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. 1979 Mar 1;177(3):951–957. doi: 10.1042/bj1770951

The mechanism of adduct formation between NAD+ and pyruvate bound to pig heart lactate dehydrogenase.

D C Wilton
PMCID: PMC1186462  PMID: 220957

Abstract

1. The rate of adduct formation between NAD+ and enol-pyruvate at the active site of lactate dehydrogenase is determined by the rate of enolization of pyruvate in solution. 2. The proportion of enol-pyruvate solutions is less than 0.01%. 3. The overall dissociation constant of adduct formation is less than 5 X 10(-8) M for pig heart lactate dehydrogenase at pH 7.0. 4. The unusual kinetics for adduct formation previously observed in the case of rabbit muscle lactate dehydrogenase [Griffin & Criddle (1970) Biochemistry 9, 1195--1205] may be attributed to the concentration of enol-pyruvate in solution being considerably less than the concentration of enzyme.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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