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Deviation from Michaelis-Menten kinetics for fumarase.

M J Crabbe·W G Bardsley
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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.

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M J Crabbe, W G Bardsley. 1976-08-01. Deviation from Michaelis-Menten kinetics for fumarase.. https://doi.org/10.1042/bj1570333

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