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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Bacillus subtilis / enzymology*
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Binding Sites
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Crystallography, X-Ray
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Glycosides / metabolism*
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L-Lactate Dehydrogenase / chemistry
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L-Lactate Dehydrogenase / genetics
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L-Lactate Dehydrogenase / metabolism
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Manganese / metabolism*
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Models, Molecular
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Molecular Sequence Data
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Molecular Structure
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NAD / chemistry*
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NAD / genetics
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NAD / metabolism*
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Protein Conformation*
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sequence Alignment
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Substrate Specificity
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alpha-Glucosidases / chemistry*
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alpha-Glucosidases / genetics
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alpha-Glucosidases / metabolism
Substances
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Bacterial Proteins
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Glycosides
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Recombinant Proteins
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NAD
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Manganese
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L-Lactate Dehydrogenase
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maltose-6'-phosphate glucosidase
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alpha-Glucosidases