Teixido F, De Arriaga D, Busto F, Soler J
Can J Biochem Cell Biol. 1985 Oct;63(10):1097-105. doi: 10.1139/o85-137.
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.
