Question

A competitive inhibitor changes both the K_M and vmax of a reaction.

A.True
B.False

Answer 1

False

Answer 2

A competitive inhibitor changes both the K_M and vmax of a reaction.

False

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In competitive inhibition, the maximum velocity (V_\max) of the reaction is unchanged, while the apparent affinity of the substrate to the binding site is decreased (the K_d dissociation constant is apparently increased). The change in K_m (Michaelis-Menten constant) is parallel to the alteration in K_d. Any given competitive inhibitor concentration can be overcome by increasing the substrate concentration in which case the substrate will outcompete the inhibitor in binding to the enzyme

Answer 3

False, competitive inhibitors do not change actual Km and Vmax.

Answer 4

hi

it is FALSE

Vmax is the maxim initial velocity (Vo) that an enzyme can achieve. Initial velocity is defined as the catalytic rate when substrate concentration is high, enough to saturate the enzyme, and the product concentration is low enough to neglect the rate of the reverse reaction. Therefore, the Vmax is the maximum catalytic rate that can be achieved by a particular enzyme. Km is determined as the substrate concentration at which 1/2 Vmax is achieved. This kinetic parameter therefore importantly defines the affinity of the substrate for the enzyme.
These two parameters for a specific enzyme defines:
Vmax - the rate at which a substrate will be converted to product once bound to the enzyme.
Km - how effectively the enzyme would bind he substrate, hence affinity.