| Entry |
|
| Name |
4-methoxybenzoate monooxygenase (O-demethylating);
4-methoxybenzoate 4-monooxygenase (O-demethylating);
4-methoxybenzoate O-demethylase;
p-anisic O-demethylase;
piperonylate-4-O-demethylase |
| Class |
Oxidoreductases;
Acting on paired donors, with O2 as oxidant and incorporation or
reduction of oxygen. The oxygen incorporated need not be derived
from O2;
Miscellaneous
 |
| Sysname |
4-methoxybenzoate,hydrogen-donor:oxygen oxidoreductase
(O-demethylating) |
| Reaction(IUBMB) |
4-methoxybenzoate + AH2 + O2 = 4-hydroxybenzoate + formaldehyde + A
+ H2O [RN:R01306] |
| Reaction(KEGG) |
R01306
 |
| Substrate |
4-methoxybenzoate [CPD:C02519];
AH2 [CPD:C00030];
O2 [CPD:C00007] |
| Product |
4-hydroxybenzoate [CPD:C00156];
formaldehyde [CPD:C00067];
A [CPD:C00028];
H2O [CPD:C00001] |
| Comment |
The bacterial enzyme consists of a ferredoxin-type protein and an
iron-sulfur flavoprotein (FMN). Also acts on 4-ethoxybenzoate,
N-methyl-4-aminobenzoate and toluate. The fungal enzyme acts best on
veratrate. |
| Pathway |
PATH: ec00623 2,4-Dichlorobenzoate degradation |
Reference Authors Title
Journal Organism
|
1 [PMID:188654]
Bernhardt FH, Nastainczyk W, Seydewitz V.
Kinetic studies on a 4-methoxybenzoate O-demethylase from
Pseudomonas putida.
Eur. J. Biochem. 72 (1977) 107-15.
Pseudomonas putida |
Reference Authors Title
Journal Organism
|
2 [PMID:25369]
Paszczynski A, Trojanowski J.
An affinity-column procedure for the purification of veratrate
O-demethylase from fungi.
Microbios. 18 (1977) 111-21.
Chaetomium piluliferum, Xerocomus badius |
Reference Authors Title
Journal Organism
|
3 [PMID:6273164]
Twilfer H, Bernhardt FH, Gersonde K.
An electron-spin-resonance study on the redox-active centers of the
4-methoxybenzoate monooxygenase from Pseudomonas putida.
Eur. J. Biochem. 119 (1981) 595-602.
Pseudomonas putida |
| Other DBs |
ExplorEnz - The Enzyme Database: 1.14.99.15
IUBMB Enzyme Nomenclature: 1.14.99.15
ExPASy - ENZYME nomenclature database: 1.14.99.15
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.99.15
BRENDA, the Enzyme Database: 1.14.99.15
CAS: 37256-78-3 |