Tyrosine & TryptophanTyrosine & Tryptophan

Submitted to: Submitted by:-Dr. Jawaid Ahsan Swati Kumari(Dept. of Biological science) M.Sc. BioinformaticsBiotechnology 2nd Semester

CUB14031220222014-2016

ContentsContents Introduction Overview Structure History Biosynthesis Catabolism Source Function Uses Defficiencies References

TyrosineTyrosine

IntroductionIntroduction

Tyrosine, organic compound, one of the 20 amino acids commonly found in animal proteins.

It is a non-essential amino acid with a polar side group.

Its codons are UAC and UAU.

A hydrophillic amino acid which is a constituent of most proteins and is important in the synthesis of some hormone.

OverviewOverview Molecular formula :- C9H11NO3

Three letter code :- Tyr

One letter code :- Y

IUPAC Name :- Tyrosine

Alternative Name :- L -2-Amino-3-(4-hydroxyphenyl)propanoic acid

Chemical Properties :- Aromatic Group & Hyroxyl Group

Physical Property :- Non Polar

Basic Property :- pI – 5.66

Occurance in protein :- 3.2%

Solubility in water :- Very soluble

StructureStructure Nonpolar aromatic

amino acid, contain o hydroxyl group attached to an aromatic ring.

Hydroxyl group is paticularly important because theae residue are utilized in the phasphorylation of other protein.

3D structure & PDB coding3D structure & PDB coding

HistoryHistory

First discovered by German chemist Justus von Liebig in 1846.

The word "tyrosine" is from the Greek tyros, which meaning is “cheese”.

Also called “Tyrosyl”, when reffered to as a “functional group” or side chain.

BiosynthesisBiosynthesis

It is not essential to the human diet, since it can be synthesized in the body from “phenylalanine”.

The conversion of “phe” to “tyr” is catalized by the enzyme “phenylalanine hydroxylase”.

Phenaylalanine & Tyrosine CatabolismPhenaylalanine & Tyrosine Catabolism

As we know that the tyrosine is derive from phenylalanine.

Thus, phenylalanine catabolism always follows the pathway of tyrosine catabolism.

Tyrosine is equally important for protein biosynthesis as well as an intermediate in the biosynthesis of several physiologically important metabolites

e.g. dopamine, norepinephrine and epinephrine.

Phenaylalanine & Tyrosine CatabolismPhenaylalanine & Tyrosine Catabolism

SourceSource Tyrosine, non-essential which can also be synthesized in the our body

from phenylalanine.

It is found in many high-protein food products such as :-

chicken,

fish,

milk,

yogurt,

cheese,

peanuts, almonds,

soy products,

lima beans,

Cottage,

bananas.

FunctionsFunctions Precursor to neurotransmitters dopamine, norepinephrine,

epinephrine (adrenaline) and melanin.

The Antidepressant- Effective anti-depressant for norepinephrine-deficient depressions.

Acts as a mood elevator; a lack of adequate amounts of tyrosine leads to a deficiency of norepinephrine in the brain, which in turn can result in depression.

Suppresses the appetite

Helps to reduce body fat.

It aids in the production of melanin (the pigment responsible for skin and hair color)

Also it aids in the functions of the adrenal, thyroid, and pituitary glands.

Increases energy, improves mental clarity and concentration.

USESUSES

Tyrosine can be used as a safe and lasting therapy, useful in a variety of clinical situations-depression, hypertension, Parkinson's disease, low sex drive, appetite suppression and therapy for cocaine addicts .

Tyrosine fights all kinds of stress because it is the precursor of adrenalin, which is used up during stress.

DeficienciesDeficiencies Phenylketonuria (PKU) -

Phenylketonuria is “inherited disorder”, increase the level of phenylalanine in the blood due to break down of phenylalanine into tyrosine not active.

Women who have high levels of phenylalanine during pregnancy are at high risk for having babies born with mental retardation, heart problems, small head size and developmental delay. This is because the babies are exposed to their mother's very high levels of phenylalanine before they are born.

Parkinson's Disease -

Also called PD, Hypokinetic Rigid Syndrome (HRS), disorder of the control nervous system.

DeficienciesDeficiencies

Hyperthyroidism -

It is “endocrine disorder” .

