Butyrate-CoA ligase

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In enzymology, a butyrate-CoA ligase (EC 6.2.1.2) is an enzyme that catalyzes the chemical reaction

ATP + an acid + CoA $\rightleftharpoons$ AMP + diphosphate + an acyl-CoA

The 3 substrates of this enzyme are ATP, acid, and CoA, whereas its 3 products are AMP, diphosphate, and acyl-CoA.

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is butanoate:CoA ligase (AMP-forming). Other names in common use include butyryl-CoA synthetase, fatty acid thiokinase (medium chain), acyl-activating enzyme, fatty acid elongase, fatty acid activating enzyme, fatty acyl coenzyme A synthetase, medium chain acyl-CoA synthetase, butyryl-coenzyme A synthetase, L-(+)-3-hydroxybutyryl CoA ligase, and short-chain acyl-CoA synthetase. This enzyme participates in butanoate metabolism.

[edit] References

IUBMB entry for 6.2.1.2
BRENDA references for 6.2.1.2 (Recommended.)
PubMed references for 6.2.1.2
PubMed Central references for 6.2.1.2
Google Scholar references for 6.2.1.2
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Websterlt JR, Gerowin LD and Rakita L (1965). "Purification and characteristics of a butyryl coenzyme A synthetase from bovine heart mitochondria". J. Biol. Chem. 240: 29–33.