title: Peroxisomal localization of D-aspartate oxidase and development of peroxisomes in the yeast Cryptococcus humicolus UJ1 grown on D-aspartate.
abstract: The peroxisomal localization of D-aspartate oxidase (EC. 1.4.3.1) was demonstrated in the yeast Cryptococcus humicolus UJ1 cells grown in the medium containing D-aspartate as a nitrogen source. The conclusion is based on the identical behavior of the enzyme with those of peroxisomal marker enzymes, catalase and urate oxidase, during all steps of subcellular fractionations. Supporting evidence was provided by the morphometric analysis of the peroxisomes with electron microscopy, showing that the cells grown on D-aspartate contained more and larger peroxisomes than those grown on L-aspartate, consistent with the 500-fold and 3-fold, higher contents of D-aspartate oxidase and catalase activities, respectively, in the former cells than the latter.
authors.affiliation: Department of Environmental Systems Engineering, Nagaoka University of Technology, Niigata, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Kera
authors.forename: A
authors.initials: A
authors.lastname: Niino
authors.forename: T
authors.initials: T
authors.lastname: Ikeda
authors.forename: H
authors.initials: H
authors.lastname: Okada
authors.forename: R
authors.initials: R
authors.lastname: Yamada
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D001224:Aspartic Acid; D003454:Cryptococcus / Q000201:enzymology* / Q000254:growth & development* / Q000648:ultrastructure; D003470:Culture Media; D050804:D-Aspartate Oxidase; D008830:Microbodies / Q000201:enzymology* / Q000648:ultrastructure; D008854:Microscopy, Electron; D013347:Subcellular Fractions / Q000201:enzymology
chemical_list: D003470:Culture Media; D001224:Aspartic Acid; D000594:Amino Acid Oxidoreductases; D050804:D-Aspartate Oxidase