EC number:1.1.1.209
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.1 Acting on the CH-OH group of donors |
| 1.1.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.1.1.209 |
|---|---|
| Description: | 3(or 17)-alpha-hydroxysteroid dehydrogenase. |
| Cath: | 3.20.20.10; 3.20.20.100; 3.40.50.720; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.1.1.209 |
| BRENDA Enzyme Link: | BRENDA 1.1.1.209 |
| KEGG Enzyme Link: | KEGG1.1.1.209 |
| BioCyc Enzyme Link: | BioCyc 1.1.1.209 |
| ExPASy Enzyme Link: | ExPASy1.1.1.209 |
| EC2PDB Enzyme Link: | EC2PDB 1.1.1.209 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.1.1.209 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.1.1.209 |
| IntEnz Enzyme Link: | IntEnz 1.1.1.209 |
| MEDLINE Enzyme Link: | MEDLINE 1.1.1.209 |
EC number:1.1.1.209
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:20381 | 3alpha-hydroxy-5alpha-androstan-17-one + NAD(+) = 5alpha-androstan-3,17-dione + H(+) + NADH |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1 |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| cDNA cloning and characterization of a cis-retinol/3alpha-hydroxysterol short-chain dehydrogenase. | Chai X, Zhai Y, Napoli JL | 1997 Dec 26 | 9407098 |
| Studies on a Tyr residue critical for the binding of coenzyme and substrate in mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21): structure of the Y224D mutant enzyme. | Dhagat U, Endo S, Mamiya H, Hara A, El-Kabbani O | 2010 Feb | 20124700 |
| Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto reductases: identification and characterization of amino acid residues critical for substrate binding. | Faucher F, Cantin L, Pereira de Jésus-Tran K, Lemieux M, Luu-The V, Labrie F, Breton R | 2007 Jun 1 | 17442338 |
| Characterization of two isoforms of mouse 3(17)alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase family. | Ishikura S, Usami N, Nakajima S, Kameyama A, Shiraishi H, Carbone V, El-Kabbani O, Hara A | 2004 Dec | 15577209 |
| Directed evolution approach to a structural genomics project: Rv2002 from Mycobacterium tuberculosis. | Yang JK, Park MS, Waldo GS, Suh SW | 2003 Jan 21 | 12524453 |
| Further characterization of human microsomal 3alpha-hydroxysteroid dehydrogenase. | Chetyrkin SV, Hu J, Gough WH, Dumaual N, Kedishvili NY | 2001 Feb 1 | 11360992 |
| Characterization of a novel type of human microsomal 3alpha -hydroxysteroid dehydrogenase: unique tissue distribution and catalytic properties. | Chetyrkin SV, Belyaeva OV, Gough WH, Kedishvili NY | 2001 Jun 22 | 11294878 |
| Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones. | Penning TM, Burczynski ME, Jez JM, Hung CF, Lin HK, Ma H, Moore M, Palackal N, Ratnam K | 2000 Oct 1 | 10998348 |
| RHEA:20377 | 3alpha-hydroxy-5alpha-androstan-17-one + NADP(+) = 5alpha-androstan-3,17-dione + H(+) + NADPH |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1 |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Studies on a Tyr residue critical for the binding of coenzyme and substrate in mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21): structure of the Y224D mutant enzyme. | Dhagat U, Endo S, Mamiya H, Hara A, El-Kabbani O | 2010 Feb | 20124700 |
| Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto reductases: identification and characterization of amino acid residues critical for substrate binding. | Faucher F, Cantin L, Pereira de Jésus-Tran K, Lemieux M, Luu-The V, Labrie F, Breton R | 2007 Jun 1 | 17442338 |
| Characterization of two isoforms of mouse 3(17)alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase family. | Ishikura S, Usami N, Nakajima S, Kameyama A, Shiraishi H, Carbone V, El-Kabbani O, Hara A | 2004 Dec | 15577209 |
| Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones. | Penning TM, Burczynski ME, Jez JM, Hung CF, Lin HK, Ma H, Moore M, Palackal N, Ratnam K | 2000 Oct 1 | 10998348 |