L-pipecolate oxidase: a distinct peroxisomal enzyme in man

Biochem Biophys Res Commun. 1989 Oct 16;164(1):550-5. doi: 10.1016/0006-291x(89)91754-3.

Abstract

We investigated the oxidation of L-pipecolate in human liver. The results obtained with L-pipecolate from which traces of D-pipecolate had been removed by a preincubation with D-aminoacid oxidase indicate that a distinct L-pipecolate oxidase rather than D-aminoacid oxidase is responsible for the L-pipecolate dependent H2O2-production in human liver. Importantly, L-pipecolate oxidase was found to be localized in peroxisomes which adds to the growing number of enzymes and metabolic functions which can be ascribed to peroxisomes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • D-Amino-Acid Oxidase / metabolism
  • Humans
  • Hydrogen Peroxide / metabolism
  • Liver / enzymology
  • Liver / metabolism
  • Microbodies / enzymology*
  • Oxidation-Reduction
  • Oxidoreductases Acting on CH-NH Group Donors / metabolism*
  • Pipecolic Acids / metabolism*
  • Rats

Substances

  • Pipecolic Acids
  • Hydrogen Peroxide
  • D-Amino-Acid Oxidase
  • Oxidoreductases Acting on CH-NH Group Donors
  • L-pipecolate dehydrogenase
  • pipecolic acid