Journal of Applied Glycoscience
Online ISSN : 1880-7291
Print ISSN : 1344-7882
ISSN-L : 1344-7882
Regular Papers
Molecular Modeling and Implications of a Bacillus α-Amylase that Acquires Enhanced Thermostability and Chelator Resistance by Deletion of an Arginine-glycine Residue
Tadahiro OzawaKazuaki IgarashiKatsuya OzakiTohru KobayashiAtsuo SuzukiTsuyoshi ShiraiTakashi YamaneSusumu Ito
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2006 Volume 53 Issue 3 Pages 193-197


Resistance to chelators, as well as thermostability, of an alkaline α-amylase (AmyK, formerly named LAMY) from an alkaliphilic Bacillus sp. strain was significantly improved by deletion of Arg181-Gly182. To clarify the mechanism of thermostability and chelator resistance conferred by the deletion mutation, we constructed models of AmyK with the 3D structure of α-amylase from Bacillus amyloliquefaciens as the template. In the structural models, Ala186 and Asp188 on a loop were both coordinated with a structural calcium ion. Molecular dynamics simulations suggested that the affinity of the Ala186 carbonyl oxygen to the calcium ion in the mutant enzyme was strengthened, thereby causing enhanced thermostability and the chelator resistance.

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© 2006 by The Japanese Society of Applied Glycoscience
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