Enzymology, enzymes graph, Michaekis menton

1. Topic: Interpretation of Michaelis Menten
Equation

2. 1. Khadija Khawar
2. Roll # 14011579-010
3. Section B
4. Biotechnology
5. University of gujrat

3. (Double reciprocal plot)

5. Km=k₂+k-₁/k1
When:
k₂ is rate limiting
k₂˂˂k-₁
Km reduces to k-₁ ̷ k₁→kd (dissociation constant)
then,
Km does not represent a measure of affinity of the
enzyme for its substrate in ES complex.
Sometimes k₂˃˃k_₁ , then km =k₂ ̷ k_₁

6.  In some cases the reaction goes through several
steps after the formation of ES complex, km can
become a more complex function of many rate
constants.
 The quantityVmax also varies from one enzyme to
the next.
 if enzyme reacts by two steps
Vmax=k₂[ Et]
 The number of reaction steps and identity of rate
limiting step can vary from enzyme to enzyme.
Michaelis Menten equation as rate
equation:

7.  for example:-
 Vmax=k3[Et]
 Vo= k₂[E][S] ̷ Km+[S]
 K₂[Et]
 Vo=Vmax [s] ̷ km+[S]
Michaelis Menten equation as rate
equation:

9. There are two cases of substrate
concentration
1. At low [S], Km >>[S]
Vo= Vmax[S]/Km
1. At high [S], [S]>> Km
Vo=Vmax Michaelis Menten curve