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著作: Sakuraba Haruhiko/Satomura Takenori/[川上 竜巳]/Kim Kwang/Hara Yusuke/Yoneda Kazunari/Ohshima Toshihisa/Crystal structure of novel dye-linked L-proline dehydrogenase from hyperthermophilic archaeon Aeropyrum pernix./[The Journal of Biological Chemistry]

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EID
262420
EOID
688011
Map
0
LastModified
2013年5月22日(水) 21:31:05
Operator
大家 隆弘
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Owner
川上 竜巳
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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
審査 推奨
カテゴリ 推奨
共著種別 推奨
学究種別 推奨
組織 推奨
著者 必須
  1. (英) Sakuraba Haruhiko
    役割 任意
    貢献度 任意
    学籍番号 推奨
  2. (英) Satomura Takenori
    役割 任意
    貢献度 任意
    学籍番号 推奨
  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])
    役割 任意
    貢献度 任意
    学籍番号 推奨
  4. (英) Kim Kwang
    役割 任意
    貢献度 任意
    学籍番号 推奨
  5. (英) Hara Yusuke
    役割 任意
    貢献度 任意
    学籍番号 推奨
  6. (英) Yoneda Kazunari
    役割 任意
    貢献度 任意
    学籍番号 推奨
  7. (英) Ohshima Toshihisa
    役割 任意
    貢献度 任意
    学籍番号 推奨
題名 必須

(英) Crystal structure of novel dye-linked L-proline dehydrogenase from hyperthermophilic archaeon Aeropyrum pernix.

副題 任意
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.

キーワード 推奨
  1. (英) Aeropyrum
  2. (英) Archaeal Proteins
  3. (英) Crystallography, X-Ray
  4. (英) Proline Oxidase
  5. (英) Protein Multimerization
  6. (英) Protein Structure, Quaternary
  7. (英) Protein Structure, Tertiary
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])
必須 287
必須 24
必須 20070 20080
都市 任意
年月日 必須 2012年 4月 16日
URL 任意
DOI 任意 10.1074/jbc.M111.319038    (→Scopusで検索)
PMID 任意 22511758    (→Scopusで検索)
NAID 任意
WOS 任意
Scopus 任意
評価値 任意
被引用数 任意
指導教員 推奨
備考 任意
  1. (英) Article.ELocationID: 10.1074/jbc.M111.319038

  2. (英) Article.Affiliation: Department of Applied Biological Science, Faculty of Agriculture, Kagawa University, 2393 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0795, Japan.

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

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

  5. (英) OtherID: PMC3370190 [Available on 06/08/13]