EC number:1.17.1.5
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.17 Acting on CH or CH2 groups |
| 1.17.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.17.1.5 |
|---|---|
| Description: | Nicotinate dehydrogenase. |
| Alternative Name: |
Nicotinic acid hydroxylase. Nicotinate hydroxylase. |
| Cath: | 1.10.1040.10; 1.10.150.120; 3.20.20.140; 3.30.365.10; 3.30.390.50; 3.30.465.10; 3.40.50.720; 2.30.40.10; 3.40.50.12340; 3.10.20.30; |
3D structure
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.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 1.17.1.5 |
| BRENDA Enzyme Link: | BRENDA 1.17.1.5 |
| KEGG Enzyme Link: | KEGG1.17.1.5 |
| BioCyc Enzyme Link: | BioCyc 1.17.1.5 |
| ExPASy Enzyme Link: | ExPASy1.17.1.5 |
| EC2PDB Enzyme Link: | EC2PDB 1.17.1.5 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.17.1.5 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.17.1.5 |
| IntEnz Enzyme Link: | IntEnz 1.17.1.5 |
| MEDLINE Enzyme Link: | MEDLINE 1.17.1.5 |
| RHEA:12236 | H2O + NADP(+) + nicotinate = 6-hydroxynicotinate + H(+) + NADPH |
| 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]:[cH;+0:10]:[*:11].[OH2;+0:12]>>[*: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](:[*:11])-[OH;+0:12] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Properties of the selenium- and molybdenum-containing nicotinic acid hydroxylase from Clostridium barkeri. | Gladyshev VN, Khangulov SV, Stadtman TC | 1996 Jan 9 | 8555176 |
| Nicotinic acid hydroxylase from Clostridium barkeri: electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme. | Gladyshev VN, Khangulov SV, Stadtman TC | 1994 Jan 4 | 8278371 |