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http://purl.uniprot.org/citations/9765262http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9765262http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9765262http://www.w3.org/2000/01/rdf-schema#comment"The gene glvA (formerly glv-1) from Bacillus subtilis has been cloned and expressed in Escherichia coli. The purified protein GlvA (449 residues, Mr = 50,513) is a unique 6-phosphoryl-O-alpha-D-glucopyranosyl:phosphoglucohydrolase (6-phospho-alpha-glucosidase) that requires both NAD(H) and divalent metal (Mn2+, Fe2+, Co2+, or Ni2+) for activity. 6-Phospho-alpha-glucosidase (EC 3.2.1.122) from B. subtilis cross-reacts with polyclonal antibody to maltose 6-phosphate hydrolase from Fusobacterium mortiferum, and the two proteins exhibit amino acid sequence identity of 73%. Estimates for the Mr of GlvA determined by SDS-polyacrylamide gel electrophoresis (51,000) and electrospray-mass spectroscopy (50,510) were in excellent agreement with the molecular weight of 50,513 deduced from the amino acid sequence. The sequence of the first 37 residues from the N terminus determined by automated analysis agreed precisely with that predicted by translation of glvA. The chromogenic and fluorogenic substrates, p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate and 4-methylumbelliferyl-alpha-D-glucopyranoside 6-phosphate were used for the discontinuous assay and in situ detection of enzyme activity, respectively. Site-directed mutagenesis shows that three acidic residues, Asp41, Glu111, and Glu359, are required for GlvA activity. Asp41 is located at the C terminus of a betaalphabeta fold that may constitute the dinucleotide binding domain of the protein. Glu111 and Glu359 may function as the catalytic acid (proton donor) and nucleophile (base), respectively, during hydrolysis of 6-phospho-alpha-glucoside substrates including maltose 6-phosphate and trehalose 6-phosphate. In metal-free buffer, GlvA exists as an inactive dimer, but in the presence of Mn2+ ion, these species associate to form the NAD(H)-dependent catalytically active tetramer. By comparative sequence alignment with its homologs, the novel 6-phospho-alpha-glucosidase from B. subtilis can be assigned to the nine-member family 4 of the glycosylhydrolase superfamily."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.42.27347"xsd:string
http://purl.uniprot.org/citations/9765262http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.42.27347"xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/author"Henrissat B."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/author"Henrissat B."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/author"Pikis A."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/author"Pikis A."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/author"Thompson J."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/author"Thompson J."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/author"Yamamoto H."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/author"Yamamoto H."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/author"Sekiguchi J."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/author"Sekiguchi J."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/author"Ruvinov S.B."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/author"Ruvinov S.B."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/pages"27347-27356"xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/pages"27347-27356"xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/title"The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-alpha-glucosidase. Assignment to family 4 of the glycosylhydrolase superfamily."xsd:string
http://purl.uniprot.org/citations/9765262http://purl.uniprot.org/core/title"The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-alpha-glucosidase. Assignment to family 4 of the glycosylhydrolase superfamily."xsd:string
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