L-pipecolate oxidase: a distinct peroxisomal enzyme in man.
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.
Wanders
R J
RJ
Department of Pediatrics, University Hospital Amsterdam, The Netherlands.
Romeyn
G J
GJ
Schutgens
R B
RB
Tager
J M
JM
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
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