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Information on EC 1.14.99.15 - 4-methoxybenzoate monooxygenase (O-demethylating)
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1.14.99.15 4-methoxybenzoate monooxygenase (O-demethylating)IUBMB Comments
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.
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Word Map
- 1.14.99.15
- putida
- rhodopseudomonas
- palustris
- heme
-
benzoic
- ferredoxins
-
para-substituted
-
regioselectivity
-
o-demethylation
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2-naphthoic
- benzene
- putidaredoxin
- dioxygen
- 4-hydroxybenzoate
-
substrate-free
-
couplers
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
cyp199a2, cyp199a4, 4-methoxybenzoate monooxygenase, 4-methoxybenzoate monooxygenase (o-demethylating), 4-methoxybenzoate o-demethylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-methoxybenzoate 4-monooxygenase (O-demethylating)
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4-methoxybenzoate monooxygenase
4-methoxybenzoate O-demethylase
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CYP199A2
CYP199A4
oxygenase, 4-methoxybenzoate 4-mono- (O-demethylating)
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p-anisic O-demethylase
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piperonylate-4-O-demethylase
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RPA1871
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-methoxybenzoate + reduced acceptor + O2 = 4-hydroxybenzoate + formaldehyde + acceptor + H2O
4-methoxybenzoate + reduced acceptor + O2 = 4-hydroxybenzoate + formaldehyde + acceptor + H2O
a terminal oxygenase
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4-methoxybenzoate + reduced acceptor + O2 = 4-hydroxybenzoate + formaldehyde + acceptor + H2O
the bacterial enzyme is a two-component enzyme, consisting of an iron-sulfur flavoprotein (FMN), NADH-putidamonooxin-reductase and a ferredoxin-type, oxygen-activating protein, putidamonooxin
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4-methoxybenzoate + reduced acceptor + O2 = 4-hydroxybenzoate + formaldehyde + acceptor + H2O
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dealkylation
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N-demethylation
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O-demethylation
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oxidation
oxidative demethylation
redox reaction
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reduction
S-demethylation
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
4-methoxybenzoate,hydrogen-donor:oxygen oxidoreductase (O-demethylating)
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.
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CAS REGISTRY NUMBER
COMMENTARY
37256-78-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-naphthoic acid + AH2 + O2
5-hydroxy-2-naphthoic acid + A + H2O
only the wild-type enzyme hydroxylates 2-naphthoic acid at the C-7 and C-8 positions, whereas all of the active F185 mutants exhibit a preference for C-5 hydroxylation
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-
?
2-naphthoic acid + AH2 + O2
7-hydroxy-2-naphthoic acid + A + H2O
only the wild-type enzyme hydroxylates 2-naphthoic acid at the C-7 and C-8 positions, whereas all of the active F185 mutants exhibit a preference for C-5 hydroxylation
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-
?
2-naphthoic acid + AH2 + O2
8-hydroxy-2-naphthoic acid + A + H2O
only the wild-type enzyme hydroxylates 2-naphthoic acid at the C-7 and C-8 positions, whereas all of the active F185 mutants exhibit a preference for C-5 hydroxylation
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-
?
3,4-dimethoxybenzoate + NADH + O2
4-hydroxy-3-methoxybenzoate + NAD+ + H2O + formaldehyde
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-
-
-
?
3-nitro-4-methoxybenzoate + NADH + O2
3-nitro-4-hydroxybenzoate + NAD+ + H2O + formaldehyde
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-
-
-
?
3-nitro-4-methoxybenzoate + NADPH + O2
3-nitro-4-hydroxybenzoate + NADP+ + H2O + formaldehyde
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-
-
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r
3-phenyl-4-methoxybenzoate + NADH + O2
3-phenyl-4-hydroxybenzoate + NAD+ + H2O + formaldehyde
4-aminobenzoate + NADH + O2
4-amino-3-hydroxybenzoate + NAD+ + H2O
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-
-
-
?
4-chlorobenzaldehyde + NADH + O2
4-chlorobenzoate + NAD+ + H2O
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-
-
-
?
4-coumaric acid + AH2 + O2
caffeic acid + A + H2O
the F185L mutant exhibits 5.5times higher hydroxylation activity for 4-coumaric acid than the wild-type enzyme, good substrate of enzyme mutant F185L, low activity with enzyme mutant sF185V, F185I, F185G, and F185A, moderate activity with the wild-type enzyme and mutants F185Y, F185W, F185S, and F185T with 4-coumaric acid
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-
?
4-ethoxybenzoate + NADH + O2
4-hydroxybenzoate + acetaldehyde + NAD+ + H2O
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-
-
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?
4-ethylbenzoate + AH2 + O2
4-(1-hydroxyethyl)-benzoate + 4-vinylbenzoate + A + H2O
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a C-C bond dehydrogenation of an unbranched alkyl group, computational docking of 4-ethylbenzoate into the active site suggests that the substrate carboxylate oxygens interact with Ser97 and Ser247, and the beta-methyl group is located over the heme iron by Phe185, this binding orientation is consistent with the observed product profile of exclusive attack at the para substituent, overview
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?
