Kinetic formulations for the reduction of ketomalonate by lactate dehydrogenase.
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.
Haro
I
I
Departament de Bioquimica i Fisiologia, Facultat de Química, Universitat de Barcelona, Spain.
Li Gelpí
J
J
Mazo
A
A
Cortés
A
A
D000818:Animals; D006168:Guinea Pigs; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D008314:Malonates / Q000378:metabolism* / Q000494:pharmacology; D009132:Muscles / Q000201:enzymology; D009243:NAD / Q000378:metabolism; D010084:Oxidation-Reduction; D013646:Tartronates / Q000494:pharmacology*
D008314:Malonates; D013646:Tartronates; D009243:NAD; C032973:tartronic acid; C008375:mesoxalic acid; D007770:L-Lactate Dehydrogenase