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. 1974 Apr;71(4):1334–1338. doi: 10.1073/pnas.71.4.1334

Structural and Functional Similarities Between Mitochondrial Malate Dehydrogenase and L-3-Hydroxyacyl CoA Dehydrogenase

Barbara E Noyes 1,*, Beat E Glatthaar 1, John S Garavelli 1, Ralpha A Bradshaw 1,†
PMCID: PMC388222  PMID: 4133851

Abstract

Pig heart mitochondrial malate dehydrogenase (EC 1.1.1.37), which has been obtained free of electrophoretic subforms, has been shown to have a molecular weight of 67,000 and to be composed of two polypeptide chains. Comparison of these and other properties, such as amino-acid composition, isoelectric point, and keto-substrate inhibition, with those of L-3-hydroxyaeyl CoA dehydrogenase (EC 1.1.1.35), another NAD+-dependent dehydrogenase of mitochondrial origin, suggests structural similarities of the type associated with proteins possessing common evolutionary origins. This conclusion is supported by immunological crossreactivity. In view of these observations, the dissimilarity in the stereospecificity of hydrogen transfer from cofactor to substrate catalyzed by the two enzymes is attributed to 180° rotation in the binding orientation of the nicotinamide moiety of the NAD+, rather than to gross differences in the geometry of the active site of the two enzymes.

Keywords: subunit structure, immunological cross-reactivity, amino-acid composition, specificity of hydrogen transfer, evolution

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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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