulosic Ethanol ResearchSigma-Aldrich is committed to helping unlock today's challenge of releasing the energy of glucose that nature has cleverly locked into lignocellulosic biomass. To the untrained eye, starch and cellulose structures appear almost identical. Yet the barriers between cellulosic biomass hydrolysis and ethanol production appear have proven to be orders of magnitude more challenging than with starch derived biomass.
Although many of the biochemical aspects of these challenges are well understood, they remain an enigma of nature. The two main, and closely related hindrances to the enzymatic hydrolysis of cellulosic polymers are:
How do we physically dismantle biomass on a molecular level to yield cellulosic polymers available to hydrolysis by cellulase and other glycolytic enzymes? How do we
penetrate the barrier posed by the closely integrated network of lignins surrounding cellulose microfibrils?
Order sigma.com/order Technical service sigma.com/techinfo sigma.com/lifescience 13
O
OCH2OH
OH
OHO
CH2OH
OH
OH
OH
O
OCH2OH
OH
OH
O
OCH2OH
OH
OH
O
OCH2OH
OH
OHO
OH
CH2OH
OH
OH
O
endo-1,4-β-D-Glucanase
Cellobiosidase II
Cellobiosidase I
b-Glucosidase
O
O
OCH2OH
OH
OHO
CH2OH
OH
OH
O
O
CH2OH
OH
OH
O OCH2OH
OHOH
O
O
OH
OH
O
Cellulase
CellulaseLaminaranase
Cellulase
b-(1-4)-D-glucose
b-(1-4)-D-glucose
b-(1-4)-D-glucose b-(1-3)-D-glucose
CH2OH
O
O
OH
OHO
OH OH
O
O
OH
OHO
OH
OH
O
O
OXylanase
Cellulase catalyzes the endohydrolysis of β−(1→4)-d-glucosidic linkages in cellulose, lichenin and cereal β-d-glucans
Most cellulase preparations contain various classes of cellulases and related activities.
The endo-β-(1• →4)-d-glucanases (EGs) cleave cellulose in its internal non-terminal regions, yielding oligosaccharides.
The two forms of cellobiohydrolases (CBH) are •considered exo-β-(1→4)-d-glucanases, releasing cellobiose disaccharides from the cellulose chain reducing end (CBHI), and non-reducing end (CBHII).
β-Glucosidase is an exohydrolase that yields glucose •monosaccharides from soluble oligosaccharaides such as cellobiose.
Other activities that can be found in cellulase preparations include xylanase, hemicellulase, and laminarinase.
Cereal β-Glucan is a polymer of β-(1→4)- d-glycopyranosyl units occupying as predominantly cellotriose and cellotetraose separated by single β-(1→3)-d-glycopyranosyl units. Crosslinking can occur within the consecutive cellotriose regions.
Hemicelluloses are a group of plant-derived heteropoly-saccharides associated with cellulose and lignin. The most common hemicelluloses are xylan, glucuronoxylan, arabinoxylan, glucomannan and xyloglucan. In angio-sperms, the principal hemicellulose component, xylan, is a polymer of β−(1→4)-d-xylopyranose. In arabinoxylan, branching occurs at the C2 & C3 postions with a-L-arab-inofunaose. Glucuronoxylan, also found in angiosperms, has the xylan backbone with 4-0 methylglucuronic acid branching. In addition, arabinose branching as well as acetylation may be present. Gymnosperms contain glucomannans comprised primarily of d-mannosyl and d-glucosyl residues..
Hemicellulase preparations are typically a mixture of •glycolytic enzymes containing xylanase, mananase and other activities.
Xylanase catalyzes the endohydrolysis of β−(1• →4)- d-xylosidic linkages in xylans yielding various β−(1→4)-d-xylooligosaccharides.
Cellulases and Related Enzyme Activities
14
Cellobiase from Aspergillus niger
Cellobiase enzyme preparation obtained by submerged fermentation of an Aspergillus niger microorganism. The cellobiase hydrolyzes cellobiose to glucose.
Novozyme 188 liquid, activity: ≥250 units/g
A product of Novozyme Corp.C6105-50ML 50 mLC6105-250ML 250 mL
▼ Cellulase
[9012-54-8]
Cellulase from Aspergillus sp.Carezyme 1000L®
activity: ≥1000 units/g
produced by submerged fermentation of a genetically modified Aspergillus microorganism
A product of Novozyme Corp.C2605-50ML 50 mLC2605-250ML 250 mL
Cellulase from Trichodermalongibrachiatum
powder, activity: ≥1.0 unit/mg solidAn acid cellulase with xylanase, pectinase, mannanase, xyloglucanase, laminarase, β-glucosidase, β-xylosidase, α-L-arabinofuranosidase, amylase, and protease activities
One unit will liberate 1.0 μmole of glucose from cellulose in one hour at pH 5.0 at 37 °C (2 hr incubation time).
C9748-100G 100 g
Cellulase from Trichoderma reeseiATCC 269211,4-(1,3:1,4)-β-D-Glucan 4-glucano-hydrol ase
lyophilized powder, activity: ≥1 unit/mg solid
One unit will liberate 1.0 μmole of glucose from cellulose in one hr at pH 5.0 at 37 °C (2 hr incubation time).C8546-2.5KU 2500 unitsC8546-5KU 5000 unitsC8546-10KU 10000 units
Celluclast® 1.5L aqueous solution, activity: ≥700 units/g
Produced by submerged fermentation of a selected strain of the fungus Trichoderma reesei and catalyzes the breakdown of cellulose into glucose, cellobiose, and higher glucose polymers.
A product of Novozyme Corp.
C2730-50ML 50 mL
Cellulase from Trichoderma viride1,4-(1,3:1,4)-β-D-Glucan 4-glucano-hydrol aseOne unit will liberate 1.0 μmole of glucose from cellulose in one hour at pH 5.0 at 37 °C (2 hr incubation time).
crude powder, activity: 3–10 units/mg solid
C9422-5KU 5000 unitsC9422-10KU 10000 units
Onozuka RS powder, activity: ≥5,000 units/g solid
Manufactured by YakultC0615-1G 1 g
Cellulase ▲
Driselase® from Basidiomycetes sp.[85186-71-6]Crude powder containing laminarinase, xylanase and cellulase.
powder
D9515-1G 1 gD9515-5G 5 gD9515-25G 25 g
▼ β-Glucanase
β-Glucanase from Aspergillus niger[9074-98-0]
powder, activity: ~1 units/mgOne unit corresponds to the amount of enzyme which will release 1 μmole of reducing sugar equivalents (expressed as glucose) per minute at pH 5.0 and 55 °C, using β-d-glucan (Cat. No. 49102) as substrate49101-100MG 100 mg49101-500MG 500 mg
β-Glucanase from Bacillus subtilis[9074-98-0]
powder, activity: ~1 units/mgOne unit corresponds to the amount of enzyme which will release 1 μmol of reducing sugar equivalents (expressed as glucose) per minute of pH 6.0 and 55 °C, using β-d-glucan (Cat. No. 49102) as substrate49106-100MG 100 mg
β-Glucanase from Trichodermalongibrachiatum
A mixture composed mainly of β-1→3 / 1→4-glucanase, xylanase, and cellulase activities. β-glucosidase, β-xylosidase, α-L-arabinofuranosidase,
amylase, and protease activities are also present.
activity: ≥1.0 units/mg solid
One unit will liberate 1.0 μmole of glucose from cellulose in one hr at pH 5.0 at 37 °C (2 hr incubation time).G4423-100G 100 g
β-Glucanase ▲
β-(1→3)-d-Glucanase from Helix pomatia
[9044-93-3]
powder, activity: 0.5–1.5 units/mgOne unit corresponds to the amount of enzyme which liberates 1 μmole of glucose from laminarin (Cat. No. 61340) per minute at pH 5.0 and 37 °C
Improved filterability of wines by enzymic decomposition of carbohydrate-containing colloids1; Induction of hydrolases as a defense reaction against pathogens, review2
Lit cited: 1. Wucherpfennig, K., and Dietrich, H. , Wein-wirtschaft 118, 598 (1982); 2. Boller, T. , UCLA Symp. Mol. Cell Biol., New Ser. 22, 247 (1985)
49103-10MG 10 mg49103-50MG 50 mg
β-Gluco sidase from almondsβ-d-Gluco side gluco hydrol ase [9001-22-3]
lyophilized powder, activity: ≥2 units/mg solidCrude
One unit will liberate 1.0 μmole of glucose from salicin per min at pH 5.0 at 37 °C.G0395-2.5KU 2500 unitsG0395-5KU 5000 unitsG0395-50KU 50000 units
lyophilized powder, activity: 20–40 units/mg solidChromatographically purified
One unit will liberate 1.0 μmole of glucose from salicin per min at pH 5.0 at 37 °C.G4511-100UN 100 unitsG4511-250UN 250 unitsG4511-1KU 1000 units
Hemicellulase from Aspergillus niger[9025-56-3]
powder, activity: 0.3–3.0 unit/mg solid (using a β-galactose dehydrogenase system and locust bean gum as substrate)
An undefined mixture of glycolytic enzymes usually containing xylanase, mannanase and other activities.
