The role of coenzyme A in the biotransformation of 2-arylpropionic acids

Chem Biol Interact. 1994 Mar;90(3):235-51. doi: 10.1016/0009-2797(94)90013-2.

Abstract

A number of 2-arylpropionic acid non-steroidal anti-inflammatory drugs ('profens') undergo highly enantioselective inversion from the (R)- to (S)-enantiomer. The mechanism of this inversion reaction involves the initial enantioselective formation of a coenzyme A thioester followed by epimerization and finally hydrolysis to regenerate free acids. Long-chain fatty acyl-CoA synthetase appears to mediate the initial thioester formation and an epimerase of an unknown physiologic function effects the second step. The hydrolases mediating the final step are poorly defined. Available evidence suggests that the liver is quantitatively the most important tissue site of inversion but local tissue inversion may influence the pharmacological and toxicological response of a given organ. Data from isolated rat hepatocytes indicate that other xenobiotics can modulate the formation and hydrolysis of ibuprofenyl-CoA by influencing inversion pathways, non-inversion pathways or both. Interactions between xenobiotics may therefore accentuate inter-individual variability in response to 2-aryl-propionic acids. The formation of 2-arylpropionyl-CoA thioesters in vivo has the potential to disrupt numerous biochemical pathways in addition to enhancing individual exposure to the potent anti-inflammatory (S)-enantiomers.

Publication types

  • Review

MeSH terms

  • Acyl Coenzyme A / metabolism
  • Animals
  • Anti-Inflammatory Agents, Non-Steroidal / metabolism*
  • Anti-Inflammatory Agents, Non-Steroidal / pharmacology
  • Biotransformation
  • Coenzyme A / metabolism*
  • Coenzyme A Ligases / metabolism
  • Humans
  • Hydrolysis
  • Liver / drug effects
  • Liver / metabolism*
  • Organ Specificity
  • Repressor Proteins*
  • Saccharomyces cerevisiae Proteins*
  • Stereoisomerism
  • Xenobiotics / pharmacology*

Substances

  • Acyl Coenzyme A
  • Anti-Inflammatory Agents, Non-Steroidal
  • Repressor Proteins
  • Saccharomyces cerevisiae Proteins
  • Xenobiotics
  • ibuprofenyl-coenzyme A
  • Coenzyme A Ligases
  • FAA2 protein, S cerevisiae
  • long-chain-fatty-acid-CoA ligase
  • Coenzyme A