A reversible inhibitor of an enzyme was studied by kinetic analysis of the enzym

Question

A reversible inhibitor of an enzyme was studied by kinetic analysis of the enzyme. When the inhibitor was present in the knetic experiment at a concentration that achieved 505 inhibition of the activity measure in the normal activity assay (saturating substrate concentration), the following was observed (the results of a control kinetic experiment done without inhibitor are also shown for comparison):

Km for substate A: No [I] Present: 0.52 +- 0.11, With [I] Present 0.55 +/- 0.20

Km for substrate B: No [I] Present: 2.2 +/- 0.4, With [I] present 4.5 +/- 0.5

Vmax: No[I] 110 +/- 5, With I present 112 +/- 10

a) What type of inhibtion is occuring?

b) does either both or neither follown Michaelis-Menten Kinetics?

c) What type of inhibition is occuring?

Explanation / Answer

In competitive inhibition:

In non-completive inhibition:

In uncompetitive inhibition:

Both Km and Vmax decreased

Based on the given data,

The Km of the both substrate A and substrate B is increased in the presence Inhibitor and the Vmax remains in unchanged, so it is a competitive inhibition.

Since, it is a reversible inhibitor both substrate A and substrate B followed Michaelis-Menten Kinetics.

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