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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1974 May;71(5):1987–1991. doi: 10.1073/pnas.71.5.1987

Mechanism of Enzymic Acetylation of des-Acetyl Citrate Lyase

H Schmellenkamp 1, H Eggerer 1
PMCID: PMC388369  PMID: 4365579

Abstract

A new enzyme, acetate:SH-[acyl-carrier-protein] enzyme ligase (AMP), has been purified about 30-fold from cell-free extracts of Klebsiella aerogenes. The enzyme, in the presence of acetate and ATP, catalyzes the acetylation of enzymically inactive des-acetyl citrate lyase to enzymically active citrate lyase (EC 4.1.3.6). Acetate and ATP could be replaced by acetyl adenylate. Acetyl-CoA can act as acetyl donor in this activation only if trace amounts of adenine nucleotides and auxiliary enzymes are present. These allow formation of acetyl adenylate in acetate- and ATP-generating reactions.

Keywords: enzymic activation, acetyl adenylate, acetate:enzyme ligase

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1987

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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