One unit will produce a relative fluidity change of 1 per 5 minutes using locust bean gum as substrate at pH 4.5 at 40 °C
H2125-150KU 150000 units
Order sigma.com/order Technical service sigma.com/techinfo sigma.com/lifescience 15
Online Metabolomics Resource Use the IUBMB–Sigma-Aldrich Interactive Metabolic Pathway Chart to find the Metabolite Standards you need.
http://www.sigma-aldrich.com/ProductLookup.html?ProdNo=C7352&Brand=SIGMA
The Metabolic Pathways Map contains over 500 hyperlinks to Sigma product listings. Just click on the metabolite name or the enzyme’s E.C. number to access product information.
You can access the chart at
sigma-aldrich.com/metpath
▼ Laminarinase
Endo-1,3(4)-β-glucanase[62213-14-3]
Laminarinase from Penicillium sp.1,3-(1,3:1,4)-β-d-Glucan 3(4)-glucano hydrol ase
lyophilized powder, activity: 5–10 units/mg protein
Lyophilized powder containing acetate buffer salts
One unit will liberate 1.0 mg of reducing sugar (measured as glucose) from laminarin per min at pH 5.0 at 37 °C.L9259-25UN 25 units
Laminarinase from Trichoderma sp.
1,3-[1,3;1,4]-β-d-Glucan 3(4)-glucano hydrol ase
View more information on enzymes for complex carbohydrate analysis at sigma-aldrich.com/enzymeexplorer
powder, activity: 100–400 units/g solidContains chitinase activity.
One unit will liberate 1.0 mg of reducing sugar (measured as glucose) from laminarin per min at pH 5.0 at 37 °C.
L5272-5UN 5 unitsL5272-25UN 25 units
Laminarinase ▲
▼ XylanaseView more information on enzymes for complex carbohydrate analysis at sigma-aldrich.com/enzymeexplorer
Xylanase from Thermomyces lanuginosus[37278-89-0]Purified endo-β−(1→4)-xylanase from Thermomyces lanuginosus produced by submerged fermentation of a genetically modified Aspergillus oryzae microorganism
Pentopan Mono BG® powder, activity: ≥2500 units/g, recombinant, expressed in Aspergillus oryzae
A product of Novozyme Corp.
X2753-10G 10 gX2753-50G 50 g
Xylanase from Trichoderma virideendo-1,4-β-Xylanase; 1,4-β-d-Xylanxylano hydrol ase [9025-57-4]
lyophilized powder, activity: 100–300 units/mg protein
Contains sorbitol and sodium acetate buffer salts
One unit will liberate 1 μmole of reducing sugar measured as xylose equivalents from xylan (Cat. No. X0627) per min at pH 4.5 at 30 °C.
X3876-250UN 250 unitsX3876-1KU 1000 units
Xylanase ▲
endo-1,4-β-Xylanase from Trichodermalongibrachiatum
1,4-β-d-Xylanxylano hydrol ase
Primary activity is an acid-neutral endo-1,4-β-d-xylanase, additional activities include β-glucanase, cellulase, pectinase, mannanase, xyloglucanase, laminarase, β-glucosidase, β-xylosidase, α-L-arabinofuranosidase, amylase, and protease.
activity: ≥1.0 units/mg solid
One unit will liberate 1 μmole of reducing sugar measured as xylose equivalents from xylan (Cat. No. X0627) per min at pH 4.5 at 30 °C.
X2629-100G 100 g
16
Enzymes for Pectin HydroylsisPectins are complex-branched heteropolysaccharides primarily containing an α-(1→4) polygalacturonic acid backbone which can be randomly acetylated and methylated. Three different pectins have been isolated from plant cell walls.
COOHO
COCH 3
OH
OH
O
O
OH
OOCH3
O
OCOOH
OH
OH
O
O
COCH 3
OH
OH
O
Pectinase Pectinase
Endo-pectin Lyase Pectinesterase
Homogalacturonan is a composed of a poly-α−(1→4)-galacturonic acid backbone with random partial methylation and acetylation.
O
CH 3
OH
OH
O
HOCH2OHCH2OH CH2OH
O
OH
CH2OH
CH2OHO
OHO
O
O
OH
O
O
CH 3
OH
OH
O
OCOCH 3
OH
OH
O
O
CH 3
OH
O
OO
COCH 3
OH
OH
O
O
CH 3
OHO
COOH
OH
OH
OO
CH2OH
O
OH
OH
O OO
OH
OH
O
OH
OH
O
HO
Oligo-a-(1-3)-D-arabinose branching
Oligo-b-(1-4)-D-galactose branching
b-Galactosidase
a-(1-2)-L-rhamnose
α-(1-4)-D-galacturonic acid
Rhamnogalacturonan I is composed of alternating α−(1→2)-l-rhamnosyl-α−(1→4)-d-galacturonosyl backbone with two types of branching composed of a ribofuranose or galactose oligomers.
COOH
O
COOCH 3
OH O
O
O
OH
O
O
COOH
OOCCH3
OH
O
O
COOCH 3
OH
OH
O
COOH
O
COOCH 3O
OH
OO
OOCCH3
O
O
O
COOH
OH
OOCCH3
O
O
COOCH 3
OH
O
O
OH
α-3-deoxy-D-manno-2-octulosonic acid (Kdo)
α-Rhamnoseβ-Arabinose
β-3-deoxy-D-lyxo-2-heptulosonic acid (Dha)
β-D-Apiose
3−β-L-Rhamnose2−α-L-Aceric(O-acetyl)β-D-Galactose
2 α-L-Arabinopyra nose2 α-L-Rhamnose
β-L-Arabinofuranose
α-D-fucose
(2-O-methyl, 3-O-acetyl-)
3'
5 5
4
2
β-D-Apiose3'
2−β-L-Rhamnose 4 α-L-fucose
β-D-Glucuronic Acid
α-D-Xylose(2-O-methyl)
β-D-Galactose
α-D-Galactose3
α-D-Galactose
2
4
3
Pectinesterase
Pectinase
Rhamnogalacturonan II is composed of poly-α−(1→4)-d-galacturonic acid backbone with random partial methylation, acetylation and four types of branching.
Order sigma.com/order Technical service sigma.com/techinfo sigma.com/lifescience 17
▼ Pectinase
Pectinase from Aspergillus aculeatus
Pectinex® Ultra SPL aqueous solution, activity: ≥9,500 units/mL
Highly active pectolytic enzyme preparation produced by a selected strain of Aspergillus aculeatus
A product of Novozyme Corp.P2611-50ML 50 mLP2611-250ML 250 mL
Pectinase from Aspergillus nigerPoly galacturonase solution from Aspergillus niger; Poly-(1,4-α-d-galacturonide) glycano hydrol ase[9032-75-1]Used in plant protoplast preparation to digest cell wall prior to organelle isolation.
aqueous glycerol solution, activity: ≥5 units/mg protein (Lowry)
Solution in 40% glycerol
One unit will liberate 1.0 μmole of galacturonic acid from polygalacturonic acid per min at pH 4.0 at 25 °C.P4716-5KU 5000 unitsP4716-10KU 10000 unitsP4716-25KU 25000 unitsP4716-100KU 100000 units
Pectinase from Aspergillus niger Pectinex 3XL® aqueous solutionPectolytic enzyme preparation produced from a selected strain of Aspergillus niger: contains mainly pectintranseliminase, polygalacturonase, and pectinesterase and small amounts of hemicellulases and cellulases.
A product of Novozyme Corp.P2736-50ML 50 mLP2736-250ML 250 mL
Pectinase from Rhizopus sp.Poly-(1,4-α-d-galacturonide) glycano hydrol ase; Poly-galacturonase[9032-75-1]Used in plant protoplast preparation to digest cell wall prior to organelle isolation.
Macerozyme R-10 powder, activity: 400–800 units/g solid
A source of pectinase activity, also containing cellulase and hemicellulase activities.
One unit will liberate 1.0 μmole of galacturonic acid from polygalacturonic acid per min at pH 4.0 at 25 °C.
P2401-500UN 500 unitsP2401-1KU 1000 unitsP2401-5KU 5000 units
Pectinase ▲
Pectolyase from Aspergillus japonicus
Reported to contain two types of pectinase, endopolygalacturonase (EC3.2.1.15), endopectin lyase (EC4.2.2.10) and a maceration stimulating factor.
Used in plant protoplast preparation to digest cell wall prior to organelle isolation.
Check out the Sigma-Aldrich Renewable & Alternative Energy Web Portal: sigma-aldrich.com/renewable
Materials for Renewable and Alternative Energy Solutions
Solar Energy Conversion (Organic, Crystalline •and Thin Film Photovoltaics)
Hydrogen Economy •Supercapacitors/Advanced Batteries•Alternative Fuels•
sigma-aldrich.com
Aldrich Materials Science — We focus on materials so you can focus on results.
