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http://purl.uniprot.org/citations/9731776http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9731776http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9731776http://www.w3.org/2000/01/rdf-schema#comment"The catalytic mechanism of 'retaining' beta-glycosidases has been the subject of considerable interest and debate for many years. The visualization of a covalent glycosyl enzyme intermediate by X-ray crystallography was first accomplished with a saccharide substrate substituted with fluorine at its 2-position. The structure implicated major roles for residue His 205 and for the 2-hydroxyl position of the proximal saccharide in binding and catalysis. Here we have studied the kinetic behavior of various His 205 mutants. One of these mutants, a double mutant H205N/E127A, has been used to stabilize a covalent glycosyl-enzyme intermediate involving an unsubstituted sugar, permitting crystallographic analysis of the interactions between its 2-hydroxyl group and the enzyme."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.org/dc/terms/identifier"doi:10.1038/1852"xsd:string
http://purl.uniprot.org/citations/9731776http://purl.org/dc/terms/identifier"doi:10.1038/1852"xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/author"Withers S.G."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/author"Withers S.G."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/author"Warren R.A."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/author"Warren R.A."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/author"Rose D.R."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/author"Rose D.R."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/author"Birsan C."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/author"Birsan C."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/author"Nitz M."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/author"Nitz M."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/author"Notenboom V."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/author"Notenboom V."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/pages"812-818"xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/pages"812-818"xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/title"Insights into transition state stabilization of the beta-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutants."xsd:string
http://purl.uniprot.org/citations/9731776http://purl.uniprot.org/core/title"Insights into transition state stabilization of the beta-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutants."xsd:string