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METABOLISM OF -AMINO ACIDS V.

Energetics of the -Aminobutyrate Fermentation by Clostridium aminobutyricum¹

^a Enzyme Section, Laboratory of Biochemistry, National Heart Institute, National Institutes of Health, Bethesda, Maryland

ABSTRACT

HARDMAN, JOHN K. (National Heart Institute, National Institutes of Health, Bethesda, Md.) AND THRESSA C. STADTMAN. Metabolism of -amino acids. V. Energetics of the -aminobutyrate fermentation by Clostridium aminobutyricum. J. Bacteriol. 85:1326–1333. 1963.—Clostridium aminobutyricum utilizes -aminobutyrate as its sole carbon, nitrogen, and energy source, producing ammonia, acetate, and butyrate as a result of this fermentation. Coenzyme A (CoA)-transferase, phosphotransacetylase, and acetokinase activities have been demonstrated in crude extracts of the organism; the coupling of the reactions catalyzed by these enzymes to the fermentation reactions provides a mechanism whereby C. aminobutyricum can obtain energy, in the form of adenosine triphosphate, from the decomposition of -aminobutyrate. Indirect evidence of additional phosphorylation, at the electron-transport level, has been obtained from molar growth yield studies and from the inhibition by 2,4-dinitrophenol of butyrate synthesis from -aminobutyrate and from crotonyl-CoA.

² Present address: Department of Biological Sciences, Stanford University, Stanford, Calif.

¹ A preliminary report of a portion of this work has been made (Hardman, 1961). This work is taken in part from a Ph.D. thesis submitted to the University of Maryland, College Park, by John K. Hardman.

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