Feeling the Heat? Then Capture It!
lyophilized powder, activity: ≥0.3 units/mg solidOne unit will liberate 1.0 μmole of galacturonic acid from polygalacturonic acid per min at pH 5.5 at 25 °C.P3026-100MG 100 mgP3026-250MG 250 mgP3026-1G 1 g
18
Enzymes for Lignin DepolymerizationTo some, lignin appears to be a foreign substance resembling a randomly modified polystyrene polymer, not resembling any of the more familiar biopolymers composed of carbohydrates, amino acids or nucleotides. However, next to cellulose, it is the second most abundant biopolymer on earth comprising as much as 30% of the dry mass of wood. Unlike other biopolymers, enzymatic degradation is oxidative versus hydrolytic and is limited to a select group of fungi and bacteria. Lignins appear to be heterogeneous and random with regards to degree of polymerization, branching, and monomer composition and sequence.
HO
OH
HO
CH3OOH
HO
CH3OOH
OCH3
p-Coumaryl alcohol Coniferyl alcohol Sinapyl alcohol
Lignin Monomers
O
OH
OH
O
O
H
O
O CH3O
HO
O
CH3O
OH
OH
H
HO
CH3O
O
CH3O
CH 3O
HO OHO
O CH3O CH3O
O
CH3OHO
HOHO
O
O
CH3O
CH3OO
O O
OH
O
CH3O
OCH3
HO
O
OCH3
HO
HO
HO
HO
HO
O
OO
OH
OH
O
O
O
H
OH
OH
OH CH 3O
CH3O
CH3O
O
HO
CH3O
Lignin
Order sigma.com/order Technical service sigma.com/techinfo sigma.com/lifescience 19
▼ Laccase
[80498-15-3]
Laccase from Rhus verniciferaBen zene diol:oxygen oxidoreductase crude acetone powder, activity: ≥50 units/mg
solidOne unit will produce a ΔA530 of 0.001 per min at pH 6.5 at 30 °C in a 3 mL reaction volume using syringaldazine as substrate.
L2157-10KU 10000 units
Laccase from Trametes versicolor
former nomenclature: Coriolus versicolor powder, activity: >20 units/mgOne unit corresponds to the amount of enzyme which converts 1 μmole of catechol per minute at pH 4.5 and 25 °C
53739-100MG-F 100 mg53739-1G-F 1 g
HO OH
O
CH3O
CH3O
O
OHHO
CH3O
O
O H
O
CH3O
H2O2 H2O
Lignin Peroxidase
Lignin peroxidase catalyzes the oxidative cleavage of carbon-carbon and ether bonds in lignin-related compounds.
2 Mn(II) + 2 H+ + H2O2 2 Mn(III) + 2 H2O
Manganese Peroxidase
Manganese peroxidase is a hemoprotein involved in the oxidative degradation of lignin in white rot basidiomycetes.
powder, activity: ≥0.5 units/mgOne unit corresponds to the amount of enzyme which converts 1 μmole of catechol per minute at pH 6.0 and 25 °C38429-1G 1 g38429-10G 10 g
Laccase, Coriolus versicolor, CLEA
Laccase, Coriolus versicolor, cross-linked enzyme aggregate activity: ≥0.3 units/mg
One unit corresponds to the amount of enzyme which oxidizes 1 μmol ABTS per minute at pH 4.5 and 25°C38837-100MG 100 mg
Laccase ▲
Lignin Peroxi daseLiP; Peroxi dase, lignin; Ligninase[42613-30-9]
powder, activity: >0.1 units/mgOne unit corresponds to the amount of enzyme, which oxidizes 1 μmole 3.4-dimethoxybenzyl alcohol per minute at pH 3.0 and 30 °C 42603-10MG-F 10 mg
Manganese Peroxi dase fromNematoloma frowardii[114995-15-2]
41563 Inquire
Manganese peroxi dase from white-rot fungus (Phanerochaete chrysosporium)MnP; Peroxi dase, manganese; Manganese-dependent lignin peroxi dase[114995-15-2]
powder, activity: ≥20 U/gonly partially soluble in water or buffer
One unit corresponds to the amount of enzyme, which oxidizes 1 μmole Mn2+ per minute to Mn3+ at pH 4.5 and 25 °C
This product is supplied as a mixture of isozymes, mol. mass (40–65 kDa).93014-10MG-F 10 mg
20
Enzymatic hydrolysis of starch-based biomass to yield monomeric glucose is often a multi-enzyme process and can involve α-amylase, β-amylase, amyloglucosidase, isoamylase and α-glucosidase.
α-Amylase catalyzes the endohydrolysis •of α−(1→4)-d-glucosidic linkages in polysaccharides containing three or more α−(1→4)-linked d-glucose units.
β-Amylase catalyzes the exohydrolysis •of α−(1→4)-d-glucosidic linkages in polysaccharides resulting in the successive liberation of maltose units from the non-reducing ends of the chains.
Amyloglucosidase (glucoamylase) catalyzes •the hydrolysis of terminal α−(1→4)-d-glucose residues successively from the non-reducing ends of maltooligo- and polysaccharides with release of β-d-glucose. Most forms of the enzyme can rapidly hydrolyze α−(1→6)-d-glucosidic bonds when the next bond in the sequence is
α-Amylase n
OCH2OH
OH
OH
OCH2OH
OH
OHOO
OCH2OH
OH
OH
O
O
CH2
OH
OHO
OCH2OH
OH
OH
O
OCH2OH
OH
OHO O
Ox
n
OCH2OH
OH
OH
OCH2OH
OH
OHOO
OCH2OH
OH
OH
O
OCH2
OH
OHO
OCH2OH
OH
OH
O
OCH2OH
OH
OHO
O
OCH2OH
OH
OHOOH
X
n
X
OCH2OH
OH
OH
OCH2OH
OH
OHOO
OCH2OH
OH
OH
O
OCH2
OH
OHO
O
HO
n
OH
OCH2OH
OH
OH
OCH2OH
OH
OH
O
OCH2
OH
OHO
O
HO
Amyloglucosidasea-Glucosidase
b-Amylase
Isoamylase
Amyloglucosidase& a-Glucosidase(terminal (1–6) residues)
Amylopectin is a polymer of α-(1→4)-d-glycopyranosyl units with approximately 4% α-(1→6)-d-glycopyranosyl branching.
OCH2OH
OH
OH
O
OCH2OH
OH
OHO
OCH2O
OH
OH
O
OCH2OH
OH
OHO O
n
OCH2OH
OH
OH
O
OCH2OH
OH
OHO
OCH2OH
OH
OH
OOH
n
OCH2OH
OH
OH
O
OCH2OH
OH
OHOOH
Amyloglucosidasea-Glucosidase
b-Amylase
a-Amylase Amylose is a polymer of
α-(1→4)-glucopyranosyl units.
1→4- and some preparations of this enzyme hydrolyze 1→6- and 1→3-α-d-glucosidic bonds in other polysaccharides.
Isoamylase catalyzes the hydrolysis of •α−(1→6)-d-glucosidic branch linkages in amylopectin and β-limit dextrins.
α-Glucosidase catalyzes the hydrolysis of •terminal 1→4-linked α-d-glucose residues successively from the non-reducing ends of maltooligo- and to a lesser extent polysaccharides with release of β-d-glucose. Most forms of the enzyme can slowly hydrolyze α−(1→6)-d-glucosidic bonds.
Enzymes for Starch Hydrolysis
Order sigma.com/order Technical service sigma.com/techinfo sigma.com/lifescience 21
▼ α-Amylase
α-Amyl ase from Aspergillus oryzae1,4-α-d-Glucan-glucano hydrol ase[9001-19-8]
lyophilized powder, activity: 150–250 units/mg protein (biuret)
Crude
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
A6211 Inquire
Fung amyl® 800 L aqueous solution, activity: ≥800 FAU/g
A product of Novozyme Corp.
A8220-50ML 50 mLA8220-250ML 250 mL
Taka-Diastase from Aspergillus oryzae; Taka-Amyl-ase A powder, activity: ~1.5 units/mg (~0.2 U acc. to Willstätter)
One unit corresponds to the amount of enzyme which liberates 1 μmol maltose per minute at pH 6.0 and 25 °C (starch acc. to Zulkowsky, Fluka No. 85642, as substrate).
Molecular weight1; Product distribution in the hydrolysis of amylose2; Application in (selective) hydrolysis/condensation of glycosidic bonds3; Suitable for use in thiamine determination4.
