Deviation from Michaelis-Menten kinetics for fumarase
- 1 August 1976
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 157 (2), 333-337
- https://doi.org/10.1042/bj1570333
Abstract
A study of the steady-state kinetics of fumarase over an extended concentration range, using novel methods of analysis, reveals an initial-rate equation of at least fourth degree for malate as substrate at pH 7.0, with no kinetically significant dead-end complex formation even up to concentrations of 100 mM. In the absence of demonstrable enzyme-aggregation phenomena, this is interpreted as indicating co-operative effects overlooked previously, although a mixture of isoenzymes, each individually of high degree and giving a complex curve, may be a contributing factor.This publication has 6 references indexed in Scilit:
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- Alteration of the Kinetic Properties of an Enzyme by the Binding of Buffer, Inhibitor, or SubstrateProceedings of the National Academy of Sciences, 1953