Enzyme Activity: Reversible Inhibition

Abstract

Data for the inhibition of enzyme‐catalysed reactions by substrate analogues provide inhibition patterns that are helpful for the elucidation of kinetic mechanisms. Analysis of such data yields values for true inhibition constants that give a measure of the strength of interaction between the enzyme and the inhibitor.

Keywords: enzyme inhibition; kinetic mechanisms; rate equations; inhibition constants; inhibition patterns

Figure 1.

Double reciprocal plots of initial velocity (v) against substrate concentration (A) at different fixed concentrations of inhibitors that gives rise to (a) linear competitive, (b) linear noncompetitive and (c) linear uncompetitive inhibition.

Figure 2.

Kinetic mechanisms for reactions with two substrates (A, B) and two products (P, Q).

Figure 3.

Kinetic mechanisms for the slow‐binding inhibition of enzyme‐catalysed reactions by substrate analogues.

Figure 4.

Progress curves for the slow‐binding inhibition of enzyme‐catalysed reactions by substrate analogues. The inhibition is described by either mechanism A (a) or mechanism B (b).

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Further Reading

Cleland WW (1963a) The kinetics of enzyme‐catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. Biochimica et Biophysica Acta 67: 104–137.

Cleland WW (1963b) The kinetics of enzyme‐catalyzed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory. Biochimica et Biophysica Acta 67: 173–187.

Cleland WW (1963c) The kinetics of enzyme‐catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection. Biochimica et Biophysica Acta 67: 188–196.

Cleland WW (1979) Statistical analysis of enzyme kinetic data. Methods in Enzymology 63: 103–138.

Morrison JF and Stone SR (1985) Approaches to the study and analysis of the inhibition of enzymes by slow‐ and tight‐binding inhibitors. Comments on Molecular and Cellular Biophysics 2: 347–368.

Morrison JF and Walsh CT (1988) The behavior and significance of slow‐binding enzyme inhibitors. Advances in Enzymology 59: 201–301.

Sculley MJ and Morrison JF (1986) The determination of kinetic constants governing the slow, tight‐binding inhibition of enzyme‐catalysed reactions. Biochimica et Biophysica Acta 874: 44–53.

Sculley MJ, Morrison JF and Cleland WW (1996) Slow‐binding inhibition: the general case. Biochimica et Biophysica Acta 1298: 78–86.

Szedlacsek SE and Duggleby RG (1995) Kinetics of slow and tight‐binding inhibition. Methods in Enzymology 249: 144–180.

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How to Cite close
Morrison, John F(Apr 2001) Enzyme Activity: Reversible Inhibition. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1038/npg.els.0000600]