4-methoxybenzoate monooxygenase (O-demethylating)

4-methoxybenzoate monooxygenase (O-demethylating)
Identifiers
EC number	1.14.99.15
CAS number	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 / EGO
Search PMC articles PubMed articles NCBI proteins

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 $\rightleftharpoons$ 4-hydroxybenzoate + formaldehyde + A + H₂O

The 3 substrates of this enzyme are 4-methoxybenzoate, an electron acceptor AH₂, and O₂, whereas its 4 products are 4-hydroxybenzoate, formaldehyde, the reduction product 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.
• 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.