RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/10572139http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10572139http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10572139http://www.w3.org/2000/01/rdf-schema#comment"The gene celF of the cryptic cel operon of Escherichia coli has been cloned, and the encoded 6-phospho-beta-glucosidase (cellobiose-6-phosphate [6P] hydrolase; CelF [EC 3.2.1.86]) has been expressed and purified in a catalytically active state. Among phospho-beta-glycosidases, CelF exhibits unique requirements for a divalent metal ion and NAD(+) for activity and, by sequence alignment, is assigned to family 4 of the glycosylhydrolase superfamily. CelF hydrolyzed a variety of P-beta-glucosides, including cellobiose-6P, salicin-6P, arbutin-6P, gentiobiose-6P, methyl-beta-glucoside-6P, and the chromogenic analog, p-nitrophenyl-beta-D-glucopyranoside-6P. In the absence of a metal ion and NAD(+), purified CelF was rapidly and irreversibly inactivated. The functional roles of the cofactors have not been established, but NAD(+) appears not to be a reactant and there is no evidence for reduction of the nucleotide during substrate cleavage. In solution, native CelF exists as a homotetramer (M(w), approximately 200,000) composed of noncovalently linked subunits, and this oligomeric structure is maintained independently of the presence or absence of a metal ion. The molecular weight of the CelF monomer (M(r), approximately 50,000), estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, is in agreement with that calculated from the amino acid sequence of the polypeptide (450 residues; M(r) = 50,512). Comparative sequence alignments provide tentative identification of the NAD(+)-binding domain (residues 7 to 40) and catalytically important glutamyl residues (Glu(112) and Glu(356)) of CelF."xsd:string
http://purl.uniprot.org/citations/10572139http://purl.org/dc/terms/identifier"doi:10.1128/jb.181.23.7339-7345.1999"xsd:string
http://purl.uniprot.org/citations/10572139http://purl.org/dc/terms/identifier"doi:10.1128/jb.181.23.7339-7345.1999"xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/author"Thompson J."xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/author"Thompson J."xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/author"Hall B.G."xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/author"Hall B.G."xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/author"Ruvinov S.B."xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/author"Ruvinov S.B."xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/author"Freedberg D.I."xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/author"Freedberg D.I."xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/pages"7339-7345"xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/pages"7339-7345"xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/title"Cellobiose-6-phosphate hydrolase (CelF) of Escherichia coli: characterization and assignment to the unusual family 4 of glycosylhydrolases."xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/title"Cellobiose-6-phosphate hydrolase (CelF) of Escherichia coli: characterization and assignment to the unusual family 4 of glycosylhydrolases."xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/volume"181"xsd:string
http://purl.uniprot.org/citations/10572139http://purl.uniprot.org/core/volume"181"xsd:string
http://purl.uniprot.org/citations/10572139http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10572139
http://purl.uniprot.org/citations/10572139http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10572139