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L-pipecolate oxidase: a distinct peroxisomal enzyme in man
R J Wanders1, G J Romeyn, R B Schutgens
1Department of Pediatrics, University Hospital Amsterdam, The Netherlands.
Biochemical and Biophysical Research Communications
|October 16, 1989
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.