| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.99 Miscellaneous |
| ID: | 1.14.99.15 |
|---|---|
| Description: | 4-methoxybenzoate monooxygenase (O-demethylating). |
| Alternative Name: |
4-methoxybenzoate O-demethylase. |
| Cath: | 1.10.630.10; |
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 1.14.99.15 |
| BRENDA Enzyme Link: | BRENDA 1.14.99.15 |
| KEGG Enzyme Link: | KEGG1.14.99.15 |
| BioCyc Enzyme Link: | BioCyc 1.14.99.15 |
| ExPASy Enzyme Link: | ExPASy1.14.99.15 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.99.15 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.99.15 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.99.15 |
| IntEnz Enzyme Link: | IntEnz 1.14.99.15 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.99.15 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:18613 | 4-methoxybenzoate + AH2 + O2 = 4-hydroxybenzoate + A + formaldehyde + H2O |
| RULE(radius=1) | [*:1]-[O;H0;+0:2]-[CH3;+0:3].[O;H0;+0:4]=[O;H0;+0:5]>>[*:1]-[OH;+0:2].[CH2;+0:3]=[O;H0;+0:4].[OH2;+0:5] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| An electron-spin-resonance study on the redox-active centers of the 4-methoxybenzoate monooxygenase from Pseudomonas putida. | Twilfer H, Bernhardt FH, Gersonde K | 1981 Oct | 6273164 |
| An affinity-column procedure for the purification of veratrate O-demethylase from fungi. | Paszczyński A, Trojanowski J | 1977 | 25369 |
| Kinetic studies on a 4-methoxybenzoate O-demethylase from Pseudomonas putida. | Bernhardt FH, Nastainczyk W, Seydewitz V | 1977 Jan 3 | 188654 |