| Literature DB >> 15341727 |
Shyamala S Rajan1, Xiaojing Yang, Frank Collart, Vivian L Y Yip, Stephen G Withers, Annabelle Varrot, John Thompson, Gideon J Davies, Wayne F Anderson.
Abstract
GlvA, a 6-phospho-alpha-glucosidase from Bacillus subtilis, catalyzes the hydrolysis of maltose-6'-phosphate and belongs to glycoside hydrolase family GH4. GH4 enzymes are unique in their requirement for NAD(H) and a divalent metal for activity. We have determined the crystal structure of GlvA in complex with its ligands to 2.05 A resolution. Analyses of the active site architecture, in conjunction with mechanistic studies and precedent from the nucleotide diphosphate hexose dehydratases and other systems, suggest a novel mechanism of glycoside hydrolysis by GlvA that involves both the NAD(H) and the metal.Entities:
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Year: 2004 PMID： 15341727 DOI： 10.1016/j.str.2004.06.020
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006