Lit cited: 1. T. Takagi, J. Biochem. 89, 363 (1981); 2. H. Kondo et al., J. Biochem. 87, 1053 (1980); 3. K. Fujita et al., Bull. Chem. Soc. Jpn. 62, 3150 (1989); 4. P.W. Defibaugh, J. Assoc. Off. Anal. Chem. 70, 514 (1987)
86250-100G 100 g86250-500G 500 g
spray-dried (powder), activity: ≥150 units/mg protein (biuret)
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
A9857-250KU 250000 unitsA9857-1MU 1000000 unitsA9857-5MU 5000000 units
α-Amylase from Bacillus sp.
ammonium sulfate suspension, activity: 40–90 units/mL packed gel
Suspension in 2.0 M (NH4)2SO4, pH 7.0
One unit will liberate 1.0 μmole of maltose from starch per min at pH 6.9 at 30 °C. (Each unit is equivalent to 0.7 of mg maltose liberated per 3 min. at 20 °C)
A0909 Inquire
α-Amyl ase from Bacillus amyloliquefaciens1,4-α-d-Glucan Glucano-hydrol ase[9000-85-5]An endoamylase that randomly hydrolyzes α-(1→4)-glycosidic linkages in amylose and amylopectin. The breakdown products are oligosaccharides and dextrins of varying chain length. This enzyme is active at high temperatures (70−90 °C).
One unit is the amount of enzyme which dextrinizes 5.26 g of dry starch per hour under standard conditions.
BAN™ 240L liquid, activity: ≥250 units/gA product of Novozyme Corp.A7595-50ML 50 mLA7595-250ML 250 mL
α-Amyl ase from Bacillus licheniformis1,4-α-d-Glucan-glucano hydrol ase[9000-85-5]One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
Term amyl® 120 saline solution, activity: 500–1,000 units/mg protein (biuret)
Aqueous solution containing approx. 15% sodium chloride and 25% sucrose.
Reported to be heat stable at temperatures as high as ~90 °C.
A product of Novozyme Corp.
A3403-500KU 500000 unitsA3403-1MU 1000000 unitsA3403-5MU 5000000 units
lyophilized powder, activity: 500–1,500 units/mg protein
Heat-stable formulation
Lyophilized powder containing potassium phosphate
A4551-100MG 100 mgA4551-1G 1 g
α-Amyl ase from Bacillus subtilis[9000-90-2]
powder, activity: ~380 units/mgOne unit is the amount of enzyme which liberates 1 μmole of maltose per minute at pH 6.9 and 25 °C (using Cat. No. 85642 as substrate)
Heat stability of bacterial α-amylases1; Action pattern on sweet potato starch, amylose and amylopectin2; Action on native wheat starch.3
Lit cited: 1. J.E. Anderson et al., J. Food Sci. 48, 1622 (1983); 2. P.L. Chang Rupp, S.J. Schwartz, J. Food Biochem. 12, 191 (1988); 3. P. Colonna et al., Biotechnol. Bioeng. 31, 895 (1988).
10069-250MG 250 mg10069-1G 1 g
powder, activity: ~50 units/mgOne unit corresponds to the amount of enzyme which liberates 1 μmole maltose per minute at pH 6.9 at 25 °C (starch acc. to Zulkowsky, Cat. No. 85642, as substrate).
Applications in (selective) hydrolysis/condensations of glycosidic bonds.1,2
Lit cited: 1. Y. Takasaki, Agric. Biol. Chem. 49, 1091 (1985); 2. C.S. Su, C.P. Yang, J. Chem. Technol. Biotechnol. 48, 313 (1990)
10070-10G 10 g10070-50G 50 g
α-Amyl ase from barley malt1,4-α-d-Glucan-glucano hydrol ase[9000-90-2]
powderβ-amylase activity: ≥1 unit/mg solid
α-amylase activity: ≥1 unit/mg solid
Package size based on α-amylase activity
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
A2771 Inquire
α-Amyl ase from human pancreas[9000-90-2]
lyophilized powder, activity: ≥100 units/mg protein
Lyophilized from Tris buffer containing NaCl and CaCl2.
Prepared by modified method of Levitzki et al.
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.A9972-100UG 100 μg
α-Amyl ase from human saliva1,4-α-d-Glucan-glucano hydrol ase[9000-90-2]
lyophilized powder, activity: 300–1,500 units/mg protein
Lyophilized powder containing (NH4)2SO4 and sodium citrate.
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.A1031-1KU 1000 unitsA1031-5KU 5000 units
lyophilized powder, activity: 1,000–3,000 units/mg protein
Lyophilized powder containing (NH4)2SO4 and sodium citrate
Chromatographically purified
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.A0521-100UN 100 unitsA0521-500UN 500 unitsA0521-2.5KU 2500 units
22
α-Amyl ase from porcine pancreas
Molecular mass: 51–54 kDa.
α-Amylase isolated from porcine pancreas is a glycoprotein. It is a single polypeptide chain of ~475 residues containing two SH groups and four disulfide bridges and a tightly bound Ca2+ necessary for stability. Chloride ions are necessary for activity and stability. The pH range for activity is 5.5 to 8.0, with the pH optimum at 7.
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
activity: ≥10 units/mg solidContains lactose
Package size based on α-amylase activityA3176-500KU 500000 unitsA3176-1MU 1000000 unitsA3176-2.5MU 2500000 unitsA3176-5MU 5000000 unitsA3176-10MU 10000000 units
DFP Treated, saline suspension, activity: 700–1400 units/mg protein (E 1%/280)
Suspension in 2.9 M NaCl solution containing 3 mM CaCl2DFP treated. 2× crystallized
View more information on enzymes for complex carbohydrate analysis at sigma-aldrich.com/enzymeexplorer
A6255-10MG 10 mgA6255-25MG 25 mgA6255-100MG 100 mg
DFP treated, ammonium sulfate suspension, activity: ≥500 units/mg protein (E 1%/280)
Suspension in 3.2 M (NH4)2SO4, pH 6.1
A2643 Inquire
PMSF treated, saline suspension, activity: 700–1400 units/mg protein (E 1%/280)
Suspension in 2.9 M NaCl solution containing 3 mM CaCl2.
2× crystallized
A4268-25MG 25 mgA4268-100MG 100 mg
α-Amylase ▲
▼ β-Amylase
1,4-α-d-Glucan malto hydrol ase[9000-91-3]
β-Amyl ase from barley
activity: 20–80 units/mg protein (biuret)Crude
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 4.8 at 20 °C.A7130-10KU 10000 unitsA7130-50KU 50000 unitsA7130-250KU 250000 units
β-Amyl ase from sweet potato
ammonium sulfate suspension, activity: ≥750 units/mg protein (E 1%/280)
Crystalline suspension in 2.3 M (NH4)2SO4
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 4.8 at 20 °C.
View more information on enzymes for complex carbohydrate analysis at sigma-aldrich.com/enzymeexplorer
A7005-10KU 10000 unitsA7005-25KU 25000 unitsA7005-50KU 50000 unitsA7005-100KU 100000 units
β-Amylase ▲
α-Amyl ase, heat-stableα-Amyl ase from Bacillus licheniformis; 1,4-α-D-Glucan-glucano hydrol ase[9000-85-5]
solution, for use in Total Dietary Fiber Assay, TDF-100A
A3306-10ML 10 mL
Amyl ase, Malto genic from Bacillus sp.Malto genic Amyl ase; Glucan 1,4-α-malto hydrol ase Nov amyl 1000BG
A2986-10G 10 g
▼ AmyloglucosidaseExo-1,4-α-gluco sidase; 1,4-α-d-Glucan gluco hydrol ase; Gluco amyl ase[9032-08-0]
Amylo gluco sidase from Aspergillus niger
lyophilized, powder, activity: ~70 units/mgFor glycogen determination in whole yeast cells; Synthesis of hetero-oligosaccharides by glucoamylase in reverse.
One unit corresponds to the amount of enzyme which liberates 1 μmole of glucose per minute at pH 4.8 and 60 °C (starch acc. to Zulkowsky, Cat. No. 85642, as substrate).10115-1G-F 1 g10115-5G-F 5 g
lyophilized powder, activity: 30–60 units/mg protein (biuret)
Lyophilized powder containing less than 0.02% glucose
One unit will liberate 1.0 mg of glucose from starch in 3 min at pH 4.5 at 55 °C.A7420-5MG 5 mgA7420-25MG 25 mgA7420-100MG 100 mg
powder, activity: ~120 units/mgOne unit corresponds to the amount of enzyme which liberates 1 μmol glucose per minute at pH 4.8 and 60 °C (starch, Fluka No. 85642, as substrate).
Synthesis of hetero-oligosaccharides by glucoamylase in reverse1.
Lit cited: 1. R.A. Rastall et al., Biotechnol. Lett. 13, 501 (1991)
10113-1G 1 g10113-5G 5 g
Amylo gluco sidase from Rhizopus sp.
activity: ≥5,000 units/g solidOne unit will liberate 1.0 mg of glucose from starch in 3 min at pH 4.5 at 55 °C.
Using soluble starch, almost theoretical yields of glucose are obtained.
A7255 Inquire
Amyloglucosidase ▲
▼ α-Glucosidaseα-d-Gluco side gluco hydrol ase[9001-42-7]Protein determined by biuret.
α-Gluco sidase from BacillusstearothermophilusMaltase
Maltase lyophilized powder, activity: ≥50 units/mg protein
Lyophilized powder containing potassium phosphate buffer salt
One unit will liberate 1.0 μmole of d-glucose from p-nitrophenyl α-d-glucoside per min at pH 6.8 at 37 °C.
