Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.14.99.15: 4-methoxybenzoate monooxygenase (O-demethylating)

This is an abbreviated version!
For detailed information about 4-methoxybenzoate monooxygenase (O-demethylating), go to the full flat file.

Word Map on EC 1.14.99.15

Reaction

4-Methoxybenzoate
+
reduced acceptor
+
O2
=
4-hydroxybenzoate
+
formaldehyde
+
acceptor
+
H2O

Synonyms

4-methoxybenzoate 4-monooxygenase (O-demethylating), 4-methoxybenzoate monooxygenase, 4-methoxybenzoate O-demethylase, CYP199A2, CYP199A4, cytochrome P450 199A2, oxygenase, 4-methoxybenzoate 4-mono- (O-demethylating), p-anisic O-demethylase, piperonylate-4-O-demethylase, RPA1871

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.99 Miscellaneous
                1.14.99.15 4-methoxybenzoate monooxygenase (O-demethylating)

Crystallization

Crystallization on EC 1.14.99.15 - 4-methoxybenzoate monooxygenase (O-demethylating)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme CYP199A2 bound to substrate 4-methoxybenzoate, X-ray diffraction structure determination and analysis at 1.8 A resolution
enzyme CYP199A4 free and bound to substrate 4-methoxybenzoate, hanging drop vapour diffusion method, for the free enzyme: mixing of 0.001 ml of protein solution containing 50 mg/ml protein in 20 mM HEPES, pH 7.4, 150 mM KCl, 1 mM DTT, with 0.001 ml of reservoir solution containing 0.1 M Bis-Tris, pH 5.5, 1.45-1.5 M ammonium sulfate, and 0.1 M sodium chloride, and equilibration against 0.2 ml of reservoir solution, 20°C, 1 week, for the substrate-bound enzyme: mixing of 0.001 ml of protein solution containing 40 mg/ml protein in 20 mM HEPES, pH 7.4, 150 mM KCl, and 10 mM 2-mercaptoethanol and saturated with 4-methoxybenzoate, with 0.001 ml of reservoir solution containing 0.1 M Bis-Tris, pH 5.5, 1.45 M ammonium sulfate, and 0.1 M sodium chloride, and equilibration against 0.2 ml of reservoir solution, 20°C, 2 weeks, X-ray diffraction structure determination and analysis at 2.6 A and 2.0 A resolution, respectively
purified recombinant CYP199A2, 16 ºC, the hanging drop vapor diffusion method under aerobic conditions, 0.0015 ml of protein solution is mixed with 0.0015 ml of reservoir solution, addition of 200 ml reservoir solution, containing 15% PEG 4000, 100 mM sodium citrate pH 5.6, 20% isopropanol with 4% v/v t-butanol, 1 week, X-ray diffraction structure deternnation and analysis at 2.0 A resolution
-