WEKO3
アイテム
X-ray crystallographic structural studies of α-amylase I from Eisenia fetida
https://repo.qst.go.jp/records/80542
https://repo.qst.go.jp/records/80542a7ad42a1-dd52-4f32-a6d0-c272ed3b159f
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2020-07-27 | |||||
| タイトル | ||||||
| タイトル | X-ray crystallographic structural studies of α-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_6501 | |||||
| 資源タイプ | journal article | |||||
| 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× Ariki, Shingo× Naka, Yuki× Ueda, Mitsuhiro× Tamada, Taro× Yuu, Hirano× Taro, Tamada |
|||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | The earthworm Eisenia fetida has some cold-active enzymes including α-amylase, β-glucanase, and β-mannanase. E. fetida possesses two isoforms of α-amylase (Ef-Amy I and II), to digest raw starch. Ef-Amy I retains its catalytic activity at temperatures below 10˚C. To identify the molecular properties of Ef-Amy I, X-ray crystal structures were determined using wild type and the inactive E249Q mutant. Ef-Amy I has structural similarities to mammalian α-amylases, including porcine pancreatic and human pancreatic α-amylases. Structural comparisons between both the overall structures as well as the Ca2+ binding sites in Ef-Amy I and the mammalian α-amylases indicate that the Ef-Amy I has increased structural flexibility and more solvent-exposed acidic residues. These structural features in Ef-Amy I can contribute to the observed catalytic activities at low temperatures because many cold-adapted enzymes have similar structural properties. The structure of the substrate complex in the inactive mutant of Ef-Amy I shows that a maltohexaose molecule is bound at the active site and a maltotetraose is bound at the cleft between the N- and C-terminal domains. The recognition of substrate molecules in Ef-Amy I exhibits some differences from those observed in the structures of human pancreatic α-amylase. This result provides insights into the structural modulation of the recognition of substrates and inhibitors. | |||||
| 書誌情報 |
Acta Crystallographica Section D 巻 76, p. 834-844, 発行日 2020-08 |
|||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 2059-7983 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1107/S2059798320010165 | |||||
| 関連サイト | ||||||
| 識別子タイプ | URI | |||||
| 関連識別子 | http://scripts.iucr.org/cgi-bin/paper?yl5001 | |||||