Activity using maltose as substrate at pH 6.0 at 25 deg C is ~2X greater than that obtained using p-nitrophenyl-α-d-glucoside as substrate at pH 6.8 at 37 °C.G3651-250UN 250 units
α-Gluco sidase from rice
Maltase
ammonium sulfate suspension, activity: 40–80 units/mg protein
Suspension in 2.8 M (NH4)2SO4 solution
One unit will convert 1.0 μmole of maltose to 2.0 μmoles of d-glucose per min at pH 4.0 at 37 °C.
G9259-100UN 100 units
Order sigma.com/order Technical service sigma.com/techinfo sigma.com/lifescience 23
α-Gluco sidase from Saccharomycescerevisiae
α-d-Gluco sidase; Maltase from yeast Hydrolysis of terminal, non-reducing 1→4-linked d-glucose residues with release of d-glucose.
For the determination of α-amylase and the synthesis of various 1’-O-sucrose and 1-O-fructose esters
recombinant, expressed in unspecified host, lyophilized powder, activity: ≥125 units/mg protein
Lyophilized powder containing potassium phosphate buffer salt pH 7.15 and approx. 70% lactose
One unit will liberate 1.0 μmole of d-glucose from p-nitrophenyl α-d-glucoside per min at pH 6.8 at 37 °C.G0660-750UN 750 units
lyophilized powder, activity: ≥10 units/mg protein (using p-nitrophenyl α-d-glucoside as substrate.)Sold on basis of p-nitrophenyl α-d-glucoside units.
One unit will liberate 1.0 μmole of d-glucose from p-nitrophenyl α-d-glucoside per min at pH 6.8 at 37 °C.
View more information on enzymes for complex carbohydrate analysis at sigma-aldrich.com/enzymeexplorer
G5003-100UN 100 unitsG5003-1KU 1000 units
α-Glucosidase ▲
Ethanol Analysis Reagents
ASTM™ D5501 Denatured Fuel EthanolStandards Kit
Use this quantitative calibration standard kit to determine if ethanol and gasoline fuel blends comply with federal and state laws. A certificate of analysis accompanies each kit.
suitable for D5501 per ASTM
ComponentsSol.#1 Ethanol:Heptane: Methanol (92%, 7.40%, 0.60%) Sol.#2 Ethanol:Heptane: Methanol (93%, 6.50%, 0.50%) Sol.#3 Ethanol:Heptane: Methanol (94%, 5.60%, 0.40%) Sol.#4 Ethanol:Heptane: Methanol (95%, 4.70%, 0.30%) Sol.#5 Ethanol:Heptane: Methanol (96%, 3.80%, 0.20%) Sol.#6 Ethanol:Heptane: Methanol (97%, 2.90%, 0.10%) Sol.#7 Ethanol:Heptane: Methanol (98%, 1.95%, 0.05%)
40361-U 1 pkg
Fuel Ethanol Residual Saccharides Mix
Quantitative standard for monitoring unfermented sugars present during the process of transforming corn feedstock into ethanol. ComponentsGlycerol 1 % (w/v)D-(+)-Glucose 2 % (w/v)Maltotriose (DP3) 1 % (w/v)Maltose monohydrate 2 % (w/v)L-(+)-Lactic acid .3 % (w/v)Acetic acid .3 % (w/v)Dextrin 3.25 % (w/v)Ethanol 12 % (w/v)
48468-U 10 × 2 mL
Ethanol standard s 10% (v/v)
Ethanol solution; Ethyl alcohol[64-17-5] C2H5OH FW 46.07
CH3CH2OH
aqueous solutionFlame-sealed flint ampuleE2385-10AMP 10 amp
sigma-aldrich.com
Sigma-Aldrich and GeneGo have integrated Sigma-Aldrich product listings into the MetaCore™ and MetaDrug™ software suites.
This partnership associates Sigma-Aldrich products to over 700 Interactive maps of Canonical pathways located in MetaCore and MetaDrug.
Users of MetaCore and MetaDrug are able to link to Sigma-Aldrich products from molecules displayed in
the Drug Detail Pages. This functionality will accelerate productivity for researchers by showing molecule availability during the information gathering process of experiments.
Learn more about GeneGo and their MetaCore and MetaDrug software suites by visiting www.genego.com
Sigma-Aldrich® and GeneGo
MetaCore and MetaDrug are trademarks of GeneGo, Inc. Patent Chemistry Database: Copyright © 2007-2008, Elsevier Inc., licensed to Elsevier Information Systems GmbH. PharmaPendium: Copyright © 2007-2008, Elsevier Inc., licensed to Elsevier Information Systems GmbH.
24
Lipases for TransesterificationAmano Lipase PS (immobilized on diatomite)
708011-10G 10 g
Amano Lipase PS, fromBurkholderia cepacia activity: ≥30,000 U/g, pH 7.0, 50 °C (Optimum pH
and temperature)
534641-10G 10 g534641-50G 50 g
Amano Lipase PS-C II (immobilizedon ceramic)One unit will produce 1.0 micromole of 1-Phenethyl alcohol to 1-Phenethyl acetate per min. at 25 °C in the presence of vinyl acetate
534889 Inquire
Amano lipase PS-IM (immobilized ondiatomaceous earth)
709603-10G 10 g
Amano Lipase PS-C I (immobilized onceramic)
One unit will produce 1.0 micromole of 1-Phenethyl alcohol to 1-Phenethyl acetate per min. at 25 °C in the presence of vinyl acetate534897 Inquire
Lipase from Candida sp. Novozymes® CALB L recombinant, expressed in
Aspergillus nigeraqueous solution
Minimum 5,000 LU/G of liquidL3170-50ML 50 mL
Lipase acrylic resin from CandidaantarcticaNovozym® 435[9001-62-1]Immobilized preparation of a thermostable lipase, particularly useful in the synthesis of esters and amides, and has a broad substrate specificity.
Lipase from (B lipase) Candida antarctica produced by submerged fermentation of a genetically modified Aspergillus oryzae microorganism and adsorbed on a macroporous resin.
Enzymes and Reagents for BioDiesel Research
Enzymes and Reagents for BioDiesel ResearchLipases for Transesterification
activity: ≥10,000 U/g, recombinant, expressed in Aspergillus niger
A product of Novozyme Corp.L4777-3G 3 gL4777-10G 10 g
Phospholipase C for Degumming Oils▼ Phospholipase C
Phos pha tidyl choline choline phos pho hydrol ase; Lecithinase C; Lipo phos pho di ester ase I; PC-PLC [9001-86-9]Hydrolyzes the phosphate bond on phosphatidylcholine and other glycerophospholipids yielding diacylglycerol; this enzyme will also hydrolyze the phosphate bonds of sphingomyelin, cardiolipin, choline plasmalogen and ceramide phospholipids.
Phos pho lipase C from Bacillus cereus
activity: ≥200 units/mg proteinLyophilized powder containing approx. 10% protein. Remainder: trehalose, zinc sulfate, and potassium phosphate
One unit will liberate 1.0 μmole of water soluble organic phosphorus from L-α-phosphatidylcholine per min at pH 7.3 at 37 °C.P6621-250UN 250 units
Phos pho lipase C from Clostridiumperfringens (C. welchii)
One unit will liberate 1.0 μmole of water soluble organic phosphorus from egg yolk l-α-phosphatidylcholine per min at pH 7.3 at 37 °C.
lyophilized powder, activity: 10–50 units/mg protein
P7633-25UN 25 unitsP7633-125UN 125 unitsP7633-500UN 500 units
lyophilized powder, activity: ≥150 units/mg protein
Lyophilized powder in buffered salts
Chromatographically purified
P4039-125UN 125 unitsP4039-500UN 500 units
Phospholipase C ▲
++
HC
HC
CH
R
R
R
O
O
O
O
O
HC
HC
CH
H
H
H
O
3 ROH O
O
O
O
O
O
O
O
O
Lipase
Transesterification of triglycerides utilizing commercial lipase preparations is currently under investigation as a low energy input alternative to current “chemical” methods.
N
CH3
CH3
H3C
HC
HC
CH2
O
O
O
O
P
OH
O
O
N
CH3
CH3
H3C
HC
H
H
C
CH2
O
O
O
O
H2O O
P
OH
OH
O
O
+
+
Phospholipase C
Degumming of feedstock oils by hydrolyisis of phospholipids can be catalyzed by phospholipase C. Treatment of phosphatidylethanol, phosphatidylcholine and phosphatidylinositol with phospholipase C enables the hydrolysis and phase separation of the hydrophilic phosphate-containing contaminants.
