『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
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種別 (必須): 学術論文 (審査論文) [継承]
言語 (必須): 英語 [継承]
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組織 (推奨):
著者 (必須): 1. (英) Sakuraba Haruhiko (日) (読)
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2. (英) Satomura Takenori (日) (読)
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3.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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4. (英) Kim Kwang (日) (読)
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5. (英) Hara Yusuke (日) (読)
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6. (英) Yoneda Kazunari (日) (読)
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7. (英) Ohshima Toshihisa (日) (読)
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題名 (必須): (英) Crystal structure of novel dye-linked L-proline dehydrogenase from hyperthermophilic archaeon Aeropyrum pernix.  (日)    [継承]
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要約 (任意): (英) Two types of dye-linked L-proline dehydrogenase (PDH1, α4β4-type hetero-octamer, and PDH2, αβγδ-type heterotetramer) have been identified so far in hyperthermophilic archaea. Here, we report the crystal structure of a third type of L-proline dehydrogenase, found in the aerobic hyperthermophilic archaeon Aeropyrum pernix, whose structure (homodimer) is much simpler than those of previously studied L-proline dehydrogenases. The structure was determined at a resolution of 1.92 Å. The asymmetric unit contained one subunit, and a crystallographic 2-fold axis generated the functional dimer. The overall fold of the subunit showed similarity to that of the PDH1 β-subunit, which is responsible for catalyzing L-proline dehydrogenation. However, the situation at the subunit-subunit interface of the A. pernix enzyme was totally different from that in PDH1. The presence of additional surface elements in the A. pernix enzyme contributes to a unique dimer association. Moreover, the C-terminal Leu(428), which is provided by a tail extending from the FAD-binding domain, shielded the active site, and an L-proline molecule was entrapped within the active site cavity. The K(m) value of a Leu(428) deletion mutant for L-proline was about 800 times larger than the K(m) value of the wild-type enzyme, although the k(cat) values did not differ much between the two enzymes. This suggests the C-terminal Leu(428) is not directly involved in catalysis, but it is essential for maintaining a high affinity for the substrate. This is the first description of an LPDH structure with L-proline bound, and it provides new insight into the substrate binding of LPDH.  (日)    [継承]
キーワード (推奨): 1. (英) Aeropyrum (日) (読) [継承]
2. (英) Archaeal Proteins (日) (読) [継承]
3. (英) Crystallography, X-Ray (日) (読) [継承]
4. (英) Proline Oxidase (日) (読) [継承]
5. (英) Protein Multimerization (日) (読) [継承]
6. (英) Protein Structure, Quaternary (日) (読) [継承]
7. (英) Protein Structure, Tertiary (日) (読) [継承]
発行所 (推奨):
誌名 (必須): The Journal of Biological Chemistry ([The American Society for Biochemistry and Molecular Biology])
(pISSN: 0021-9258, eISSN: 1083-351X)

ISSN (任意): 1083-351X
ISSN: 0021-9258 (pISSN: 0021-9258, eISSN: 1083-351X)
Title: The Journal of biological chemistry
Title(ISO): J Biol Chem
Publisher: American Society for Biochemistry and Molecular Biology
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
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(必須): 287 [継承]
(必須): 24 [継承]
(必須): 20070 20080 [継承]
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年月日 (必須): 西暦 2012年 4月 16日 (平成 24年 4月 16日) [継承]
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DOI (任意): 10.1074/jbc.M111.319038    (→Scopusで検索) [継承]
PMID (任意): 22511758    (→Scopusで検索) [継承]
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備考 (任意): 1.(英) Article.ELocationID: 10.1074/jbc.M111.319038  (日)    [継承]
2.(英) Article.Affiliation: Department of Applied Biological Science, Faculty of Agriculture, Kagawa University, 2393 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0795, Japan.  (日)    [継承]
3.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
4.(英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't  (日)    [継承]
5.(英) OtherID: PMC3370190 [Available on 06/08/13]  (日)    [継承]

標準的な表示

和文冊子 ● Haruhiko Sakuraba, Takenori Satomura, Ryushi Kawakami, Kwang Kim, Yusuke Hara, Kazunari Yoneda and Toshihisa Ohshima : Crystal structure of novel dye-linked L-proline dehydrogenase from hyperthermophilic archaeon Aeropyrum pernix., The Journal of Biological Chemistry, Vol.287, No.24, 20070-20080, 2012.
欧文冊子 ● Haruhiko Sakuraba, Takenori Satomura, Ryushi Kawakami, Kwang Kim, Yusuke Hara, Kazunari Yoneda and Toshihisa Ohshima : Crystal structure of novel dye-linked L-proline dehydrogenase from hyperthermophilic archaeon Aeropyrum pernix., The Journal of Biological Chemistry, Vol.287, No.24, 20070-20080, 2012.

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