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Kinetic formulations for the reduction of ketomalonate by lactate dehydrogenase
1Departament de Bioquimica i Fisiologia, Facultat de Química, Universitat de Barcelona, Spain.
Journal of Enzyme Inhibition
|January 1, 1990
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.