In this disorder thyroid gland doesn't produced enough thyroid hormone.

Drug addiction and dependency Depression low blood pressure low body temperature (such as cold hands and feet) restless leg syndrome.

TyptophanTyptophan

IntroductionIntroduction

Tryptophan , organic compound, one of the 20 amino acid commonly found in animal proteins.

It is “essential amino acid”.

Tryptophan is an amino acid needed for normal growth in infants and for nitrogen balance in adults.

Its codons are UGG.

OverveiwOverveiw Molecular formula :- C11H12N2O2

Three letter code :- Trp

One letter code :- W

IUPAC Name :- Typrtophan

Alternative Name :- indole-3-alanie

Chemical Properties :- Aromatic Group

Physical Property :- Non Polar

Basic Property :- pI – 5.89

Occurance in protein :- 1.4 %

Solubility in water :- soluble in hot alchohal, insoluble in chloroform

StructureStructure

Typtophan is an amino acid of aromatic ring of nitrogen & hydrogen group and is hydrophillic.

One of the side chain is 5 membered while the other is 6 and 2 carbon are shared by both aromatic ring.

3D structure & PDB coding3D structure & PDB coding

HistoryHistory

The amino acid was isolated from casein (milk protein) in 1901, by Frederick Hopkins.

Its structure was established in 1907.

Tryptophan metabolismTryptophan metabolism

Firstly Tryptophan is converted into 5-Hydroxy-tryptophan with the help of enzme Tryptophan hydroylase.

With the help of enzme Decarboxylase 5-Hydroxy-tryptophan is converted into Serotonin, which is important for normal nerve and brain function.

SourceSource Tryptophan is an essential amino acid, meaning we need to get it from

our diet because our body cannot produce it.

Rich Food Sources of Tryptophan :-

Cheese

Chicken

Eggs

Fish

Milk

Nuts

Soya

Pumpkin seed

Peanuts

Turkey

FunctionFunction Production of Niacin (Vitamin B) The Sleep Promoter : Effective sleep aid, due to conversion to

serotonin. Reduces anxiety. Effective in some forms of depression and to stabilize moods. Treatment for migraine headaches. Stimulates growth hormone. Helps to control hyperactivity in children. Alleviates stress. Aids in weight control by reducing appetite. Produce sertonin, a neurotransmitter important for normal nerve

and brain function.

UsesUses

Tryptophan is also beneficial in some forms of schizophrenia; it probably acts by balancing dopamine excess.

Patients with kidney failure, on birth control pills, or with Down's syndrome may need more tryptophan.

DeficienciesDeficiencies

Pellagra -

It is “vitamin-deficiency disease” most frequency caused by a chronic lack of niacin (vitamin B) in diet.

Insomnia -

Also known as “Sleepnees” is a sleep disorder in which there is an inability to fall asleep or to stay asleep as long as desired.

ALS -

Also called “Amyotrophic lateral sclerosis” is specific disorder that involves the death of neurons.

DeficienciesDeficiencies Fructose malabsorption -

The disorder fructose malabsorption causes improper absorption of tryptophan in the intestine, reduced levels of tryptophan in the blood,and depression.

Depression.

Diarreha.

Digestion problems.

Headaches.

Sleepness.

REFERENCESREFERENCES http://www.nlm.nih.gov/medlineplus/ency/article/002332.htm

http://chemistry.about.com/od/foodcookingchemistry/a/Tryptophan-Facts.htm

.http://www.nlm.nih.gov/medlineplus/ency/article/002332.htm

http://www.aminomics.com/aminoacids/tryptophan.htm

http://www.wolframalpha.com/input/?i=typtophan

http://www.dcnutrition.com/AminoAcids/Detail.CFM?RecordNumber=129

http://www.biology.arizona.edu/biochemistry/problem_sets/aa/tyrosine.html

http://bestvitaminsources.com/html_pgs/amino_acids_all/amino_tyrosine.html

http://orthomolecular.org/nutrients/tyrosine.html

http://www.healingwithnutrition.com/aminoacid.html

http://www.encyclopedia.com/topic/tyrosine.aspx

http://en.wikipedia.org/wiki/Tyrosine

http://www.wolframalpha.com/input/?i=tyrosine