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Closed complex of the D-3-hydroxybutyrate dehydrogenase induced by an enantiomeric competitive inhibitor.
http://hdl.handle.net/10069/22323
http://hdl.handle.net/10069/2232390a31125-5a5d-4c3e-883f-8b0f4e5a7311
名前 / ファイル | ライセンス | アクション |
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JB145_467.pdf (899.2 kB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2009-11-06 | |||||
タイトル | ||||||
タイトル | Closed complex of the D-3-hydroxybutyrate dehydrogenase induced by an enantiomeric competitive inhibitor. | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | hydroxybutyrate dehydrogenase | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | short-chain dehydrogenase/reductase family | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | crystal structure | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | conformational change | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | substrate recognition | |||||
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 | journal article | |||||
著者 |
Nakashima, Kanako
× Nakashima, Kanako× Ito, Kiyoshi× Nakajima, Yoshitaka× Yamazawa, Ryuji× Miyakawa, Syunsuke× Yoshimoto, Tadashi |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | D-3-Hydroxybutyrate dehydrogenase (HBDH) from Pseudomonas fragi showed a strict stereospecificity to the d-enantiomer of 3-hydroxybutyrate (d-3-HB) as a substrate. The l-enantiomer acts as a competitive inhibitor, with a K(i) value comparable to the K(m) value for d-3-HB. We have determined the crystal structures of the ternary complex of HBDH-NAD(+)-l-3-HB and the binary complex of HBDH-NAD(+). The former structure showed a so-called closed-form conformation, which is considered an active form for catalysis, while the latter stayed mostly in a open-form conformation. The determined structures along with the site-directed mutagenesis confirmed the substrate recognition mechanism that we proposed previously. The hydrogen bonding interaction between Gln196, located in the moving helix, and the carboxyl group of the substrate/inhibitor is important for the stable ternary complex formation. Finally, the crystal structures of the Thr190 mutants, T190S and T190A, indicate that the Thr190 is a key residue for the open-closed conformational change. T190S retained 37% of the activity. In T190A, however, the activity decreased to 0.1% that of the wild-type enzyme. Fixing the position of the hydroxyl group of Thr190 to form hydrogen bonds to the pyrophosphate moiety and the carboxamide of NAD(+) seems to be a significant factor for the open-closed conformational change. | |||||
書誌情報 |
Journal of biochemistry 巻 145, 号 4, p. 467-479, 発行日 2009-04 |
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出版者 | ||||||
出版者 | 日本生化学会 | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0021924X | |||||
EISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 1756-2651 | |||||
書誌レコードID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA00694073 | |||||
PubMed番号 | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | PMID | |||||
関連識別子 | 19122202 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1093/jb/mvn186 | |||||
権利 | ||||||
権利情報 | (c) The Authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved | |||||
著者版フラグ | ||||||
出版タイプ | AM | |||||
出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
引用 | ||||||
内容記述タイプ | Other | |||||
内容記述 | Journal of biochemistry, 145(4), pp.467-479; 2009 |