Affiliation:
1. Department of Microbiology, University of Massachusetts, Amherst, Massachusetts 01002
Abstract
Various bacteria which degrade pyruvate by the phosphoroclastic reaction were examined with respect to the role of coenzyme A (CoA) in this reaction. The strictly anaerobic bacteria, which cleave pyruvate by the phosphoroclastic reaction characteristic of
Clostridia
, required catalytic levels of CoA for the CO
2
-pyruvate exchange and acetoin-forming portions of the phosphoroclastic reaction. These reactions were reversibly inhibited by the CoA analogue, desulfo-CoA. In contrast, using cell-free extracts of bacteria which degrade pyruvate by the coliform phosphoroclastic reaction (pyruvate formate-lyase), no requirement for CoA could be observed for the formate-pyruvate exchange reaction. It is suggested that CoA serves a regulatory function in the early portion of the clostridal type of phosphoroclastic reaction.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
13 articles.
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