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. 1974 Jun;139(3):797–800. doi: 10.1042/bj1390797

Histidine residues and the enzyme activity of pig heart supernatant malate dehydrogenase (Short Communication)

J John Holbrook 1, A Lodola 1, Nicholas P Illsley 1
PMCID: PMC1166348  PMID: 4368772

Abstract

1. Supernatant pig heart malate dehydrogenase is completely inhibited by reaction with diethyl pyrocarbonate at pH6.5, when 0.58±0.1 residue of ethoxycarbonylhistidine is formed per NADH-binding site. 2. Oxaloacetate and hydroxymalonate protect the enzyme from inhibition in the absence of coenzyme. 3. Limited ethoxycarbonylation does not alter the binding of NADH to the enzyme but prevents the enzyme–NADH complex from interacting with hydroxymalonate in a ternary complex.

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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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