The inhibition of lactate dehydrogenase by hydrated pyruvate
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The lactate dehydrogenase-catalyzed reduction of pyruvate by NADH was studied using a spectroscopic method. The inhibitory effect exhibited by high concentrations of pyruvate was investigated in phosphate and 2,2-diethylmalonate buffers. Kinetic studies were carried out in which the rate of the enzyme-catalyzed reaction was monitored at various stages of pyruvate hydration, H2O + CH3COCO2− ⇋ CH3C(OH)22C02−. Buffered solutions of different initial relative amounts of ketopyruvate and hydrated pyruvate (2,2-dihydroxypropanoic acid) were also preincubated with the enzyme and NAD+. Kinetic runs were initiated in the resultant solutions at various stages of incubation by the introduction of NADH. The results of the present investigation indicate that hydrated pyruvate is a major inhibitor of lactate dehydrogenase and forms an inhibitory complex with the enzyme and oxidized coenzyme.
Waddington, M., & Meany, J. (1981). The inhibition of lactate dehydrogenase by hydrated pyruvate. Archives of Biochemistry and Biophysics, 211(1), 447–453. https://doi.org/10.1016/0003-9861(81)90476-8
Archives of Biochemistry and Biophysics
Copyright © 1981 Published by Elsevier Inc.