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  • Title: Cytoplasmic malate dehydrogenase from Phycomyces blakesleeanus: kinetics and mechanism.
    Author: Teixido F, De Arriaga D, Busto F, Soler J.
    Journal: Can J Biochem Cell Biol; 1985 Oct; 63(10):1097-105. PubMed ID: 4075224.
    Abstract:
    The kinetics and reaction mechanism of cytoplasmic malate dehydrogenase (L-malate:NAD+ oxidoreductase, EC 1.1.1.37) from mycelium of Phycomyces blakesleeanus NRRL 1555 (-) in 0.1 M potassium phosphate buffer (pH 7.5) at 30 degrees C have been investigated. The initial rate and product inhibition studies were consistent with an ordered bi-bi mechanism that involved more than one kinetically significant ternary complex and also with the coenzyme binding first. The dissociation of the coenzyme from the enzyme-coenzyme complex appeared to be the slowest step in either direction of the reaction. The kinetic and rate constants for the individual steps of the reaction were determined.
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