The kinetic mechanism of pyruvate reduction by lactate dehydrogenase from Phycomyces blakesleeanus.
The kinetics of pyruvate reduction by lactate dehydrogenase from Phycomyces blakesleeanus NRRL 1555 (-) have been determined at pH 6.0. Initial rate studies performed in the pyruvate reduction direction suggest that a sequential mechanism is operating. Product inhibition studies with NAD+ and L(+)-lactate are consistent with an ordered sequential mechanism if we considered that NAD+ mimics the NADH that binds cooperatively on the enzyme and also the existence of dead-end complex responsible for substrate inhibition by pyruvate at this pH value.
D005658:Fungi / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D007773:Lactates / Q000494:pharmacology; D019344:Lactic Acid; D009243:NAD / Q000378:metabolism / Q000494:pharmacology; D010084:Oxidation-Reduction; D010800:Phycomyces / Q000201:enzymology*; D011773:Pyruvates / Q000378:metabolism*; D019289:Pyruvic Acid
D007773:Lactates; D011773:Pyruvates; D009243:NAD; D019344:Lactic Acid; D019289:Pyruvic Acid; D007770:L-Lactate Dehydrogenase