KEGG   ENZYME: 1.14.99.15Help
Entry
EC 1.14.99.15               Enzyme                                 

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
BRITE hierarchy
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
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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

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