1. Please select the answer True or False Almost all irreversible enzyme inhibit

Question

1. Please select the answer True or False

Almost all irreversible enzyme inhibitors bind noncovalently to the enzyme.

2. Initial rate data for an enzyme that obeys Michaelis-Menten kinetics are shown in the following table. When the enzyme concentration is 3 nmol ml1, a Lineweaver-Burk plot of this data gives a line with a y-intercept of 0.00426 (mol1ml s).

When the reactions in part (B) are repeated in the presence of 12 M of an uncompetitive inhibitor, they-intercept of the Lineweaver-Burk plot is 0.352 (mol1 ml s). Calculate KI for this inhibitor.

Express your answer with the appropriate units.

(Part B answer was 124 micro meter)

Explanation / Answer

1. False

Inhibitor binding can stop substrate from binding to the active site. Inhibitor binding is of two types:-reversible or irreversible.

Irreversible inhibitors usually bind to the the enzyme via covalent bond. In contrast reversible inhibitors bind non-covalently.

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