Relations Between Coenzyme A and Presumptive Acyl Carrier Protein in Different Conditions of Streptococcal Growth

Author:

Das D. N.1,Toennies G.1

Affiliation:

1. Department of Microbiology, Temple University School of Medicine, Philadelphia, Pennsylvania 19140

Abstract

Exploration of the specific role of cystine in the postexponential growth of Streptococcus faecalis led to an inquiry into the fate of cellular coenzyme A (CoA) and acyl carrier protein (ACP), both of which depend for their biosynthesis on cystine and pantothenate as precursors. In S. faecalis cells labeled by growth in the presence of 14 C-pantothenate, the label could be separated on the basis of solubility at p H 2.1 into two fractions of sharply differing metabolic characteristics. The fractions were not purified, but the soluble 14 C behaved analytically like CoA, and the insoluble 14 C was considered to represent an ACP-like entity on the basis of circumstantial evidence. The fate of these two fractions under various conditions of growth was studied. When the medium contained an excess of the needed precursors, the cellular content of CoA and ACP appeared to remain constant during exponential growth, and in a molar ratio of about 4 CoA to 1 ACP. Cellular ACP, once formed, appeared to be stable under these conditions, but CoA was degraded and replaced at the rate of approximately 20% per division period. With restrictive levels of pantothenate in the medium, initially formed CoA disappeared during growth, as a result, apparently of being converted to ACP. However, when the resulting CoA-depleted cells were returned to a medium containing enough pantothenate, resumption of normal growth was preceded by a lag period, during which rapid conversion of ACP to CoA appeared to take place.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference15 articles.

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4. The condensation reaction of fatty acid biosynthesis. II. Requirements of the enzymes of the condensation reaction for fatty acid synthesis;Goldman P.;J. Biol. Chem.,1963

5. Isolation of an enzymecoenzyme A intermediate from succinyl coenzyme A-acetoacetate coenzyme A transferase;Hersh L. B.;J. Biol. Chem.,1967

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