@misc{oai:repo.qst.go.jp:00077138,
 author = {Hirano, Yuu and Tsukamoto, Kana and Yuki, Naka and Ueda, Mitsuhiro and Tamada, Taro and Hirano, Yuu and Tamada, Taro},
 month = {Oct},
 note = {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., International symposium on diffraction structural biology 2019},
 title = {X-ray crystal structures of alpha-amylase I from Eisenia fetida},
 year = {2019}
}