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. 1965 Feb;89(2):373–377. doi: 10.1128/jb.89.2.373-377.1965

Nature of Butyrate Oxidation by Mycoplasma hominis

P J VanDemark 1,2,1, P F Smith 1,2
PMCID: PMC305517  PMID: 14255703

Abstract

VanDemark, P. J. (Cornell University, Ithaca, N.Y.), and P. F. Smith. Nature of butyrate oxidation by Mycoplasma hominis. J. Bacteriol. 89:373–377. 1965.—Cell-free extracts of butyrate - grown Mycoplasma hominis strain O7, though lacking thiokinase activity on butyric acid, were found to activate butyrate via an acetyl-butyric thiophorase. These extracts also contained an aceto-coenzyme A (CoA) kinase, a butyryl-CoA dehydrogenase, a crotonase, a reduced nicotinamide adenine dinucleotide-specific β-hydroxybutyryl-CoA dehydrogenase, and a thiolase. Thiolase activity was stimulated by the addition of magnesium ions. The presence of these enzyme activities in this Mycoplasma species supports the hypothesis that a fatty acid oxidation represents an energy source for the nonfermentative pleuropneumonia-like organisms.

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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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