| http://purl.uniprot.org/citations/11418619 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11418619 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11418619 | http://www.w3.org/2000/01/rdf-schema#comment | "The cDNA of a novel human glutathione transferase (GST) of the Alpha class was cloned, and the corresponding protein, denoted GST A3-3, was heterologously expressed and characterized. GST A3-3 was found to efficiently catalyze obligatory double-bond isomerizations of Delta(5)-androstene-3,17-dione and Delta(5)-pregnene-3,20-dione, precursors to testosterone and progesterone, respectively, in steroid hormone biosynthesis. The catalytic efficiency (k(cat)/K(m)) with Delta(5)-androstene-3,17-dione was determined as 5 x 10(6) m(-1) s(-1), which is considerably higher than with any other GST substrate tested. The rate of acceleration afforded by GST A3-3 is 6 x 10(8) based on the ratio between k(cat) and the rate constant for the nonenzymatic isomerization of Delta(5)-androstene-3,17-dione. Besides being high in absolute numbers, the k(cat)/K(m) value of GST A3-3 exceeds by a factor of approximately 230 that of 3beta-hydroxysteroid dehydrogenase/isomerase, the enzyme generally considered to catalyze the Delta(5)-Delta(4) double-bond isomerization. Furthermore, GSTA3-specific polymerase chain reaction analysis of cDNA libraries from various tissues showed a message only in those characterized by active steroid hormone biosynthesis, indicating a selective expression of GST A3-3 in these tissues. Based on this finding and the high activity with steroid substrates, we propose that GST A3-3 has evolved to catalyze isomerization reactions that contribute to the biosynthesis of steroid hormones."xsd:string |
| http://purl.uniprot.org/citations/11418619 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m104539200"xsd:string |
| http://purl.uniprot.org/citations/11418619 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m104539200"xsd:string |
| http://purl.uniprot.org/citations/11418619 | http://purl.uniprot.org/core/author | "Mannervik B."xsd:string |
| http://purl.uniprot.org/citations/11418619 | http://purl.uniprot.org/core/author | "Mannervik B."xsd:string |
| http://purl.uniprot.org/citations/11418619 | http://purl.uniprot.org/core/author | "Johansson A.-S."xsd:string |
| http://purl.uniprot.org/citations/11418619 | http://purl.uniprot.org/core/author | "Johansson A.-S."xsd:string |
| http://purl.uniprot.org/citations/11418619 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11418619 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11418619 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11418619 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11418619 | http://purl.uniprot.org/core/pages | "33061-33065"xsd:string |
| http://purl.uniprot.org/citations/11418619 | http://purl.uniprot.org/core/pages | "33061-33065"xsd:string |
| http://purl.uniprot.org/citations/11418619 | http://purl.uniprot.org/core/title | "Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones."xsd:string |
| http://purl.uniprot.org/citations/11418619 | http://purl.uniprot.org/core/title | "Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones."xsd:string |
| http://purl.uniprot.org/citations/11418619 | http://purl.uniprot.org/core/volume | "276"xsd:string |
| http://purl.uniprot.org/citations/11418619 | http://purl.uniprot.org/core/volume | "276"xsd:string |
| http://purl.uniprot.org/citations/11418619 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11418619 |
| http://purl.uniprot.org/citations/11418619 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11418619 |
| http://purl.uniprot.org/citations/11418619 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11418619 |
| http://purl.uniprot.org/citations/11418619 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11418619 |
| http://purl.uniprot.org/uniprot/Q16772 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11418619 |
| http://purl.uniprot.org/uniprot/Q16772#attribution-28D318F2FDA472856380A307332CC264 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/11418619 |