Characteristics and subcellular localization of pristanoyl-CoA synthetase in rat liver

Biochim Biophys Acta. 1992 May 8;1125(3):274-9. doi: 10.1016/0005-2760(92)90056-2.

Abstract

We have investigated the activation of pristanic acid to its CoA-ester in rat liver. The results show that peroxisomes, mitochondria as well as microsomes contain pristanoyl-CoA synthetase activity. On the basis of competition experiments and immunoprecipitation studies using antibodies raised against rat liver microsomal long-chain fatty acyl-CoA synthetase (EC 6.2.1.3) we conclude that pristanic acid is activated by the same enzyme which activates long-chain fatty acids, i.e., long-chain fatty acyl-CoA synthetase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Coenzyme A Ligases / isolation & purification*
  • Coenzyme A Ligases / metabolism
  • Dicarboxylic Acids / metabolism
  • Fatty Acids / metabolism*
  • Hydrogen-Ion Concentration
  • Liver / enzymology*
  • Male
  • Octoxynol
  • Palmitic Acid
  • Palmitic Acids / metabolism
  • Polyethylene Glycols / pharmacology
  • Rats
  • Rats, Inbred Strains
  • Repressor Proteins*
  • Saccharomyces cerevisiae Proteins*
  • Subcellular Fractions / enzymology

Substances

  • Dicarboxylic Acids
  • Fatty Acids
  • Palmitic Acids
  • Repressor Proteins
  • Saccharomyces cerevisiae Proteins
  • Palmitic Acid
  • Polyethylene Glycols
  • pristanic acid
  • Octoxynol
  • dodecanedioic acid
  • Coenzyme A Ligases
  • FAA2 protein, S cerevisiae
  • long-chain-fatty-acid-CoA ligase