Cytochemical localization of a D-amino acid oxidizing enzyme in peroxisomes of Drosophila melanogaster.
A peroxide generating oxidase is demonstrated cytochemically in the peroxisomes of adult and larval Drosophila melanogaster, Oregon R and Rosy-506 strains. This enzyme activity is demonstrable using D-pipecolate or D-proline, but not L-proline, as substrate and is inhibited by kojic acid. Thus this enzyme shares cytochemical characteristics with vertebrate D-amino acid oxidase.
St Jules
R
R
Department of Biological Sciences, Columbia University, New York 10027.
Beard
M
M
Holtzman
E
E
D000375:Aging / Q000378:metabolism; D000818:Animals; D002374:Catalase / Q000378:metabolism; D003605:D-Amino-Acid Oxidase / Q000032:analysis*; D004331:Drosophila melanogaster / Q000201:enzymology*; D006651:Histocytochemistry; D007814:Larva / Q000201:enzymology; D008830:Microbodies / Q000201:enzymology*; D008854:Microscopy, Electron
D002374:Catalase; D003605:D-Amino-Acid Oxidase