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Inenzymology, a4-methoxybenzoate monooxygenase (O-demethylating) (EC1.14.99.15) is anenzyme thatcatalyzes thechemical reaction
| 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 PDBPDBePDBsum | ||||||||
| Gene Ontology | AmiGO /QuickGO | ||||||||
| |||||||||
- 4-methoxybenzoate + AH2 + O2 4-hydroxybenzoate + formaldehyde + A + H2O
The 3substrates of this enzyme are4-methoxybenzoate, anelectron acceptor AH2, andO2, whereas its 4products are4-hydroxybenzoate,formaldehyde, the reduction product A, andH2O.
This enzyme belongs to the family ofoxidoreductases, 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. Thesystematic name of this enzyme class is4-methoxybenzoate,hydrogen-donor:oxygen oxidoreductase (O-demethylating). Other names in common use include4-methoxybenzoate 4-monooxygenase (O-demethylating),4-methoxybenzoate O-demethylase,p-anisic O-demethylase, andpiperonylate-4-O-demethylase. This enzyme participates in2,4-dichlorobenzoate degradation.
References
edit- 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.
- 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.
