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http://purl.uniprot.org/citations/8672244http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8672244http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8672244http://www.w3.org/2000/01/rdf-schema#comment"In contrast to humans, who possess a hydroxysteroid sulfotransferase (HSST), namely, DHEA sulfotransferase (DHEA-ST), that displays broad substrate specificities, HSSTs of the guinea pig show a high substrate stereoselectivity, as shown by the recent cloning of a chiral-specific 3alpha-hydroxysteroid sulfotransferase. Herein, we report the cloning and expression of the substrate and chiral-specific pregnenolone sulfotransferase (PREG-ST). Transfection of the pCMV expression vector containing PREG-ST cDNA in transformed human embryonal kidney (293) cells showed that the expressed enzyme selectively catalyzes the 3beta-hydroxysteroid substrate. It converts pregnenolone to pregnenolone sulfate most efficiently, whereas dehydroepiandrosterone and epiandrosterone were transformed at a much lower rate, and androsterone, a 3alpha-hydroxysteroid, was not significantly metabolized (30-fold lower). Thus, the enzyme was identified as pregnenolone sulfotransferase. DNA analysis predicts a protein of 287 amino acids with a calculated molecular mass of 34,199 daltons. Alignment of the amino acid sequence with other sulfotransferases indicated that guinea pig pregnenolone sulfotransferase shares 75 and 80% homology with human DHEA sulfotransferase and rat hydroxysteroid dehydrogenase, respectively. RNA blot analysis using guinea pig liver, intestine, adrenal, kidney, epididymis, testis, and lung showed a single RNA species at 1.3 kb is expressed in liver, intestine, and kidney. Guinea pig 3beta-hydroxysteroid sulfotransferase is thus different from that in humans, who possess two mRNA species of 1.3 and 1.8 kb."xsd:string
http://purl.uniprot.org/citations/8672244http://purl.org/dc/terms/identifier"doi:10.1089/dna.1996.15.481"xsd:string
http://purl.uniprot.org/citations/8672244http://purl.org/dc/terms/identifier"doi:10.1089/dna.1996.15.481"xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/author"Belanger A."xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/author"Belanger A."xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/author"Labrie F."xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/author"Labrie F."xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/author"Luu-The V."xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/author"Luu-The V."xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/author"Dufort I."xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/author"Dufort I."xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/author"Tremblay Y."xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/author"Tremblay Y."xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/name"DNA Cell Biol."xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/name"DNA Cell Biol."xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/pages"481-487"xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/pages"481-487"xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/title"Isolation and characterization of a stereospecific 3beta-hydroxysteriod sulfotransferase (pregnenolone sulfotransferase) cDNA."xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/title"Isolation and characterization of a stereospecific 3beta-hydroxysteriod sulfotransferase (pregnenolone sulfotransferase) cDNA."xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/8672244http://purl.uniprot.org/core/volume"15"xsd:string