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Catalytic function of the residues of phenylalanine and tyrosine conserved in squalene-hopene cyclases.
http://hdl.handle.net/10191/6340
http://hdl.handle.net/10191/634051665cf4-3dd1-44c8-8ece-4426cae53a7c
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
07_0016.pdf (1.3 MB)
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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 | Catalytic function of the residues of phenylalanine and tyrosine conserved in squalene-hopene cyclases. | |||||
| 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 | hopene | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | triterpene | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | terpene cyclase | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | Alicyclobacillus acidocaldarius | |||||
| 資源タイプ | ||||||
| 資源 | http://purl.org/coar/resource_type/c_6501 | |||||
| タイプ | journal article | |||||
| 著者 |
Sato, Tsutomu
× Sato, Tsutomu× Hoshino, Tsutomu |
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| 著者別名 | ||||||
| 識別子Scheme | WEKO | |||||
| 識別子 | 4348 | |||||
| 姓名 | 佐藤, 努 | |||||
| 言語 | ja | |||||
| 著者別名 | ||||||
| 識別子Scheme | WEKO | |||||
| 識別子 | 4349 | |||||
| 姓名 | 星野, 力 | |||||
| 言語 | ja | |||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Site-directed mutagenesis experiments on all the conserved residues of Phe and Tyr in all the known squalene-hopene cyclases (SHCs) were carried out to identify the active site residues of thermophilic Alicyclobacillus acidocaldarius SHC. The following functions are proposed on the basis of kinetic data and trapping of the prematurely cyclized products: (1) The Y495 residue probably amplifies the D376 acidity, which is assumed to work as a proton donor for initiating the polycyclization cascade, but its role is moderate. (2) Y609 possibly assists the function of F365, which has previously been assigned to exclusively stabilize the C-8 carbocation intermediate through cation-π interaction. The Y609A mutant produced a partially cyclized bicyclic triterpene. (3) Y612 works to stabilize both the C10 and C8 carbocations, this being verified by the finding that mono- and bicyclic products were formed with the Y612A mutant. (4) F129 was first identified to play a crucial role in catalysis. (5) The three residues, Y372, Y474 and Y540, are responsible for reinforcing the protein structure against thermal denaturation, Y474 being located inside QW motif 3. | |||||
| 言語 | en | |||||
| 書誌情報 |
en : Bioscience, Biotechnology, and Biochemistry 巻 65, 号 10, p. 2233-2242, 発行日 2001 |
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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.65.2233 | |||||
| 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 | |||||
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Cite as
Sato, Tsutomu, Hoshino, Tsutomu, 2001, Catalytic function of the residues of phenylalanine and tyrosine conserved in squalene-hopene cyclases.: Japan Society for Bioscience, Biotechnology, and Agrochemistry, 2233–2242 p.
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