Fatty Acyl-CoA Synthetases

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Fatty acyl-CoA synthetase (ACS) catalyzes the adenosine triphosphate dependent formation of a thioester bond between a fatty acid and coenzyme A. This fundamental reaction allows the fatty acid to be degraded for energy production, incorporated into complex lipids, or participate in other metabolic pathways. Different ACS proteins exhibit preferences for fatty acid substrates of varying chain lengths, ranging from 2 to more than 30 carbon atoms. ACSs also differ in their tissue and cellular expression patterns, and subcellular locations. Humans and mice have 26 different ACSs. Emerging evidence suggests that each may perform a unique function essential for the maintenance of normal lipid homeostasis.

Original languageEnglish (US)
Title of host publicationEncyclopedia of Biological Chemistry
Subtitle of host publicationSecond Edition
PublisherElsevier Inc.
Pages290-295
Number of pages6
ISBN (Electronic)9780123786319
ISBN (Print)9780123786302
DOIs
StatePublished - Feb 15 2013

Keywords

  • Activated fatty acid
  • Acyl-CoA
  • Acyl-CoA synthetase
  • Bubblegum acyl-CoA synthetase
  • Coenzyme A
  • Fatty acid
  • Fatty acid activation
  • Fatty acid transport protein
  • Fatty acyl-CoA synthetase
  • Long-chain acyl-CoA synthetase
  • Medium-chain acyl-CoA synthetase
  • Motif
  • Short-chain acyl-CoA synthetase
  • Thioester bond
  • Very long chain acyl-CoA synthetase

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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