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http://purl.uniprot.org/citations/9668121http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9668121http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9668121http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/9668121http://www.w3.org/2000/01/rdf-schema#comment"The universal sulfonate donor, 3'-phosphoadenosine 5'-phosphosulfate (PAPS), is synthesized by the concerted action of ATP sulfurylase and adenosine 5'-phosphosulfate (APS) kinase, which in animals are fused into a bifunctional protein. The cDNA for human PAPS synthase (hPAPSS) along with polymerase chain reaction products corresponding to several NH2- and COOH-terminal fragments were cloned and expressed in COS-1 cells. A 1-268-amino acid fragment expressed APS kinase activity, whereas a 220-623 fragment evinced ATP sulfurylase activity. The 1-268 fragment and full-length hPAPSS (1-623) exhibited hyperbolic responses against APS substrate with equivalent Km values (0.6 and 0.4 microM, respectively). The 1-268 fragment demonstrated Michaelis-Menten kinetics against ATP as substrate (Km 0.26 mM); however, full-length hPAPSS exhibited a sigmoidal response (apparent Km 1.5 mM) suggesting cooperative binding. Catalytic efficiency (Vmax/Km) of the 1-268 fragment was 64-fold higher than full-length hPAPSS for ATP. The kinetic data suggest that the COOH-terminal domain of hPAPSS exerts a regulatory role over APS kinase activity located in the NH2-terminal domain of this bifunctional protein. In addition, the 1-268 fragment and full-length hPAPSS were overexpressed in Escherichia coli and column purified. Purified full-length hPAPSS, in contrast to the COS-1 cell-expressed cDNA construct, exhibited a hyperbolic response curve against ATP suggesting that hPAPSS is perhaps modified in vivo."xsd:string
http://purl.uniprot.org/citations/9668121http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.30.19311"xsd:string
http://purl.uniprot.org/citations/9668121http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.30.19311"xsd:string
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/author"Akita H."xsd:string
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/author"Akita H."xsd:string
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/author"Strott C.A."xsd:string
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/author"Strott C.A."xsd:string
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/author"Venkatachalam K.V."xsd:string
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/author"Venkatachalam K.V."xsd:string
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/pages"19311-19320"xsd:string
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/pages"19311-19320"xsd:string
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/title"Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains."xsd:string
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/title"Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains."xsd:string
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/volume"273"xsd:string
http://purl.uniprot.org/citations/9668121http://purl.uniprot.org/core/volume"273"xsd:string
http://purl.uniprot.org/citations/9668121http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9668121
http://purl.uniprot.org/citations/9668121http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9668121
http://purl.uniprot.org/citations/9668121http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9668121