Order sigma.com/order Technical service sigma.com/techinfo sigma.com/lifescience 25
BioDiesel AnalysisGC Columns for BioDiesel Analysis
MET-Biodiesel
This rugged metal column was designed specifically for the determination of free and total glycerin in B100 biodiesel samples. Features and benefits of this column include:
Metal is used as the column material, •virtually eliminating accidental column breakage during handling
Metal columns do not require a coating •to provide strength (NOTE: the protective polyimide coating on the outside of fused silica columns slowly burns off at 380 °C, exposing bare fused silica which is fragile and susceptible to breakage)
Includes a guard that both protects the •analytical column from excess reagent and non-volatile compounds, extending column life, and acts as a retention gap, minimizing peak broadening
The guard is an integrated guard, thereby •providing protection with a leak-free connection (the guard and analytical column are one continuous piece of tubing; there is no union between the guard and analytical column)
Low bleed characteristic, even at 380 °C•Provides good peak shape and resolution •for all glyceride impurities of interest
Able to separate glycerin in addition to •mono-/diglycerides (as methyl esters) plus triglycerides from the FAMEs
A maximum temperature of 380 °C •(isothermal) and 430 °C (programmed) exceeds the temperature limitations specified in biodiesel methods such as ASTM D6584 and EN 14105
GC capillary columns
Temp. Limits:
•–60°Cto380°C(isothermal)
•–60°Cto430°C(programmable)
0 10 20Min
1
2
4
3 56
1. Glycerin2. Butanetriol (I.S.)3. Monoolein4. Tricaprin (I.S.)5. Diolein6. Triolein
28668-U 1 ea
Derivatization
N-Methyl-N-(tri methyl silyl)tri fluoro acet -amide
MSTFA; N-Tri methyl silyl-N-methyl tri-fluoro acet amide[24589-78-4] CF3CON(CH3)Si(CH3)3 FW 199.25
SiCH3
NCH3
CH3F3C
O
H3C
Silylating agent used to form volatile derivatives for GC-MS analysis.2
Improved silylation procedure for simultaneous detection of steroid hormones 17-α-ethynylestradiol and estrone.1
Lit cited: 1. J. Chromatogr. 1108, 121 (2006); 2. Phosphorus, Sulfur Silicon Relat. Elem. 88, 53 (1994).
394866-10X1ML 10 × 1 mL394866-5ML 5 mL394866-25ML 25 mL
BioDiesel Calibration Standards
Supelco glycerin impurities in biodiesel reference solutions meet the specifications called out in ASTM D6584 and DIN EN 14105. Our reference solutions have been carefully formulated to save 4–6 hours in prep time, minimize the possibility of human error, and eliminate the need to prepare pyridine dilutions. Our standards offer:
Raw materials tested for identity and purity •Stock solutions for preparing your own •multi-component solutions
Multilevel, multi-component solutions •ready for derivatization
Monoglyceride commercial mixture for •EN14105
Internal standard solutions •Certificate of composition shipped with •each standard
Instructions for derivatization with each kit •Our standards are manufactured under the Quality Management System which is registered under ISO 9001:2000.
26
Name Suitability Composition Cat. No.
ASTM® D6584 Individual Standard Solution and Internal Standards Kit
D6584 ASTM ASTM® D6584 Standard Solution 1 (Supelco 44899-U), 1 mLASTM® D6584 Standard Solution 2 (Supelco 44914-U), 1 mLASTM® D6584 Standard Solution 3 (Supelco 44915-U), 1 mLASTM® D6584 Standard Solution 4 (Supelco 44916-U), 1 mLASTM® D6584 Standard Solution 5 (Supelco 44917-U), 1 mLASTM D6584 1,2,4-Butanetriol Solution, Internal Standard #1 (Supelco 44896-U), 5 mLASTM D6584 Tricaprin Solution, Internal Standard #2 (Supelco 44897-U), 5 mL
44918-U
ASTM® D6584 Standard Solution 1 D6584 ASTM 1,3-Diolein, 50 μg/mLGlycerol, 5 μg/mLMonoolein, 100 μg/mLGlyceryl trioleate, 50 μg/mL
44899-U
ASTM® D6584 Standard Solution 2 D6584 ASTM 1,3-Diolein, 100 μg/mLGlycerol, 15 μg/mLMonoolein, 250 μg/mLGlyceryl trioleate, 100 μg/mL
44914-U
ASTM® D6584 Standard Solution 3 D6584 ASTM 1,3-Diolein, 200 μg/mLGlycerol, 25 μg/mLMonoolein, 500 μg/mLGlyceryl trioleate, 200 μg/mL
44915-U
ASTM® D6584 Standard Solution 4 D6584 ASTM 1,3-Diolein, 350 μg/mLGlycerol, 35 μg/mLMonoolein, 750 μg/mLGlyceryl trioleate, 350 μg/mL
44916-U
ASTM® D6584 Standard Solution 5 D6584 ASTM 1,3-Diolein, 500 μg/mLGlycerol, 50 μg/mLMonoolein, 1000 μg/mLGlyceryl trioleate, 500 μg/mL
44917-U
EN 14105:2003 Monoglyceride Stock Solution EN 14105 DIN MonooleinMonopalmitinMonostearin
49446-U
EN 14105:2003 Standard Solution 1 EN 14105 DIN Butanetriol, 80 μg/mL1,3-Diolein, 50 μg/mLGlycerol, 5 μg/mLMonoolein, 250 μg/mLTricaprin, 800 μg/mLTriolein, 50 μg/mL
49441-U
EN 14105:2003 Standard Solution 2 EN 14105 DIN Butanetriol, 80 μg/mLDiolein, 200 μg/mLGlycerol, 20 μg/mLMonoolein, 600 μg/mLTricaprin, 800 μg/mLTriolein, 150 μg/mL
49442-U
EN 14105:2003 Standard Solution 3 EN 14105 DIN Butanetriol, 80 μg/mLDiolein, 350 μg/mLGlycerol, 35 μg/mLMonoolein, 950 μg/mLTricaprin, 800 μg/mLTriolein, 300 μg/mL
49443-U
EN 14105:2003 Standard Solution 4 EN 14105 DIN Butanetriol, 80 μg/mLDiolein, 500 μg/mLGlycerol, 50 μg/mLMonoolein, 1250 μg/mLTricaprin, 800 μg/mLTriolein, 400 μg/mL
49444-U
EN 14105:2003 Standard Solution Kit EN 14105 DIN EN 14105:2003 Standard Solution 1 (Supelco 49441-U), 1 mLEN 14105:2003 Standard Solution 2 (Supelco 49442-U), 1 mLEN 14105:2003 Standard Solution 3 (Supelco 49443-U), 1 mLEN 14105:2003 Standard Solution 4 (Supelco 49444-U), 1 mL
49445-U
Biodiesel Calibration Standards
Order sigma.com/order Technical service sigma.com/techinfo sigma.com/lifescience 27
Name Grade Cat. No.
HYDRANAL®-Composite 1 one-component reagent for volumetric Karl Fischer titration 34827-500ML-R34827-6X500ML-R34827-1L-R34827-6X1L-R
HYDRANAL®-Composite 2 one-component reagent for volumetric Karl Fischer titration 34806-500ML34806-6X500ML34806-1L34806-6X1L34806-2.5L34806-4X2.5L
HYDRANAL®-Composite 5 one-component reagent for volumetric Karl Fischer titration 34805-500ML-R34805-6X500ML-R34805-1L-R34805-6X1L-R34805-2.5L-R34805-4X2.5L-R
HYDRANAL®-Composite 5 K one-component reagent for volumetric Karl Fischer titration in ketones and aldehydes 34816-500ML-R34816-6X500ML-R34816-1L-R34816-6X1L-R34816-2.5L-R34816-4X2.5L-R
HYDRANAL®-CompoSolver E – 34734-1L-R34734-6X1L-R34734-2.5L-R34734-4X2.5L-R
HYDRANAL®-KetoSolver – 34738-500ML-R34738-6X500ML-R34738-1L-R34738-6X1L-R
HYDRANAL®-LipoSolver CM – 37855-1L37855-6X1L
HYDRANAL®-LipoSolver MH – 37856-1L37856-6X1L
HYDRANAL®-Medium K – 34698-1L-R34698-6X1L-R
HYDRANAL®-Methanol dry – 34741-1L-R34741-6X1L-R34741-2.5L-R34741-4X2.5L-R
HYDRANAL®-Methanol Rapid – 37817-1L-R37817-6X1L-R37817-2.5L-R37817-4X2.5L-R
HYDRANAL®-Solver (Crude) oil – 34697-1L-R34697-6X1L-R34697-2.5L-R34697-4X2.5L-R
HYDRANAL®-Working Medium K – 34817-1L34817-6X1L
Karl-Fischer reagent for titrimetric determination of water with one solution 36115-1L36115-6X1L
Karl Fischer Titration—HYDRANAL® Reagents for the Determination of Water in Biodiesel
The presence of water in biodiesel poses problems for a number of reasons. Some of the water is residual from processing while some comes from condensation in
the storage tanks. Water content can be determined accurately and reproducibly by Karl Fischer Titration (volumetric, coulometric, and KF-oven methods) using reliable, superior, and proven HYDRANAL reagents (EN 14214).
One-Component Volumetric Reagents
Biodiesel contains components of different chain lengths. Therefore, a solubilizer is often required to dissolve or disperse it in order to extract the moisture. A number of HYDRANAL media are available for effective dispersion of biodiesel. HYDRANAL-Composite 2 is used as the titration agent.
