1995年2月
NOVEL NADP-LINKED ISOCITRATE DEHYDROGENASE PRESENT IN PEROXISOMES OF N-ALKANE-UTILIZING YEAST, CANDIDA-TROPICALIS - COMPARISON WITH MITOCHONDRIAL NAD-LINKED ISOCITRATE DEHYDROGENASE
ARCHIVES OF MICROBIOLOGY
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- ,
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- 巻
- 163
- 号
- 2
- 開始ページ
- 104
- 終了ページ
- 111
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1007/BF00381783
- 出版者・発行元
- SPRINGER VERLAG
Peroxisomal NADP-linked isocitrate dehydrogenase (Ps-NADP-IDH) was purified for the first time from Candida tropicalis cells grown on n-alkcane as a carbon source, which was effective in proliferation of peroxisomes. The properties of Ps-NADP-IDH were compared with those of mitochondrial NAD-linked isocitrate dehydrogenase (Mt-NAD-IDH) purified from the cells grown on acetate, in which peroxisomes did not proliferate. PsNADP-IDH was a homodimer of identical subunits (45 kDa), while Mt-NAD-LDH was suggested to be a heterooctamer composed of two types of subunits with different molecular masses (41 and 38 kDa). Kinetic studies revealed that Ps-NADP-IDH gave Michaelis-Menten saturation curves against isocitrate and NADP concentrations, whereas Mt-NAD-IDH was an allosteric enzyme regulated by ATP, AMP, and citrate. Inhibition by 2-oxoglutarate, a precursor of glutamate, was observed only for Ps-NADP-IDH. Both enzymes were inhibited by concomitant addition of oxalacetate and glyoxylate. The function of Ps-NADP-IDH seems to be completely discriminated from that of Mt-NAD-IDH as reflected by their distinct subcellular localizations. Furthermore, the properties of Ps-NADP-IDH were also compared with those of other mitochondrial and cytosolic IDHs from sources reported previously.
- リンク情報
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- DOI
- https://doi.org/10.1007/BF00381783
- J-GLOBAL
- https://jglobal.jst.go.jp/detail?JGLOBAL_ID=200902115107600713
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/7710326
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:A1995QK49900004&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1007/BF00381783
- ISSN : 0302-8933
- J-Global ID : 200902115107600713
- PubMed ID : 7710326
- Web of Science ID : WOS:A1995QK49900004