The K_M can be considered to be the same as the dissociation constant K_S for E + S binding if A)the concentration of [ES] is unchanged. B)ES $\to$ E + P is fast compared to ES $\to$ E + S. C)k₁ k₂ D)k₂

Question

The K_M can be considered to be the same as the dissociation constant K_S for E + S binding if A)the concentration of [ES] is unchanged. B)ES $\to$ E + P is fast compared to ES $\to$ E + S. C)k₁ >> k₂ D)k₂ << k_-1. E)this statement cannot be completed because K_M can never approximate K_S.

Quizplus · Accepted Answer

K_M approximates K_S when the rate of product formation (k₂) is much smaller than the rate of substrate dissociation (k_-1), meaning the enzyme-substrate complex dissociates back to enzyme and substrate more readily than forming product.

The KM Can Be Considered to Be the Same as the Dissociation

The K_M Can Be Considered to Be the Same as the Dissociation