title: L-pipecolate oxidase: a distinct peroxisomal enzyme in man.
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.
authors.affiliation: Department of Pediatrics, University Hospital Amsterdam, The Netherlands.
authors.forename: R J
authors.initials: RJ
authors.lastname: Wanders
authors.forename: G J
authors.initials: GJ
authors.lastname: Romeyn
authors.forename: R B
authors.initials: RB
authors.lastname: Schutgens
authors.forename: J M
authors.initials: JM
authors.lastname: Tager
mesh_terms: D000818:Animals; D003605:D-Amino-Acid Oxidase / Q000378:metabolism; D006801:Humans; D006861:Hydrogen Peroxide / Q000378:metabolism; D008099:Liver / Q000201:enzymology / Q000378:metabolism; D008830:Microbodies / Q000201:enzymology*; D010084:Oxidation-Reduction; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism*; D010875:Pipecolic Acids / Q000378:metabolism*; D051381:Rats
chemical_list: D010875:Pipecolic Acids; D006861:Hydrogen Peroxide; D003605:D-Amino-Acid Oxidase; D000587:Oxidoreductases Acting on CH-NH Group Donors; C032771:L-pipecolate dehydrogenase; C031345:pipecolic acid