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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)

Engineering

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

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F185A
site-directed mutagenesis, the mutant shows activity with cinnamic acid in contrast to the wild-type enzyme
F185G
site-directed mutagenesis, the mutant shows activity with cinnamic acid in contrast to the wild-type enzyme
F185I
F185L
site-directed mutagenesis, the mutant shows activity with cinnamic acid in contrast to the wild-type enzyme, the F185L mutant exhibits 5.5times higher hydroxylation activity for 4-coumaric acid than the wild-type enzyme
F185S
site-directed mutagenesis, the mutant shows reduced activity with 2-naphthoic acid compared to the wild-type enzyme
F185T
site-directed mutagenesis, the mutant shows reduced activity with 2-naphthoic acid compared to the wild-type enzyme
F185V
F185W
site-directed mutagenesis, inactive mutant
F185Y
site-directed mutagenesis, inactive mutant
R243T
site-directed mutagenesis, the mutation reduces the spin state shift from low- to high-spin on the addition of 4-methoxybenzoate by about 25% compared to the wild-type enzyme, the mutant shows reduced NADH consumption and product formation
R92E
site-directed mutagenesis, the spin state shift is similar to the wild-type enzyme, but the mutant shows 3fold higher KD for the substrate, NADH consumption is reduced 9fold compared to the wild-type enzyme
S95V
site-directed mutagenesis, the mutation abolishes the spin state shift from low- to high-spin on the addition of 4-methoxybenzoate and results in a 99% drop in the NADH consumption rate comared to the wild-type enzyme
F185I
-
site-directed mutagenesis, the mutation reduces the spin state shift from low- to high-spin on the addition of 4-methoxybenzoate by about 25% compared to the wild-type enzyme, the mutant shows reduced NADH consumption and product formation
-
F185V
-
site-directed mutagenesis, the mutation reduces the spin state shift from low- to high-spin on the addition of 4-methoxybenzoate by about 35% compared to the wild-type enzyme, the mutant shows reduced NADH consumption and product formation
-
R243T
-
site-directed mutagenesis, the mutation reduces the spin state shift from low- to high-spin on the addition of 4-methoxybenzoate by about 25% compared to the wild-type enzyme, the mutant shows reduced NADH consumption and product formation
-
R92E
-
site-directed mutagenesis, the spin state shift is similar to the wild-type enzyme, but the mutant shows 3fold higher KD for the substrate, NADH consumption is reduced 9fold compared to the wild-type enzyme
-
S95V
-
site-directed mutagenesis, the mutation abolishes the spin state shift from low- to high-spin on the addition of 4-methoxybenzoate and results in a 99% drop in the NADH consumption rate comared to the wild-type enzyme
-
additional information
substrate specficities of wild-type and F185 mutants, overview