The inhibition of lactate dehydrogenase by hydrated pyruvate

Authors

Mark Dean Waddington, Central Washington University
John E. Meany, Central Washington University

Document Type

Article

Department or Administrative Unit

Chemistry

Publication Date

10-1-1981

Abstract

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.

Comments

This article was originally published in Archives of Biochemistry and Biophysics. The full-text article from the publisher can be found here.

Due to copyright restrictions, this article is not available for free download from ScholarWorks @ CWU.

Recommended Citation

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

Journal

Archives of Biochemistry and Biophysics

Rights

Copyright © 1981 Published by Elsevier Inc.