EC number:1.14.14.20
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor |
| ID: | 1.14.14.20 |
|---|---|
| Description: | Phenol 2-monooxygenase (FADH(2)). |
| Cath: | 3.30.9.10; 3.50.50.60; 3.90.56.10; 2.30.110.10; 3.40.30.20; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.14.20 |
| BRENDA Enzyme Link: | BRENDA 1.14.14.20 |
| KEGG Enzyme Link: | KEGG1.14.14.20 |
| BioCyc Enzyme Link: | BioCyc 1.14.14.20 |
| ExPASy Enzyme Link: | ExPASy1.14.14.20 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.14.20 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.14.20 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.14.20 |
| IntEnz Enzyme Link: | IntEnz 1.14.14.20 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.14.20 |
EC number:1.14.14.20
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:49280 | FADH2 + O2 + phenol = catechol + FAD + H(+) + H2O |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]1-[*:3]:[*:4]-[NH;+0:5]-[c;H0;+0:6](:[*:7]):[c;H0;+0:8]-1:[nH;+0:9]:[*:10].[*:11]:[cH;+0:12]:[*:13].[O;H0;+0:14]=[O;H0;+0:15]>>[*:1]-[n;H0;+0:2]1:[*:3]:[*:4]:[n;H0;+0:5]:[c;H0;+0:6](:[*:7])-[c;H0;+0:8]:1:[n;H0;+0:9]:[*:10].[*:11]:[c;H0;+0:12](:[*:13])-[OH;+0:14].[OH2;+0:15] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Cloning, purification and characterization of two components of phenol hydroxylase from Rhodococcus erythropolis UPV-1. | Saa L, Jaureguibeitia A, Largo E, Llama MJ, Serra JL | 2010 Mar | 19787347 |
| Structural studies on flavin reductase PheA2 reveal binding of NAD in an unusual folded conformation and support novel mechanism of action. | van den Heuvel RH, Westphal AH, Heck AJ, Walsh MA, Rovida S, van Berkel WJ, Mattevi A | 2004 Mar 26 | 14703520 |
| Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD. | Kirchner U, Westphal AH, Müller R, van Berkel WJ | 2003 Nov 28 | 12968028 |