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Site-directed mutagenesis experiments on the putative deprotonation site of squalene-hopene cyclase from Alicyclobacillus acidocaldarius.
http://hdl.handle.net/10191/6338
http://hdl.handle.net/10191/6338a8eb7591-bf7e-4c4a-9e0e-9a3e80f8b206
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
07_0014.pdf (186.7 kB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2008-04-23 | |||||
| タイトル | ||||||
| タイトル | Site-directed mutagenesis experiments on the putative deprotonation site of squalene-hopene cyclase from Alicyclobacillus acidocaldarius. | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | squalene | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | terpene cyclase | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | triterpene | |||||
| 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 |
Sato, Tsutomu
× Sato, Tsutomu× Kouda, Masanori× Hoshino, Tsutomu |
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| 著者別名 | ||||||
| 識別子Scheme | WEKO | |||||
| 識別子 | 4303 | |||||
| 姓名 | 佐藤, 努 | |||||
| 言語 | ja | |||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | To provide insight into the catalytic mechanism for the final deprotonation reaction of squalene-hopene cyclase (SHC) from Alicyclobacillus acidocaldarius, mutagenesis experiments were conducted for the following ten residues: Thr41, Glu45, Glu93, Arg127, Trp133, Gln262, Pro263, Tyr267, Phe434 and Phe437. An X-ray analysis of SHC has revealed that two types of water molecules ("front water" and "back waters") were involved around the deprotonation site. The results of these mutagenesis experiments allow us to propose the functions of these residues. The two residues of Gln262 and Pro263 probably work to keep away the isopropyl group of the hopanyl cation intermediate from the "front water molecule," that is, to place the "front water" in a favorable position, leading to the minimal production of by-products, i.e., hopanol and hop-21(22)-ene. The five residues of Thr41, Glu45, Glu93, Arg127 and Trp133, by which the hydrogen-bonded network incorporating the "back waters" is constructed, increase the polarization of the "front water" to facilitate proton elimination from the isopropyl moiety of the hopanyl cation, leading to the normal product, hop-22(29)-ene. The three aromatic residues of Tyr267, Phe434 and Phe437 are likely to play an important role in guiding squalene from the enzyme surface to the reaction cavity (substrate channeling) by the strong affinity of their aromatic residues to the squalene substrate. | |||||
| 言語 | en | |||||
| 書誌情報 |
en : Bioscience, Biotechnology, and Biochemistry 巻 68, 号 3, p. 728-738, 発行日 2004 |
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| 出版者 | ||||||
| 出版者 | Japan Society for Bioscience, Biotechnology, and Agrochemistry | |||||
| 言語 | en | |||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0916-8451 | |||||
| 書誌レコードID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AA10824164 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | http://doi.org/10.1271/bbb.68.728 | |||||
| 出版タイプ | ||||||
| 出版タイプ | VoR | |||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
| 著者版フラグ | ||||||
| 値 | publisher | |||||
