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Functional analyses of Tyr420 and Leu607 of Alicyclobacillus acidocaldarius squalene-hopene cyclase. Neoachillapentaene, a novel triterpene with the 1, 5, 6-trimethylcyclohexene moiety produced through a folding of the constrained boat structure.
http://hdl.handle.net/10191/6339
http://hdl.handle.net/10191/6339e7f37324-62fd-47dc-ae5c-523ce7e9951a
名前 / ファイル | ライセンス | アクション |
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2008-04-23 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Functional analyses of Tyr420 and Leu607 of Alicyclobacillus acidocaldarius squalene-hopene cyclase. Neoachillapentaene, a novel triterpene with the 1, 5, 6-trimethylcyclohexene moiety produced through a folding of the constrained boat structure. | |||||
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 | terpene cyclase | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | un-natural natural product | |||||
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× Sasahara, Shigehiro× Yamakami, Toshiyuki× Hoshino, Tsutomu |
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著者別名 | ||||||
識別子 | 4314 | |||||
識別子Scheme | WEKO | |||||
姓名 | 佐藤, 努 | |||||
言語 | ja | |||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | The functions of Tyr420 and Leu607 were analyzed by constructing various site-directed mutants. The mutation at position 420 into Ala and Gly gave bicyclic α- and γ-polypodatetraene in significant amounts, but with a trace amount of tricyclic malabaricatriene. The kinetic data for and the product distribution of the Y420F mutant indicate that the major function of Tyr420 is to stabilize the 6/6-fused bicyclic cation. Mutation experiments on Leu607 demonstrate that the appropriate steric bulk size at position 607 is required to strongly bind with the product-like conformation formed during the polycyclization process. Introduction of the bulkiest Tip residue into 420 or 607 led to the production of a novel monocyclic triterpene having the (5R, 6R)-1,5,6-trimethylcyclohexene ring, named neoachillapentaene,indicating that the enzymatic cyclization proceeded via a constrained boat structure. Folding of the squalene molecule into a boat conformation by squalene cyclase has not been reported before. | |||||
書誌情報 |
en : Bioscience, Biotechnology, and Biochemistry 巻 66, 号 8, p. 1660-1670, 発行日 2002 |
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出版者 | ||||||
言語 | en | |||||
出版者 | Japan Society for Bioscience, Biotechnology, and Agrochemistry | |||||
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.66.1660 | |||||
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 |