The inhibition of lactate dehydrogenase by hydrated pyruvate |
| |
Authors: | M.D. Waddington J.E. Meany |
| |
Affiliation: | Department of Chemistry, Central Washington University, Ellensburg, Washington 98926 USA |
| |
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. |
| |
Keywords: | Author to whom correspondence should be addressed. |
本文献已被 ScienceDirect 等数据库收录! |