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http://purl.uniprot.org/citations/15237973http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15237973http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15237973http://www.w3.org/2000/01/rdf-schema#comment"Among the numerous well-characterized families of glycosidases, family 4 appears to be the anomaly, requiring both catalytic NAD+ and a divalent metal for activity. The unusual cofactor requirement prompted the proposal of a mechanism involving key NAD+-mediated redox steps as well as elimination of the glycosidic oxygen. Primary kinetic isotope effects for the 2- and 3-deutero substrate analogues, isotopic exchange with solvent, and structural analysis of a 6-phospho-beta-glucosidase, BglT (E.C. 3.2.1.6), provided evidence in support of the proposed mechanism, which has striking resemblances to that of the sugar dehydratases. Furthermore, analysis of the stereochemical outcome indicated that family 4 enzymes are retaining glycosidases."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.org/dc/terms/identifier"doi:10.1021/ja047632w"xsd:string
http://purl.uniprot.org/citations/15237973http://purl.org/dc/terms/identifier"doi:10.1021/ja047632w"xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Anderson W.F."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Anderson W.F."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Davies G.J."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Davies G.J."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Rajan S.S."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Rajan S.S."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Thompson J."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Thompson J."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Yang X."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Yang X."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Varrot A."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Varrot A."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Withers S.G."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Withers S.G."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Yip V.L.Y."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/author"Yip V.L.Y."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/name"J. Am. Chem. Soc."xsd:string
http://purl.uniprot.org/citations/15237973http://purl.uniprot.org/core/name"J. Am. Chem. Soc."xsd:string