One Component Reagents
28
Two-Component Volumetric Reagents
Name Grade Cat. No.
HYDRANAL®-Solvent – 34800-1L-R34800-6X1L-R34800-2.5L-R34800-4X2.5L-R
HYDRANAL®-Solvent E – 34730-500ML-R34730-6X500ML-R34730-1L-R34730-6X1L-R34730-2.5L-R34730-4X2.5L-R
HYDRANAL®-Solvent CM – 34812-1L34812-6X1L34812-2.5L34812-4X2.5L
HYDRANAL®-Solvent Oil – 34749-1L34749-6X1L
HYDRANAL®-Titrant 2 – 34811-500ML34811-6X500ML34811-1L34811-6X1L
HYDRANAL®-Titrant 5 – 34801-500ML34801-6X500ML34801-1L34801-6X1L34801-2.5L34801-4X2.5L
HYDRANAL®-Titrant 2 E – 34723-1L-R34723-6X1L-R
HYDRANAL®-Titrant 5 E – 34732-100ML-R34732-500ML-R34732-6X500ML-R34732-1L-R34732-6X1L-R34732-2.5L-R34732-4X2.5L-R
Karl-Fischer reagent for titrimetric determination of water with two separate solutions 36116-1L36116-6X1L
Karl-Fischer reagent for titrimetric determination of water with two separate solutions 36117-1L36117-6X1L
Order sigma.com/order Technical service sigma.com/techinfo sigma.com/lifescience 29
Coulometric Titration Reagents
The coulometric procedure is more sensitive than the volumetric titration method. Determination of water is carried out in a coulometric cell (with or without diaphragm). The precision of the coulometric cell and the sample manipulation can be tested by means of HYDRANAL Water Standard 0.10.
Name Grade Cat. No.
HYDRANAL®-Coulomat A anolyte for coulometric Karl Fischer titration (for cells with diaphragm) 34807-500ML34807-6X500ML
HYDRANAL®-Coulomat E – 34726-500ML-R34726-6X500ML-R
HYDRANAL®-Coulomat AD reagent for coulometric Karl Fischer titration for cells without diaphragm 34810-500ML-R34810-6X500ML-R
HYDRANAL®-Coulomat AF 7 anolyte for coulometric Karl Fischer titration (suitable for coulometer AF7) 34829-1L-R34829-6X1L-R
HYDRANAL®-Coulomat AG anolyte for coulometric Karl Fischer titration. Suitable for cells with and without diaphragm 34836-500ML-R34836-6X500ML-R34836-1L-R34836-6X1L-R
HYDRANAL®-Coulomat AG-H anolyte for coulometric Karl Fischer titration in long-chained hydrocarbons (free of halogenated hydrocarbons)
34843-500ML34843-6X500ML
HYDRANAL®-Coulomat AG-Oven – 34739-500ML-R34739-6X500ML-R
HYDRANAL®-Coulomat AK anolyte for coulometric Karl Fischer titration in ketones (for cells with and without diaphragm) 34820-500ML-R34820-6X500ML-R
HYDRANAL®-Coulomat CG catholyte for coulometric Karl Fischer titration. Free of halogenated hydrocarbons 34840-50ML-R34840-6X50ML-R
HYDRANAL®-Coulomat CG-K – 34821-50ML-R34821-6X50ML-R
HYDRANAL®-Coulomat Oil – 34868-100ML-R34868-6X100ML-R34868-500ML-R34868-6X500ML-R
Karl Fischer Oven products
This method is suitable for samples that release water at a higher temperature. In this method, HYDRANAL-Coulomat CG is placed in the cathode chamber and HYDRANAL Coulomat AG Oven is added to the anode chamber of a coulometric cell with diaphragm. A cell without a diaphragm requires only the Coulomat AG Oven. HYDRANAL Coulomat AG-H or HYDRANAL Coulomat AD may be used as a replacement for HYDRANAL Coulomat AG Oven. HYDRANAL Molecular Sieve 0.3 mm is a drying medium for the carrier gas.
Name Grade Cat. No.
HYDRANAL®-Coulomat AG-Oven – 34739-500ML-R34739-6X500ML-R
HYDRANAL®-Coulomat CG catholyte for coulometric Karl Fischer titration. Free of halogenated hydrocarbons 34840-50ML-R34840-6X50ML-R
HYDRANAL®-Molecular sieve 0.3 nm – 34241-250G-R34241-1KG-R
HYDRANAL®-Water Standard KF-Oven, 140–160 °C
– 34693-10G-R
HYDRANAL®-Water Standard KF-Oven 220 °C–230 °C
– 34748-10G-R34748-6X10G-R
30
Metabolite Standards for Mevalonate and Isoprenoid Pathway Analysis
Metabolite Standards for Mevalonate and Isoprenoid Pathway Analysis
ETHANOL ISOPENTANOL PROPANOL BUTANOL
Acetaldehyde Valeryl-CoA Propionyl-CoA Butyryl-CoA
Acetyl-CoA Acetoacetyl-CoAPyruvatePEPG3P
1-Deoxy-D-xylulose-5-phosphate
2-C-Methyl-D-erythritol-4-phosphate
TCA-Cycle
3-Hydroxy-3-methyl-glutaryl-CoA
Mevalonate
Mevalonate-5-phosphate
Mevalonate-5-pyrophosphate
Isopentenyl-pyrophosphateDimethylallyl-pyrophosphate
Geranyl-pyrophosphate
(E,E)-Farnesyl-pyrophosphate
Geranylgeranyl-pyrophosphate
Isopentenol
Isopentanol
Even-numberedfatty acid
Odd-numberedfatty acid
Even-numberedalkane
Odd-numberedfatty alcohol
Even-numberedfatty alcohol
Odd- numberedalkane
Esters
Esters
GeraniolMonoterpene
Sesquiterpene Farnesol
Diterpene Geranylgeraniol
Alternatives to the classical glycolysis and fermentation pathways are also being studied as sources of common biofuels as well as potential sources of new biofuels such as isoprenoids. The mevalonate-isoprenoid pathway may prove to be a rich source of a variety of hydrocar-bon-based biofuels.
Sigma-Aldrich’s comprehensive and unique range of metabolites enables new approaches towards molecular understanding of the relevant mevalonate pathway (center) and the DXP pathway (left) towards the isoprenoid compounds (bottom), the fatty-acid or fatty acyl-CoA pathways (top and right) towards the different alcohols, esters and alkanes.
Name Cat. No.Acetoacetyl coenzyme A sodium salt hydrate A1625-5MG
A1625-10MGA1625-25MG
Acetyl coenzyme A sodium salt, powder A2056-1MGA2056-5MGA2056-10MG
Acetyl coenzyme A trilithium salt A2181-1MGA2181-5MGA2181-10MG
Butyryl coenzyme A lithium salt hydrate B1508-5MGB1508-10MGB1508-25MG
1-Deoxy-d-xylulose-5-phosphate sodium salt 13368-1MG13368-5MG
γ,γ-Dimethylallyl pyrophosphate triammonium salt D4287-1VLD4287-5VL
Farnesyl monophosphate ammonium salt solution, methanol:ammonia solution
F1803-5VL
Farnesyl pyrophosphate ammonium salt solution, methanol:ammonia solution
F6892-1VLF6892-5VL
Geranylgeranyl monophosphate ammonium salt solution, methanol:ammonia solution
G2543-5VL
Geranylgeranyl pyrophosphate ammonium salt solution methanol:ammonia solution
G6025-1VLG6025-5VL
Geranyl monophosphate ammonium salt solution, methanol:ammonia solution
G2293-1VLG2293-5VL
Geranyl pyrophosphate ammonium salt G6772-1VLG6772-5VL
dl-Glyceraldehyde 3-phosphate solution G5251-25MGG5251-100MG
dl-3-Hydroxy-3-methylglutaryl coenzyme A sodium salt H6132-5MGH6132-10MG
Isopentenyl monophosphate ammonium salt solution I1157Isopentenyl pyrophosphate triammonium salt solution I0503-1VL
I0503-5VL(R)-Mevalonic acid sodium salt 41288(±)-Mevalonic acid 5-phosphate trilithium salt hydrate 79849-10MG
79849-50MG(R)-Mevalonic acid 5-pyrophosphate tetralithium salt 77631(±)-Mevalonic acid 5-pyrophosphate tetralithium salt 94259-10MG
94259-50MG(R)-(−)-Mevalonolactone 68519-100MG(±)-Mevalonolactone M4667-1GPhospho(enol)pyruvic acid monopotassium salt P7127-100MGPhospho(enol)pyruvic acid monosodium salt hydrate P0564-100MGPhospho(enol)pyruvic acid trisodium salt hydrate P7002-100MGn-Propionyl coenzyme A lithium salt P5397-5MGPyruvic acid 107360-25GSodium pyruvate 15990-25G
Renewable and Alternative Energy Web Portal
Have you seen these Material MattersTM issues on Alternative Energy?
