The pre-eminence of kcat. in the manifestation of optimal enzymic activity delineated by using the Briggs-Haldane two-step irreversible kinetic model
- 1 October 1976
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 159 (1), 165-166
- https://doi.org/10.1042/bj1590165
Abstract
The suggestion by Fersht that enzymes that provide maximal rates of catalysis should be characterized by values of Ks, the dissociation constant of the enzyme-substrate complex, greater than 10 times the value of the ambient substrate concentration was examined. For such enzymes Ks is not relevant, and attention is best focused on the relative numerical values of kcat (in units of s-1) and the substrate molarity. It is necessary only that the former be about 1010-1011 times the latter to ensure that the rate of product formation be diffusion-limited and thus maximal.This publication has 6 references indexed in Scilit:
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