PMID: 9545602Apr 18, 1998Paper

Peroxisomal localization of D-aspartate oxidase and development of peroxisomes in the yeast Cryptococcus humicolus UJ1 grown on D-aspartate

Biochimica Et Biophysica Acta
Y KeraR Yamada

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.

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Citations

Feb 9, 2000·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·G TedeschiS Ronchi
Dec 5, 2006·The FEBS Journal·Masumi KataneHiroshi Homma
Jun 22, 2010·Chemistry & Biodiversity·Masumi Katane, Hiroshi Homma
Nov 15, 2006·Chemical Record : an Official Publication of the Chemical Society of Japan ... [et Al.]·Ryo-hei YamadaShouji Takahashi
Jul 4, 2018·Biogerontology·Nayan M DeoriShirisha Nagotu
Feb 12, 2020·Applied Microbiology and Biotechnology·Shouji Takahashi

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