Long-chain acyl-CoA Hydrolase in the Brain

Amino Acids. 2005 May;28(3):273-8. doi: 10.1007/s00726-005-0181-1. Epub 2005 Mar 2.

Abstract

Long-chain acyl-CoA hydrolases are a group of enzymes that cleave acyl-CoAs into fatty acids and coenzyme A (CoA-SH). Because acyl-CoAs participate in numerous reactions encompassing lipid synthesis, energy metabolism and regulation, modulating intracellular levels of acyl-CoAs would affect cellular functions. Therefore, acyl-CoA synthetases have been intensively studied. In contrast, acyl-CoA hydrolases have been less investigated, especially in the brain despite the fact that its long-chain acyl-CoA hydrolyzing activity is much higher than that in any other organ in the body. However, recent studies have dissected the multiplicity of this class of enzymes on a genomic basis, and have allowed us to discuss their function. Here, we describe a cytosolic long-chain acyl-CoA hydrolase (referred to as BACH) that is constitutively expressed in the brain, comparing it with other acyl-CoA hydrolases found in peripheral organs that have a role in fatty acid oxidation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acyl Coenzyme A / metabolism*
  • Animals
  • Brain / enzymology*
  • Coenzyme A Ligases / metabolism
  • Energy Metabolism / physiology*
  • Humans
  • Isoenzymes / metabolism
  • Lipid A / biosynthesis*
  • Organ Specificity / physiology

Substances

  • Acyl Coenzyme A
  • Isoenzymes
  • Lipid A
  • Coenzyme A Ligases