Kinetics of the reduction of oxaloacetate catalyzed by mitochondrial malate dehydrogenase of Toxocara canis muscle.
1. The reaction of reduction of oxaloacetate to L-malate in the presence of NADH catalyzed by mitochondrial malate dehydrogenase (EC 1.1.1.37) of Toxocara canis muscle has been studied. 2. The data obtained in initial velocity experiments as well as those involving product inhibition suggest that the reaction mechanism is of the sequential type with a kinetically significant ternary complex and in which the coenzymes bind to the free enzyme. 3. The kinetic parameters, including the inhibition constant for NADH were estimated by non-linear regression analysis using the appropriate rate equations.
Mansini
E
E
Departamento de Bioquimica, Universidade Federal do Rio de Janeiro, Brasil.
Oestreicher
E G
EG
Ribeiro
L P
LP
D000818:Animals; D004285:Dogs; D007700:Kinetics; D008291:Malate Dehydrogenase / Q000378:metabolism*; D008293:Malates / Q000378:metabolism; D008931:Mitochondria, Muscle / Q000201:enzymology*; D009243:NAD / Q000378:metabolism; D010071:Oxaloacetates / Q000378:metabolism*; D010084:Oxidation-Reduction; D014119:Toxocara / Q000201:enzymology*
D008293:Malates; D010071:Oxaloacetates; D009243:NAD; C030298:malic acid; D008291:Malate Dehydrogenase