Novel Catalytic Mechanism of Glycoside Hydrolysis Based on the Structure of an NAD+/Mn2+-Dependent Phospho-α-Glucosidase from Bacillus subtilis

Molecular Pharmacology and Biological Chemistry, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
Structure (Impact Factor: 6.79). 10/2004; 12(9):1619-29. DOI: 10.1016/j.str.2004.06.020
Source: PubMed

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.

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