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Updated: Jul 28, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Theoretical analysis of compartmented coupling in linear enzyme systems
S P Brooks1, K B Storey, C H Suelter
1Institute of Biochemistry, Carleton University, Ottawa, Ontario, Canada.
Abstract:
Exact equations which describe the kinetic patterns of enzyme/enzyme complexes, when compartmented coupling occurs between them, are presented. Compartmented coupling refers to the creation of a local environment in which the concentration of an intermediate, shared by two enzymes, is higher than its solution concentration. This results in a higher coupling enzyme activity, a condition reflected in a shorter transition time for the system. In this paper, equations are presented which allow experimenters to quantitate the effect of compartmented coupling in terms of changes in the apparent Km and Vmax values. The equations presented in this paper are more exact than those previously derived since they do not incorporate first order assumptions before derivation.
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