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Title: L-pipecolate oxidase: a distinct peroxisomal enzyme in man. Author: Wanders RJ, Romeyn GJ, Schutgens RB, Tager JM. Journal: Biochem Biophys Res Commun; 1989 Oct 16; 164(1):550-5. PubMed ID: 2572224. 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.[Abstract] [Full Text] [Related] [New Search]