http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID187665
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs. 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. |
| title | type2_17beta_HSD-like_SDR_c |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12594091 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/23348248 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2891610 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7069461 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/23244160 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1593773 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11202089 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16710222 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3572512 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18571449 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10564311 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16710219 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12436988 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/362763 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10564095 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20634749 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20634752 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1524449 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9101072 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7012779 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20647905 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10413281 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11999127 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18562181 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/23928768 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/26126890 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
Total number of triples: 54.