Archives of Microbiology

, Volume 114, Issue 1, pp 55–60 | Cite as

Regulation of citrate synthase from blue-green bacteria by succinyl coenzyme A

  • Catherine Lucas
  • P. D. J. Weitzman


Citrate synthase (EC was prepared from nine species of blue-green bacteria. In every case the citrate synthase was of the “large” type otherwise found only in Gram-negative bacteria.

In addition to inhibition by α-oxoglutarate, the enzymes were all sensitive to inhibition by succinyl coenzyme A, acting competitively with respect to acetyl coenzyme A. Desensitization by potassium chloride and a sigmoidal dependence of inhibition on succinyl coenzyme A concentration suggested the possibility of an allosteric mechanism. Multiple-inhibition analysis using pairs of the competitive inhibitors succinyl coenzyme A, bromoacetyl coenzyme A and ATP confirmed the existence of a distinct site for succinyl coenzyme A.

It is suggested that the specific sensitivity of bluegreen bacterial citrate synthases to succinyl coenzyme A, as well as to α-oxoglutarate, is related to the particular metabolic role of the enzyme in these organisms. The absence of a complete energy-yielding citric acid cycle, resulting from the lack of α-oxoglutarate dehydrogenase, confers a strictly biosynthetic role on citrate synthase, which initiates a branched pathway leading to the two end-products α-oxoglutarate and succinyl coenzyme A. Inhibition of the enzyme by these compounds constitutes a plausible regulatory mechanism.

Key words

Citrate synthase Blue-green bacteria Succinyl coenzyme A Citric acid cycle Multiple-inhibition analysis End-product inhibition 


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Copyright information

© Springer-Verlag 1977

Authors and Affiliations

  • Catherine Lucas
    • 1
  • P. D. J. Weitzman
    • 1
  1. 1.Department of Biochemistry, School of Biological SciencesUniversity of LeicesterLeicesterEngland

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