EC number:1.3.1.14
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.3 Acting on the CH-CH group of donors |
| 1.3.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.3.1.14 |
|---|---|
| Description: | Dihydroorotate dehydrogenase (NAD(+)). |
| Alternative Name: |
Orotate reductase (NADH). Orotate reductase (NADH(2)). Dihydroorotate oxidase. DHOdehase. DHODase. DHOD. |
| Cath: | 3.20.20.70; 2.30.26.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.3.1.14 |
| BRENDA Enzyme Link: | BRENDA 1.3.1.14 |
| KEGG Enzyme Link: | KEGG1.3.1.14 |
| BioCyc Enzyme Link: | BioCyc 1.3.1.14 |
| ExPASy Enzyme Link: | ExPASy1.3.1.14 |
| EC2PDB Enzyme Link: | EC2PDB 1.3.1.14 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.3.1.14 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.3.1.14 |
| IntEnz Enzyme Link: | IntEnz 1.3.1.14 |
| MEDLINE Enzyme Link: | MEDLINE 1.3.1.14 |
| RHEA:13513 | (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate |
| RULE(radius=1) | [*:1]-[n+;H0:2]1:[cH;+0:3]:[cH;+0:4]:[cH;+0:5]:[c;H0;+0:6](-[*:7]):[cH;+0:8]:1.[*:9]=[C;H0;+0:10]1-[NH;+0:11]-[C;H0;+0:12](=[*:13])-[CH2;+0:14]-[CH;+0:15](-[*:16])-[NH;+0:17]-1>>[*:1]-[N;H0;+0:2]1-[CH;+0:3]=[CH;+0:4]-[CH2;+0:5]-[C;H0;+0:6](-[*:7])=[CH;+0:8]-1.[*:9]=[c;H0;+0:10]1:[nH;+0:11]:[c;H0;+0:12](=[*:13]):[cH;+0:14]:[c;H0;+0:15](-[*:16]):[nH;+0:17]:1 |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The B form of dihydroorotate dehydrogenase from Lactococcus lactis consists of two different subunits, encoded by the pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers. | Nielsen FS, Andersen PS, Jensen KF | 1996 Nov 15 | 8910599 |
| Two different dihydroorotate dehydrogenases in Lactococcus lactis. | Andersen PS, Jansen PJ, Hammer K | 1994 Jul | 8021180 |
| Stereospecificity of the dihydroorotate-dehydrogenase reaction. | Blattmann P, Rétey J | 1972 Oct 17 | 4343805 |
| Thermodynamic basis of electron transfer in dihydroorotate dehydrogenase B from Lactococcus lactis: analysis by potentiometry, EPR spectroscopy, and ENDOR spectroscopy. | Mohsen AW, Rigby SE, Jensen KF, Munro AW, Scrutton NS | 2004 Jun 1 | 15157083 |
| Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster. | Rowland P, Nørager S, Jensen KF, Larsen S | 2000 Dec 15 | 11188687 |
| Dihydroorotate dehydrogenase from Clostridium oroticum is a class 1B enzyme and utilizes a concerted mechanism of catalysis. | Argyrou A, Washabaugh MW, Pickart CM | 2000 Aug 29 | 10956027 |
| Biochemical characterization of the heteromeric Bacillus subtilis dihydroorotate dehydrogenase and its isolated subunits. | Kahler AE, Nielsen FS, Switzer RL | 1999 Nov 15 | 10545205 |
| Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism. | Marcinkeviciene J, Tinney LM, Wang KH, Rogers MJ, Copeland RA | 1999 Oct 5 | 10529184 |