title: Kinetic formulations for the reduction of ketomalonate by lactate dehydrogenase.
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.
authors.affiliation: Departament de Bioquimica i Fisiologia, Facultat de Química, Universitat de Barcelona, Spain.
authors.forename: I
authors.initials: I
authors.lastname: Haro
authors.forename: J
authors.initials: J
authors.lastname: Li Gelpí
authors.forename: A
authors.initials: A
authors.lastname: Mazo
authors.forename: A
authors.initials: A
authors.lastname: Cortés
mesh_terms: 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*
chemical_list: D008314:Malonates; D013646:Tartronates; D009243:NAD; C032973:tartronic acid; C008375:mesoxalic acid; D007770:L-Lactate Dehydrogenase