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X-ray crystal structures of alpha-amylase I from Eisenia fetida
https://repo.qst.go.jp/records/77138
https://repo.qst.go.jp/records/771384ad03ce8-af99-4658-ac4b-751c7c0b4336
Item type | 会議発表用資料 / Presentation(1) | |||||
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公開日 | 2019-10-09 | |||||
タイトル | ||||||
タイトル | X-ray crystal structures of alpha-amylase I from Eisenia fetida | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_c94f | |||||
資源タイプ | conference object | |||||
アクセス権 | ||||||
アクセス権 | metadata only access | |||||
アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
著者 |
Hirano, Yuu
× Hirano, Yuu× Tsukamoto, Kana× Yuki, Naka× Ueda, Mitsuhiro× Tamada, Taro× Hirano, Yuu× Tamada, Taro |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | The earthworm Eisenia fetida has some cold-adapted carbohydrases including alpha-amylase, cellulase, glucanase and beta-mannanase. We have identified two types of raw-starch digesting alpha-amylases from E. fetida (Ef-Amy I and II), which exhibit activities at low-temperatures. In this study, X-ray structure analyses were performed to understand the molecular mechanisms in biochemical properties of Ef-Amy I. Ef-Amy I shows structural similarities with alpha-amylases from porcine pancreatic and human pancreatic. The surface electrostatic potential indicates that large part of surface area consists of acidic residues in Ef-Amy I. We also determined X-ray crystal structures of the inactive mutant (E249Q) of Ef-Amy I both in apo and substrate complex forms. An electron density map shows a maltohexaose molecule binding at the active site and an electron density blob corresponds to maltotetraose was observed around the cleft between the N and C terminal domains. These structural features display important characteristics for cold-adaptation and substrate recognition in Ef-Amy I. | |||||
会議概要(会議名, 開催地, 会期, 主催者等) | ||||||
内容記述タイプ | Other | |||||
内容記述 | International symposium on diffraction structural biology 2019 | |||||
発表年月日 | ||||||
日付 | 2019-10-18 | |||||
日付タイプ | Issued |