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PMID: 2572224 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

L-pipecolate oxidase: a distinct peroxisomal enzyme in man.

Biochemical and biophysical research communications ·Vol. 164 ·No. 1 ·1989-10-16 ·Pages 550-5

Wanders RJ, Romeyn GJ, Schutgens RB, Tager JM

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.

MeSH Terms
Animals D-Amino-Acid Oxidase/metabolism Humans Hydrogen Peroxide/metabolism Liver/enzymology,metabolism Microbodies/enzymology Oxidation-Reduction Oxidoreductases Acting on CH-NH Group Donors/metabolism Pipecolic Acids/metabolism Rats
Chemicals
Pipecolic Acids Hydrogen Peroxide D-Amino-Acid Oxidase Oxidoreductases Acting on CH-NH Group Donors L-pipecolate dehydrogenase pipecolic acid
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Wanders R J
Department of Pediatrics, University Hospital Amsterdam, The Netherlands.
Romeyn G J
Schutgens R B
Tager J M
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1989-10-16
Pages
550-5
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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