ENZYMES ;KINETICS

V˳ It shows initial rate of reaction/forward reaction. Vmax Max. initial rate of catalyzed reaction(when all the

available enzyme is present as E-S complex),& all the E is saturated with S ,so further ↑ in S has no effect on rate /velocity.

STEADY STATE assumption E-S conc. remains constant. Rate of formation of E-S ≈ Rate of dissociation( E+P).

KmKm is S conc. (moles/L) at ⅟2 V max. 50% of E molecules are bound with S molecules

at that particular S conc.Km is independent of E conc.If E conc. Is doubled ,Vmax will be double. But

Km will remain same.

LINE-WEAVER BURK PLOT