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January 1, 1990Journal of enzyme inhibition

Kinetic Formulations for the Reduction of Ketomalonate by Lactate Dehydrogenase

Isabel Haro Josep Lluis Gelpí A. Mazo Antonio Cortés

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Abstract

Initial rate kinetic studies of lactate dehydrogenase with ketomalonate and NADH as substrates suggest that this enzymatic system is adapted to a rapid equilibrium ordered bi-bi ternary complex mechanism. The application of the reaction product inhibition method reveals the existence of the enzyme-NADH-hydroxymalonate and enzyme-NAD(+)-ketomalonate abortive complexes. This kinetic behaviour is confirmed by the differential inhibition induced by several alternate products on the pyruvate-lactate dehydrogenase-NADH and ketomalonate-lactate dehydrogenase-NADH systems.

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Haro et al. (1990) studied this question.

synapsesocial.com/papers/6a7f34f8228e4fb72e39d8d1 https://doi.org/10.3109/14756369009035836

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