| EC Tree |
| 1. Oxidoreductases |
| 1.3 Acting on the CH-CH group of donors |
| 1.3.99 With unknown physiological acceptors |
| ID: | 1.3.99.4 |
|---|---|
| Description: | 3-oxosteroid 1-dehydrogenase. |
| Cath: | 3.50.50.60; 3.90.700.10; |
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 1.3.99.4 |
| BRENDA Enzyme Link: | BRENDA 1.3.99.4 |
| KEGG Enzyme Link: | KEGG1.3.99.4 |
| BioCyc Enzyme Link: | BioCyc 1.3.99.4 |
| ExPASy Enzyme Link: | ExPASy1.3.99.4 |
| EC2PDB Enzyme Link: | EC2PDB 1.3.99.4 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.3.99.4 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.3.99.4 |
| IntEnz Enzyme Link: | IntEnz 1.3.99.4 |
| MEDLINE Enzyme Link: | MEDLINE 1.3.99.4 |
| RHEA:51056 | A + androst-4-ene-3,17-dione = AH2 + androsta-1,4-diene-3,17-dione |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[CH2;+0:3]-[*:4]>>[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| 3-Keto-5alpha-steroid Delta(1)-dehydrogenase from Rhodococcus erythropolis SQ1 and its orthologue in Mycobacterium tuberculosis H37Rv are highly specific enzymes that function in cholesterol catabolism. | Knol J, Bodewits K, Hessels GI, Dijkhuizen L, van der Geize R | 2008 Mar 1 | 18031290 |
| Identification and targeted disruption of the gene encoding the main 3-ketosteroid dehydrogenase in Mycobacterium smegmatis. | Brzostek A, Sliwiński T, Rumijowska-Galewicz A, Korycka-Machała M, Dziadek J | 2005 Jul | 16000729 |
| RHEA:51052 | 5alpha-androstan-3,17-dione + A = 5alpha-androst-1-ene-3,17-dione + AH2 |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[CH2;+0:3]-[*:4]>>[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Comamonas testosteroni 3-ketosteroid-delta 4(5 alpha)-dehydrogenase: gene and protein characterization. | Florin C, Köhler T, Grandguillot M, Plesiat P | 1996 Jun | 8655514 |
| RHEA:13329 | A + a 3-oxosteroid = a 3-oxo-Delta(1)-steroid + AH2 |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[CH2;+0:3]-[*:4]>>[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| 3-Keto-5alpha-steroid Delta(1)-dehydrogenase from Rhodococcus erythropolis SQ1 and its orthologue in Mycobacterium tuberculosis H37Rv are highly specific enzymes that function in cholesterol catabolism. | Knol J, Bodewits K, Hessels GI, Dijkhuizen L, van der Geize R | 2008 Mar 1 | 18031290 |
| Identification and targeted disruption of the gene encoding the main 3-ketosteroid dehydrogenase in Mycobacterium smegmatis. | Brzostek A, Sliwiński T, Rumijowska-Galewicz A, Korycka-Machała M, Dziadek J | 2005 Jul | 16000729 |
| Bacterial oxidation of steroids. II. Studies on the enzymatic mechanism of ring A dehydrogenation. | LEVY HR, TALALAY P | 1959 Aug | 13673006 |