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http://purl.uniprot.org/citations/14718531http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14718531http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14718531http://www.w3.org/2000/01/rdf-schema#comment"The glucose-6-phosphatase (Glc-6-Pase) family comprises two active endoplasmic reticulum (ER)-associated isozymes: the liver/kidney/intestine Glc-6-Pase-alpha and the ubiquitous Glc-6-Pase-beta. Both share similar kinetic properties. Sequence alignments predict the two proteins are structurally similar. During glucose 6-phosphate (Glc-6-P) hydrolysis, Glc-6-Pase-alpha, a nine-transmembrane domain protein, forms a covalently bound phosphoryl enzyme intermediate through His(176), which lies on the lumenal side of the ER membrane. We showed that Glc-6-Pase-beta is also a nine-transmembrane domain protein that forms a covalently bound phosphoryl enzyme intermediate during Glc-6-P hydrolysis. However, the intermediate was not detectable in Glc-6-Pase-beta active site mutants R79A, H114A, and H167A. Using [(32)P]Glc-6-P coupled with cyanogen bromide mapping, we demonstrated that the phosphate acceptor in Glc-6-Pase-beta is His(167) and that it lies inside the ER lumen with the active site residues, Arg(79) and His(114). Therefore Glc-6-Pase-alpha and Glc-6-Pase-beta share a similar active site structure, topology, and mechanism of action."xsd:string
http://purl.uniprot.org/citations/14718531http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m313271200"xsd:string
http://purl.uniprot.org/citations/14718531http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m313271200"xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/author"Ghosh A."xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/author"Ghosh A."xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/author"Chou J.Y."xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/author"Chou J.Y."xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/author"Pan C.-J."xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/author"Pan C.-J."xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/author"Shieh J.-J."xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/author"Shieh J.-J."xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/pages"12479-12483"xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/pages"12479-12483"xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/title"Histidine 167 is the phosphate acceptor in glucose-6-phosphatase-beta forming a phosphohistidine enzyme intermediate during catalysis."xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/title"Histidine 167 is the phosphate acceptor in glucose-6-phosphatase-beta forming a phosphohistidine enzyme intermediate during catalysis."xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/14718531http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/14718531http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14718531
http://purl.uniprot.org/citations/14718531http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14718531