EC number:1.14.13.166
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor |
| ID: | 1.14.13.166 |
|---|---|
| Description: | 4-nitrocatechol 4-monooxygenase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.13.166 |
| BRENDA Enzyme Link: | BRENDA 1.14.13.166 |
| KEGG Enzyme Link: | KEGG1.14.13.166 |
| BioCyc Enzyme Link: | BioCyc 1.14.13.166 |
| ExPASy Enzyme Link: | ExPASy1.14.13.166 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.13.166 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.13.166 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.13.166 |
| IntEnz Enzyme Link: | IntEnz 1.14.13.166 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.13.166 |
EC number:1.14.13.166
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:34311 | 4-nitrocatechol + NADH + O2 = 2-hydroxy-1,4-benzoquinone + H2O + NAD(+) + nitrite |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[*:9]=[N+;H0:10](-[*:11])-[c;H0;+0:12]1:[cH;+0:13]:[cH;+0:14]:[c;H0;+0:15](-[OH;+0:16]):[c;H0;+0:17](-[*:18]):[cH;+0:19]:1.[O;H0;+0:20]=[O;H0;+0:21]>>[*:18]-[C;H0;+0:17]1=[CH;+0:19]-[C;H0;+0:12](=[O;H0;+0:20])-[CH;+0:13]=[CH;+0:14]-[C;H0;+0:15]-1=[O;H0;+0:16].[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:9]=[N;H0;+0:10]-[*:11].[OH2;+0:21] |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A two-component monooxygenase catalyzes both the hydroxylation of p-nitrophenol and the oxidative release of nitrite from 4-nitrocatechol in Bacillus sphaericus JS905. | Kadiyala V, Spain JC | 1998 Jul | 9647818 |
| A novel p-nitrophenol degradation gene cluster from a gram-positive bacterium, Rhodococcus opacus SAO101. | Kitagawa W, Kimura N, Kamagata Y | 2004 Aug | 15262926 |
| RHEA:34307 | 4-nitrocatechol + NADPH + O2 = 2-hydroxy-1,4-benzoquinone + H2O + NADP(+) + nitrite |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[*:9]=[N+;H0:10](-[*:11])-[c;H0;+0:12]1:[cH;+0:13]:[cH;+0:14]:[c;H0;+0:15](-[OH;+0:16]):[c;H0;+0:17](-[*:18]):[cH;+0:19]:1.[O;H0;+0:20]=[O;H0;+0:21]>>[*:18]-[C;H0;+0:17]1=[CH;+0:19]-[C;H0;+0:12](=[O;H0;+0:20])-[CH;+0:13]=[CH;+0:14]-[C;H0;+0:15]-1=[O;H0;+0:16].[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:9]=[N;H0;+0:10]-[*:11].[OH2;+0:21] |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A two-component monooxygenase catalyzes both the hydroxylation of p-nitrophenol and the oxidative release of nitrite from 4-nitrocatechol in Bacillus sphaericus JS905. | Kadiyala V, Spain JC | 1998 Jul | 9647818 |
| A novel p-nitrophenol degradation gene cluster from a gram-positive bacterium, Rhodococcus opacus SAO101. | Kitagawa W, Kimura N, Kamagata Y | 2004 Aug | 15262926 |