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Kinetic study of the mechanisms of eliminating substrate inhibition of lactate dehydrogenase by anions and pH

Saburova, E.A.; Iagodina, L.O.

Biokhimiia 55(10): 1819-1825

1990

ISSN/ISBN: 0320-9725
PMID: 2078626
Document Number: 356638
The dependence of lactate dehydrogenase inhibition at high pyruvate concentrations on pH and neutral salt anions was studied. It was shown that Cl- anions compete with the substrate within the ternary inhibitory complex, ENADpyr in equilibrium ENADCl-, as a result of which the pyruvate-induced inhibition is eliminated. The KD values for Cl- (50 mM) and I- (27 mM) were calculated from the substrate velocity curves at high concentrations of pyruvate. It was supposed that pyruvate inhibition elimination by OH- proceeds via the same kinetic mechanism. The pK value (7.1 +/- 0.1) calculated from this model corresponds to pKn of essential His-195. The additivity of OH- and Cl- function was demonstrated.

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