The Michaelis constant, K m , is often spoken of as if it were a measure of
Fantastic news! We've Found the answer you've been seeking!
Question:
The Michaelis constant, Km, is often spoken of as if it were a measure of the affinity of the enzyme for the substrate: the lower the Km, the higher the binding affinity. This would be true if Km were the same as Kd (the equilibrium constant for the dissociation reaction), but it is not. For an enzyme-catalyzed reaction
A. In terms of these rate constants, what is Kd for dissociation of the ES complex to E + S?
B. Under what conditions is Km approximately equal to Kd?
C. Does Km consistently overestimate or underestimate the binding affinity? Or does it sometimes overestimate and sometimes underestimate the binding affinity?
Related Book For
Posted Date: