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J Bacteriol. 1965 February; 89(2): 373-377
Copyright © 1965 American Society for Microbiology. All Rights Reserved.

Nature of Butyrate Oxidation by Mycoplasma hominis

Division of Bacteriology, New York State College of Agriculture, Cornell University, Ithaca, New York
Department of Microbiology, School of Medicine, University of South Dakota, Vermillion, South Dakota

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 ß-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.

¹ This work was done while at the University of South Dakota, Vermillion.

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