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著作: [川上 竜巳]/[櫻庭 春彦]/Tsuge Hideaki/[郷田 秀一郎]/Katunuma Nobuhiko/[大島 敏久]/A second novel dye-linked L-proline dehydrogenase complex is present in the hyperthermophilic archaeon Pyrococcus horikoshii OT-3/[The FEBS Journal]

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EID
123483
EOID
667814
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2012年10月26日(金) 21:52:38
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大家 隆弘
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[学科長]/[徳島大学.工学部.生物工学科]
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種別 必須 学術論文(審査論文)
言語 必須 英語
招待 推奨
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  1. 徳島大学.工学部.生物工学科.生物反応工学講座
  2. 徳島文理大学
著者 必須
  1. 川上 竜巳([徳島大学.大学院社会産業理工学研究部.生物資源産業学域.食料科学系.食料科学分野]/[徳島大学.生物資源産業学部])
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  2. 櫻庭 春彦
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    貢献度 任意
    学籍番号 推奨
  3. (英) Tsuge Hideaki
    役割 任意
    貢献度 任意
    学籍番号 推奨
  4. 郷田 秀一郎([長崎大学])
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    学籍番号 推奨
  5. (英) Katunuma Nobuhiko
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    学籍番号 推奨
  6. 大島 敏久([九州大学])
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題名 必須

(英) A second novel dye-linked L-proline dehydrogenase complex is present in the hyperthermophilic archaeon Pyrococcus horikoshii OT-3

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(英) Two distinguishable activity bands for dye-linked l-proline dehydrogenase (PDH1 and PDH2) were detected when crude extract of the hyperthermophilic archaeon Pyrococcus horikoshii OT-3 was run on a polyacrylamide gel. After purification, PDH1 was found to be composed of two different subunits with molecular masses of 56 and 43 kDa, whereas PDH2 was composed of four different subunits with molecular masses of 52, 46, 20 and 8 kDa. The native molecular masses of PDH1 and PDH2 were 440 and 101 kDa, respectively, indicating that PDH1 has an alpha4beta4 structure, while PDH2 has an alphabetagammadelta structure. PDH2 was found to be similar to the dye-linked l-proline dehydrogenase complex from Thermococcus profundus, but PDH1 is a different type of enzyme. After production of the enzyme in Escherichia coli, high-performance liquid chromatography showed the PDH1 complex to contain the flavins FMN and FAD as well as ATP. Gene expression and biochemical analyses of each subunit revealed that the beta subunit bound FAD and exhibited proline dehydrogenase activity, while the alpha subunit bound ATP, but unlike the corresponding subunit in the T. profundus enzyme, it exhibited neither proline dehydrogenase nor NADH dehydrogenase activity. FMN was not bound to either subunit, suggesting it is situated at the interface between the alpha and beta subunits. A comparison of the amino-acid sequences showed that the ADP-binding motif in the alpha subunit of PDH1 clearly differs from that in the alpha subunit of PDH2. It thus appears that a second novel dye-linked l-proline dehydrogenase complex is produced in P. horikoshii.

キーワード 推奨
  1. (英) Amino Acid Sequence
  2. (英) Chromatography, High Pressure Liquid
  3. (英) Coloring Agents
  4. (英) Genes, Archaeal
  5. (英) Molecular Sequence Data
  6. (英) Proline Oxidase
  7. (英) Pyrococcus horikoshii
  8. (英) Recombinant Proteins
  9. (英) Sequence Homology, Amino Acid
発行所 推奨 (英) The Federation of European Biochemical Society
誌名 必須 The FEBS Journal([Federation of European Biochemical Societies])
(pISSN: 1742-464X, eISSN: 1742-4658)
ISSN 任意 1742-464X
ISSN: 1742-464X (pISSN: 1742-464X, eISSN: 1742-4658)
Title: The FEBS journal
Title(ISO): FEBS J
Supplier: Federation of European Biochemical Societies
Publisher: Wiley Publishing
 (NLM Catalog  (Wiley  (Scopus  (CrossRef (Scopus information is found. [need login])
必須 272
必須 16
必須 4044 4054
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年月日 必須 2005年 8月 初日
URL 任意
DOI 任意 10.1111/j.1742-4658.2005.04810.x    (→Scopusで検索)
PMID 任意 16098188    (→Scopusで検索)
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備考 任意
  1. (英) Article.Affiliation: Department of Biological Science and Technology, Faculty of Engineering, The University of Tokushima, Japan.

  2. (英) Article.PublicationTypeList.PublicationType: Journal Article

  3. (英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't