| EC Tree |
| 1. Oxidoreductases |
| 1.1 Acting on the CH-OH group of donors |
| 1.1.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.1.1.213 |
|---|---|
| Description: | 3-alpha-hydroxysteroid dehydrogenase (Re-specific). |
| Alternative Name: |
3-alpha-hydroxysteroid dehydrogenase (A-specific). 3-alpha-hydroxysteroid dehydrogenase. |
| Cath: | 3.20.20.10; 3.20.20.100; 3.40.50.720; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 1.1.1.213 |
| BRENDA Enzyme Link: | BRENDA 1.1.1.213 |
| KEGG Enzyme Link: | KEGG1.1.1.213 |
| BioCyc Enzyme Link: | BioCyc 1.1.1.213 |
| ExPASy Enzyme Link: | ExPASy1.1.1.213 |
| EC2PDB Enzyme Link: | EC2PDB 1.1.1.213 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.1.1.213 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.1.1.213 |
| IntEnz Enzyme Link: | IntEnz 1.1.1.213 |
| MEDLINE Enzyme Link: | MEDLINE 1.1.1.213 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:34783 | a 3alpha-hydroxysteroid + NADP(+) = a 3-oxosteroid + 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 |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells. | Hara A, Matsuura K, Tamada Y, Sato K, Miyabe Y, Deyashiki Y, Ishida N | 1996 Jan 15 | 8573067 |
| 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 |
| Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase. | Dufort I, Rheault P, Huang XF, Soucy P, Luu-The V | 1999 Feb | 9927279 |
| Expression and characterization of recombinant type 2 3 alpha-hydroxysteroid dehydrogenase (HSD) from human prostate: demonstration of bifunctional 3 alpha/17 beta-HSD activity and cellular distribution. | Lin HK, Jez JM, Schlegel BP, Peehl DM, Pachter JA, Penning TM | 1997 Dec | 9415401 |
| Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases. | Khanna M, Qin KN, Wang RW, Cheng KC | 1995 Aug 25 | 7650035 |
| Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3). | Penning TM, Burczynski ME, Jez JM, Lin HK, Ma H, Moore M, Ratnam K, Palackal N | 2001 Jan 22 | 11165022 |
| Crystal structures of mouse 17alpha-hydroxysteroid dehydrogenase (apoenzyme and enzyme-NADP(H) binary complex): identification of molecular determinants responsible for the unique 17alpha-reductive activity of this enzyme. | Faucher F, Pereira de Jésus-Tran K, Cantin L, Luu-The V, Labrie F, Breton R | 2006 Dec 8 | 17034817 |
| Comparison of crystal structures of human type 3 3alpha-hydroxysteroid dehydrogenase reveals an "induced-fit" mechanism and a conserved basic motif involved in the binding of androgen. | Couture JF, de Jésus-Tran KP, Roy AM, Cantin L, Côté PL, Legrand P, Luu-The V, Labrie F, Breton R | 2005 Jun | 15929998 |
| Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolution. | Nahoum V, Gangloff A, Legrand P, Zhu DW, Cantin L, Zhorov BS, Luu-The V, Labrie F, Breton R, Lin SX | 2001 Nov 9 | 11514561 |
| RHEA:34779 | a 3alpha-hydroxysteroid + NAD(+) = a 3-oxosteroid + 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 |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells. | Hara A, Matsuura K, Tamada Y, Sato K, Miyabe Y, Deyashiki Y, Ishida N | 1996 Jan 15 | 8573067 |
| 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 |
| Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase. | Dufort I, Rheault P, Huang XF, Soucy P, Luu-The V | 1999 Feb | 9927279 |
| Expression and characterization of recombinant type 2 3 alpha-hydroxysteroid dehydrogenase (HSD) from human prostate: demonstration of bifunctional 3 alpha/17 beta-HSD activity and cellular distribution. | Lin HK, Jez JM, Schlegel BP, Peehl DM, Pachter JA, Penning TM | 1997 Dec | 9415401 |
| Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases. | Khanna M, Qin KN, Wang RW, Cheng KC | 1995 Aug 25 | 7650035 |
| Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3). | Penning TM, Burczynski ME, Jez JM, Lin HK, Ma H, Moore M, Ratnam K, Palackal N | 2001 Jan 22 | 11165022 |
| Crystal structures of mouse 17alpha-hydroxysteroid dehydrogenase (apoenzyme and enzyme-NADP(H) binary complex): identification of molecular determinants responsible for the unique 17alpha-reductive activity of this enzyme. | Faucher F, Pereira de Jésus-Tran K, Cantin L, Luu-The V, Labrie F, Breton R | 2006 Dec 8 | 17034817 |
| Comparison of crystal structures of human type 3 3alpha-hydroxysteroid dehydrogenase reveals an "induced-fit" mechanism and a conserved basic motif involved in the binding of androgen. | Couture JF, de Jésus-Tran KP, Roy AM, Cantin L, Côté PL, Legrand P, Luu-The V, Labrie F, Breton R | 2005 Jun | 15929998 |
| Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolution. | Nahoum V, Gangloff A, Legrand P, Zhu DW, Cantin L, Zhorov BS, Luu-The V, Labrie F, Breton R, Lin SX | 2001 Nov 9 | 11514561 |