WEKO3
アイテム
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IDENTIFICATION AND CHARACTERIZATION OF A 9-CIS-HEXADECENOIC ACID CIS-TRANS ISOMERASE FROM A PSYCHROTROPHIC BACTERIUM, PSEUDOMONAS SP. STRAIN E-3 (18th Symposium on Polar Biology)
https://doi.org/10.15094/00005346
https://doi.org/10.15094/00005346d918d42c-08e2-425f-8cee-55274db560b6
名前 / ファイル | ライセンス | アクション |
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Item type | 紀要論文(ELS) / Departmental Bulletin Paper(1) | |||||
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公開日 | 1997-02-01 | |||||
タイトル | ||||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | departmental bulletin paper | |||||
ID登録 | ||||||
ID登録 | 10.15094/00005346 | |||||
ID登録タイプ | JaLC | |||||
ページ属性 | ||||||
内容記述タイプ | Other | |||||
内容記述 | P(論文) | |||||
記事種別(英) | ||||||
en | ||||||
Proceeding | ||||||
論文名よみ | ||||||
その他のタイトル | IDENTIFICATION AND CHARACTERIZATION OF A 9-CIS-HEXADECENOIC ACID CIS-TRANS ISOMERASE FROM A PSYCHROTROPHIC BACTERIUM, PSEUDOMONAS SP. STRAIN E-3 (18th Symposium on Polar Biology) | |||||
著者名よみ |
オクヤマ, ヒデトシ
× オクヤマ, ヒデトシ× エナリ, ダイスケ× モリタ, ナオキ |
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著者名(英) |
OKUYAMA, Hidetoshi
× OKUYAMA, Hidetoshi× ENARI, Daisuke× MORITA, Naoki |
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著者所属(英) | ||||||
en | ||||||
Laboratory of Environmental Molecular Biology, Graduate School of Environmental Earth Science, Hokkaido University | ||||||
著者所属(英) | ||||||
en | ||||||
Laboratory of Environmental Molecular Biology, Graduate School of Environmental Earth Science, Hokkaido University | ||||||
著者所属(英) | ||||||
en | ||||||
Division of Biological Science, Graduate School of Science, Hokkaido University:(Present address)Laboratory of Biochemistry, Hokkaido National Industrial Research Institute, AIST | ||||||
抄録(英) | ||||||
内容記述タイプ | Other | |||||
内容記述 | A cell-free extract of Pseudomonas sp. strain E-3 (Pseudomonas E-3) had activities that catalyzed the conversion of 9-cis-hexadecenoic acid [16:1(9c)] to 9-trans-hexadecenoic acid [16:1(9t)] in the free acid form, and when 16:1(9c) was esterified to phosphatidylethanolamine (PE). A soluble 16:1(9c) cis-trans isomerase (9-Iase) was purified to complete homogeneity from the extract of Pseudomonas E-3 and characterized. Electrophoresis on both denaturing and incompletely-denaturing polyacrylamide gels of the purified enzyme preparation showed the single band of a protein with a molecular mass of 80 kDa, suggesting that the 9-Iase is a monomeric protein of 80 kDa. The 9-Iase, assayed with 16:1(9c) as a substrate, had a specific activity of 22.8 μmol per h per mg of protein and a Km of 118 μM. The enzyme had the optimum temperature for catalysis at 30℃ and catalyzed the cis to trails conversion of a double bond of 16:1(9c) in the free acid form, but it was able to isomerize 16:1(9c) esterified to PE in the presence of the cell membrane fraction. Irrespective of the temperature at which cells of Pseudomonas E-3 were grown, the level of 16:1(9t) was around 2-4% of the total cellular fatty acids. However, when cells grown at 4℃ were warmed up to 30℃ at a rate of about 20℃/min, the level of 16:1(9t) was increased from 3% to 14%. Since the level in situ of free fatty acids in this bacterium is negligible, it is suggested that the 9-Iase is operative in vivo as the cis to trans isomerase of 16:1(9c) that is esterified to PE together with the membranous factor, and that the 9-Iase might work as a stringent modulator of membrane fluidity under abrupt alteration in growth temperature. | |||||
雑誌書誌ID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA10819561 | |||||
書誌情報 |
Proceedings of the NIPR Symposium on Polar Biology 巻 10, p. 153-162, 発行日 1997-02 |
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出版者 | ||||||
出版者 | National Institute of Polar Research |