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 |
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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: | |
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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 |
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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 |