Kinetics Overflow Flashcards
E + S ⇌ ES ⇌ E + P
what is k1?
equilibrium constant for forming enzyme-substrate from E and S.
k1 = [ES]/[E][S]
E + S ⇌ ES ⇌ E + P
what is k2?
equilibrium constant for forming enzyme + product from ES.
k2 = [E][P]/[ES]
E + S ⇌ ES ⇌ E + P
how to calculate Rate1?
Rate1 = k1 [E][S]
(rate constant k1 = [ES]/[E][S]), assumed to be
E + S ⇌ ES ⇌ E + P
how to calculate Rate2?
Rate2 = k2 [ES]
( rate constant k2 = kcat = Vmax/[E]t )
steady-state assumption in enzyme kinematics
E + S ⇌ ES ⇌ E + P
steady-state assumption: [ES] is constant
formation of ES = loss of ES
Rate1 + Rate-2 = Rate-1 + Rate2
Rate-2 is generally ignored because we assume that formation of E + P is thermodynamically favourable and so that the reverse reaction is negligible, so
E + S ⇌ ES ⟶ E + P
Rate1 = Rate-1 + Rate2
E + S ⇌ ES ⇌ E + P
what is the rate of formation of ES?
Rate1 + Rate-2
both of these reactions lead to formation of ES, either from forward reaction of E+S ⟶ ES (Rate1) or reverse reaction of ES ⟵ E+P (Rate-2)
E + S ⇌ ES ⇌ E + P
Why do we generally ignore Rate-2?
( E + S ⇌ ES ⟶ E + P )
We assume
E + S ⇌ ES ⇌ E + P
how to calculate Rate-1?
Rate-1 = K-1 [ES]
(rate constant K-1 = [E][S]/[ES])