4-methoxybenzoate monooxygenase (O-demethylating)
| 4-methoxybenzoate monooxygenase (O-demethylating) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.99.15 | ||||||||
| CAS no. | 37256-78-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a 4-methoxybenzoate monooxygenase (O-demethylating) (EC 1.14.99.15) is an enzyme that catalyzes the chemical reaction
- 4-methoxybenzoate + AH2 + O2 4-hydroxybenzoate + formaldehyde + A + H2O
The 3 substrates of this enzyme are 4-methoxybenzoate, AH2, and O2, whereas its 4 products are 4-hydroxybenzoate, formaldehyde, A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is 4-methoxybenzoate,hydrogen-donor:oxygen oxidoreductase (O-demethylating). Other names in common use include 4-methoxybenzoate 4-monooxygenase (O-demethylating), 4-methoxybenzoate O-demethylase, p-anisic O-demethylase, and piperonylate-4-O-demethylase. This enzyme participates in 2,4-dichlorobenzoate degradation.
References
- Bernhardt FH, Nastainczyk W, Seydewitz V (1977). "Kinetic studies on a 4-methoxybenzoate O-demethylase from Pseudomonas putida". Eur. J. Biochem. 72 (1): 107–15. doi:10.1111/j.1432-1033.1977.tb11230.x. PMID 188654.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - Paszczynski A, Trojanowski J (1977). "An affinity-column procedure for the purification of veratrate O-demethylase from fungi". Microbios. 18 (72): 111–21. PMID 25369.
- Twilfer H, Bernhardt FH, Gersonde K (1981). "An electron-spin-resonance study on the redox-active centers of the 4-methoxybenzoate monooxygenase from Pseudomonas putida". Eur. J. Biochem. 119 (3): 595–602. doi:10.1111/j.1432-1033.1981.tb05649.x. PMID 6273164.
{{cite journal}}: CS1 maint: multiple names: authors list (link)