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2-Arylpropionyl-CoA epimerase: partial peptide sequences and tissue localization

C Reichel1, H Bang, K Brune

  • 1Department of Experimental and Clinical Pharmacology and Toxicology, University of Erlangen-Nürnberg, Germany.

Biochemical Pharmacology
|November 27, 1995
PubMed
Summary

Researchers isolated and purified a rat liver epimerase responsible for metabolic chiral inversion of 2-arylpropionic acids. This enzyme shows homology to fatty acid metabolism enzymes and its tissue distribution was analyzed.

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Enzymology

Background:

  • Metabolic chiral inversion of R-enantiomers of 2-arylpropionic acids (2-APAs) like ibuprofen is species- and substrate-dependent.
  • This process involves activation to acyl-CoA-thioesters and subsequent epimerization by a specific enzyme.

Purpose of the Study:

  • To isolate and characterize the epimerase responsible for chiral inversion of 2-APAs.
  • To investigate the enzyme's sequence homology, tissue distribution, and activity in rats and guinea pigs.

Main Methods:

  • Isolation and purification of a 42 kDa epimerase from rat liver cytosol.
  • Generation of polyclonal antibodies against the purified epimerase.
  • Amino acid sequence analysis of peptide fragments and Western blot analysis for tissue distribution.

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Main Results:

  • A homogeneous 42 kDa epimerase was isolated from rat liver cytosol.
  • Sequence analysis revealed homology to fatty acid metabolism enzymes.
  • Western blot analysis demonstrated tissue-specific distribution of the epimerase in rats and guinea pigs.

Conclusions:

  • The study successfully isolated and characterized a key enzyme in the metabolic chiral inversion of 2-APAs.
  • The findings suggest a link between fatty acid metabolism and chiral inversion pathways.
  • Further research is warranted to explore the physiological significance of this epimerase across different tissues and species.