Get your complimentary subscription today: sigma-aldrich.com/mm
The Portal offers a comprehensive set of links about environmentally benign production, storage and conversion of energy.
Solar Energy•Hydrogen Economy•Batteries•Supercapacitors•Alternative Fuels•Relevant events and conferences are also highlighted.•
We focus on materials, so you can focus on results. For more information, visit sigma-aldrich.com/renewable
sigma-aldrich.com
Alternative EnergyPhotovoltaics, Ionic Liquids, and MOFs
Solar light is energy for everyone
Effi cient Dye-Sensitized Solar Cells for Direct Conversion of Sunlight to Electricity
Organic Dyes for Effi cient and Stable Dye-Sensitized Solar Cells
The Relentless Rise of Disruptive PhotovoltaicsIonic Liquids for Energy Storage Applications
Selected Applications of Metal-Organic Frameworks in Sustainable Energy Technologies
TM
Vol. 4, No. 4
MPC73457-510295
1050
Order/Customer Service (800) 325-3010 • Fax (800) 325-5052 Technical Service (800) 325-5832 • sigma-aldrich.com/techservice Development/Custom Manufacturing Inquiries (800) 244-1173 Safety-related Information sigma-aldrich.com/safetycenter
Sigma-Aldrich® Worldwide Offices
©2010 Sigma-Aldrich Co. All rights reserved. SIGMA, SAFC, SIGMA-ALDRICH, ALDRICH, FLUKA, and SUPELCO are trademarks belonging to Sigma-Aldrich Co. and its affiliate Sigma-Aldrich Biotechnology, L.P. Sigma brand products are sold through Sigma-Aldrich, Inc. Sigma-Aldrich, Inc. warrants that its products conform to the information contained in this and other Sigma-Aldrich publications. Purchaser must determine the suitability of the product(s) for their particular use. Additional terms and conditions may apply. Please see reverse side of the invoice or packing slip. ASTM is a registered trademark of American Society for Testing and Materials, Biomek is a registered trademark of Beckman Instruments, Inc., HypoThermosol is a registered trademark of BioLife Solutions, Inc., CryoStor is a trademark of BioLife Solutions, Inc., CellBIND, Corning and HYPER Flask are registered trademarks of Corning, Inc., TWEEN is a registered trademark of Croda International PLC, Triton is a registered trademark of Dow Chemical Co., Nafion is a registered trademark of E.I. du Pont de Nemours & Co., Inc., Eppendorf is a registered trademark of Eppendorf-Netheler-Hinz GmbH, Cy and Sepharose are registered trademarks of GE Healthcare, nanoHA, Select-HA are trademarks of Hyalose LLC, Coomassie is a registered trademark of Imperial Chemical Industries Ltd., Legato is a trademark of KDScientific, Driselase is a registered trademark of Kyowa Hakko Kogyo Co. Ltd., Alexa, SYBR amd Texas Red are registered trademarks of Molecular Probes, Inc., Nanomiser is a trademark of nGimat, Carezyme, Celluclast, Fungamyl, Novozym, Pectinex, Pentopan and Termamyl are registered trademarks of Novozymes Corp., BAN is a trademark of Novozymes Corp., Shimadzu is a registered trademark of Shimadzu Corporation, Aldrich, HYDRANAL and Prestige Antibodies are registered trademarks of Sigma-Aldrich Biotechnology LP and Sigma-Aldrich Co., and Ampliflu, EZBlue, GlycoProfile, HumanKine, Material Matters, ProteoMass, ProteoSilver and Sigma are trademarks of Sigma-Aldrich Biotechnology LP and Sigma-Aldrich Co.
World Headquarters 3050 Spruce St.
St. Louis, MO 63103 (314) 771-5765
sigma-aldrich.com
Accelerating Customers’ Success through Innovation and Leadership in Life Science, High Technology and Service
ArgentinaFree Tel: 0810 888 7446 Tel: (+54) 11 4556 1472 Fax: (+54) 11 4552 1698
AustraliaFree Tel: 1800 800 097 Free Fax: 1800 800 096 Tel: (+61) 2 9841 0555 Fax: (+61) 2 9841 0500
AustriaTel: (+43) 1 605 81 10 Fax: (+43) 1 605 81 20
BelgiumFree Tel: 0800 14747 Free Fax: 0800 14745 Tel: (+32) 3 899 13 01 Fax: (+32) 3 899 13 11
BrazilFree Tel: 0800 701 7425 Tel: (+55) 11 3732 3100 Fax: (+55) 11 5522 9895
CanadaFree Tel: 1800 565 1400 Free Fax: 1800 265 3858 Tel: (+1) 905 829 9500 Fax: (+1) 905 829 9292
ChileTel: (+56) 2 495 7395 Fax: (+56) 2 495 7396
ChinaFree Tel: 800 819 3336 Tel: (+86) 21 6141 5566 Fax: (+86) 21 6141 5567
Czech RepublicTel: (+420) 246 003 200 Fax: (+420) 246 003 291
DenmarkTel: (+45) 43 56 59 00 Fax: (+45) 43 56 59 05
FinlandTel: (+358) 9 350 9250 Fax: (+358) 9 350 92555
FranceFree Tel: 0800 211 408 Free Fax: 0800 031 052 Tel: (+33) 474 82 28 88 Fax: (+33) 474 95 68 08
GermanyFree Tel: 0800 51 55 000 Free Fax: 0800 64 90 000 Tel: (+49) 89 6513 0 Fax: (+49) 89 6513 1160
HungaryIngyenes telefonszám: 06 80 355 355 Ingyenes fax szám: 06 80 344 344 Tel: (+36) 1 235 9063 Fax: (+36) 1 269 6470
IndiaTelephone Bangalore: (+91) 80 6621 9400 New Delhi: (+91) 11 4358 8000 Mumbai: (+91) 22 2570 2364 Hyderabad: (+91) 40 4015 5488 Kolkata: (+91) 33 4013 8003 Fax Bangalore: (+91) 80 6621 9550 New Delhi: (+91) 11 4358 8001 Mumbai: (+91) 22 4087 2364 Hyderabad: (+91) 40 4015 5488 Kolkata: (+91) 33 4013 8000
IrelandFree Tel: 1800 200 888 Free Fax: 1800 600 222 Tel: (+353) 402 20370 Fax: (+ 353) 402 20375
IsraelFree Tel: 1 800 70 2222 Tel: (+972) 8 948 4100 Fax: (+972) 8 948 4200
ItalyFree Tel: 800 827 018 Tel: (+39) 02 3341 7310 Fax: (+39) 02 3801 0737
JapanTel: (+81) 3 5796 7300 Fax: (+81) 3 5796 7315
Korea Free Tel: (+82) 80 023 7111 Free Fax: (+82) 80 023 8111 Tel: (+82) 31 329 9000 Fax: (+82) 31 329 9090
MalaysiaTel: (+60) 3 5635 3321 Fax: (+60) 3 5635 4116
MexicoFree Tel: 01 800 007 5300 Free Fax: 01 800 712 9920 Tel: (+52) 722 276 1600 Fax: (+52) 722 276 1601
The NetherlandsFree Tel: 0800 022 9088 Free Fax: 0800 022 9089 Tel: (+31) 78 620 5411 Fax: (+31) 78 620 5421
New ZealandFree Tel: 0800 936 666 Free Fax: 0800 937 777 Tel: (+61) 2 9841 0555 Fax: (+61) 2 9841 0500
NorwayTel: (+47) 23 17 60 00 Fax: (+47) 23 17 60 10
PolandTel: (+48) 61 829 01 00 Fax: (+48) 61 829 01 20
PortugalFree Tel: 800 202 180 Free Fax: 800 202 178 Tel: (+351) 21 924 2555 Fax: (+351) 21 924 2610
RussiaTel: (+7) 495 621 5828 Fax: (+7) 495 621 6037
SingaporeTel: (+65) 6779 1200 Fax: (+65) 6779 1822
SlovakiaTel: (+421) 255 571 562 Fax: (+421) 255 571 564
South AfricaFree Tel: 0800 1100 75 Free Fax: 0800 1100 79 Tel: (+27) 11 979 1188 Fax: (+27) 11 979 1119
SpainFree Tel: 900 101 376 Free Fax: 900 102 028 Tel: (+34) 91 661 99 77 Fax: (+34) 91 661 96 42
SwedenTel: (+46) 8 742 4200 Fax: (+46) 8 742 4243
SwitzerlandFree Tel: 0800 80 00 80 Free Fax: 0800 80 00 81 Tel: (+41) 81 755 2828 Fax: (+41) 81 755 2815
United KingdomFree Tel: 0800 717 181 Free Fax: 0800 378 785 Tel: (+44) 1747 833 000 Fax: (+44) 1747 833 313
United StatesToll-Free: 800 325 3010 Toll-Free Fax: 800 325 5052 Tel: (+1) 314 771 5765 Fax: (+1) 314 771 5757
VietnamTel: (+84) 3516 2810 Fax: (+84) 6258 4238
Internet sigma-aldrich.com