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  1. 極地研刊行誌
  2. 英文誌
  3. 極域生物
  4. Proceedings of the NIPR Symposium on Polar Biology (ISSN 0914-563X)
  5. No.10 (Feb. 1997)

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/10.15094/00005346
d918d42c-08e2-425f-8cee-55274db560b6
名前 / ファイル ライセンス アクション
KJ00000767689.pdf KJ00000767689 (877.4 kB)
license.icon
Item type 紀要論文(ELS) / Departmental Bulletin Paper(1)
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

WEKO 9414

オクヤマ, ヒデトシ

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エナリ, ダイスケ

× エナリ, ダイスケ

WEKO 9415

エナリ, ダイスケ

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モリタ, ナオキ

× モリタ, ナオキ

WEKO 9416

モリタ, ナオキ

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著者名(英) OKUYAMA, Hidetoshi

× OKUYAMA, Hidetoshi

WEKO 9417

en OKUYAMA, Hidetoshi

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ENARI, Daisuke

× ENARI, Daisuke

WEKO 9418

en ENARI, Daisuke

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MORITA, Naoki

× MORITA, Naoki

WEKO 9419

en 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
出版者
出版者 National Institute of Polar Research
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