Item type |
紀要論文(ELS) / Departmental Bulletin Paper(1) |
公開日 |
1997-02-01 |
タイトル |
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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) |
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言語 |
eng |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
departmental bulletin paper |
ID登録 |
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ID登録 |
10.15094/00005346 |
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ID登録タイプ |
JaLC |
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内容記述タイプ |
Other |
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内容記述 |
P(論文) |
記事種別(英) |
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en |
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Proceeding |
論文名よみ |
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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
エナリ, ダイスケ
モリタ, ナオキ
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著者名(英) |
OKUYAMA, Hidetoshi
ENARI, Daisuke
MORITA, Naoki
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著者所属(英) |
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en |
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Laboratory of Environmental Molecular Biology, Graduate School of Environmental Earth Science, Hokkaido University |
著者所属(英) |
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en |
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Laboratory of Environmental Molecular Biology, Graduate School of Environmental Earth Science, Hokkaido University |
著者所属(英) |
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en |
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Division of Biological Science, Graduate School of Science, Hokkaido University:(Present address)Laboratory of Biochemistry, Hokkaido National Industrial Research Institute, AIST |
抄録(英) |
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内容記述タイプ |
Other |
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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 |
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収録物識別子タイプ |
NCID |
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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 |
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出版者 |
National Institute of Polar Research |