4-Hydroxy-3-methoxybenzoate + NADH + O2
?
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vanillate, partial uncoupler
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?
4-methoxybenzoate + NADH + O2
4-hydroxybenzoate + NAD+ + H2O + formaldehyde
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?
4-methoxybenzoate + NADPH + O2
4-hydroxybenzoate + NADP+ + H2O + formaldehyde
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r
4-methoxybenzoate + reduced ferredoxin + O2
4-hydroxybenzoate + formaldehyde + ferredoxin + H2O
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?
4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
4-methoxybenzoate + reduced putidaredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized putidaredoxin + H2O
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very low activity with putidaredoxin
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?
4-methoxybenzoic acid + NADH + O2
4-hydroxybenzoate + formaldehyde + NAD+ + H2O
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?
4-methoxyphenylacetate + AH2 + O2
4-hydroxyphenylacetate + formaldehyde + A + H2O
low activity
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?
4-methoxyphenylboronic acid + AH2 + O2
4-hydroxyphenylboronic acid + formaldehyde + A + H2O
low activity
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?
4-vinylbenzoate + NADH + O2
4-glycylbenzoate + NAD+ + H2O
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external dioxygenase reaction by substrate induced modulation
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?
cinnamic acid + AH2 + O2
? + A + H2O
good substrate of enzyme mutant F185L, and F185G, low activity with enzyme mutants F185V, F185I, F185A F185S, and F185T, no activity with the wild-type enzyme and mutants F185Y and F185W with cinnamic acid
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?
N,N'-dimethyl-4-aminobenzoate + NADH + O2
4-aminobenzoate + NAD+ + H2O + formaldehyde
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?
N-methyl-4-aminobenzoate + NADH + O2
4-aminobenzoate + NAD+ + H2O + formaldehyde
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?
3,4-methylenedioxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O + formaldehyde
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piperonylate
protocatechuate
?
3,4-methylenedioxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O + formaldehyde
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piperonylate
protocatechuate
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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partial uncoupler
in the uncoupled part of the reaction, 3-hydroxybenzoate is not hydroxylated and H2O2 is a product, too
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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partial uncoupler
in the uncoupled part of the reaction, 3-hydroxybenzoate is not hydroxylated and H2O2 is a product, too
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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partial uncoupler
in the uncoupled part of the reaction, 3-hydroxybenzoate is not hydroxylated and H2O2 is a product, too
?
3-methoxybenzoate + NADH + O2
3-hydroxybenzoate + NAD+ + H2O + formaldehyde
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partial uncoupler
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?
3-methoxybenzoate + NADH + O2
3-hydroxybenzoate + NAD+ + H2O + formaldehyde
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partial uncoupler
in the uncoupled part of the reaction 3-methoxybenzoate is not hydroxylated, and H2O2 is a product, too
?
3-phenyl-4-methoxybenzoate + NADH + O2
3-phenyl-4-hydroxybenzoate + NAD+ + H2O + formaldehyde
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?
3-phenyl-4-methoxybenzoate + NADH + O2
3-phenyl-4-hydroxybenzoate + NAD+ + H2O + formaldehyde
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partial uncoupler
in the uncoupled part of the reaction 3-phenyl-4-methoxybenzoate is not hydroxylated and H2O2 is also a product of the reaction
?
4-ethylbenzoate + AH2 + O2
?
computational docking study
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?
4-ethylbenzoate + AH2 + O2
?
computational docking study
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?
4-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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?
4-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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?
4-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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?
4-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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?
4-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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?
4-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
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ring hydroxylation
?
4-methoxyacetophenone + AH2 + O2
4-hydroxyacetophenone + formaldehyde + A + H2O
low activity
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?
4-methoxyacetophenone + AH2 + O2
4-hydroxyacetophenone + formaldehyde + A + H2O
low activity
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?
4-methoxybenzaldehyde + AH2 + O2
4-hydroxybenzaldehyde + formaldehyde + A + H2O
low activity
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?
4-methoxybenzaldehyde + AH2 + O2
4-hydroxybenzaldehyde + formaldehyde + A + H2O
low activity
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?
4-methoxybenzamide + AH2 + O2
4-hydroxybenzamide + formaldehyde + A + H2O
low activity
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?
4-methoxybenzamide + AH2 + O2
4-hydroxybenzamide + formaldehyde + A + H2O
low activity
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?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
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-
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?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
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?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
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?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
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?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
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?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
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?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
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?
4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
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?
4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
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?
4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
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?
4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
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?
4-methylbenzoate + NADH + O2
4-carboxybenzylalcohol + NAD+ + H2O
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?
4-methylbenzoate + NADH + O2
4-carboxybenzylalcohol + NAD+ + H2O
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p-toluate, partial uncoupler
in the uncoupled part of the reaction, p-toluate is not hydroxylated and H2O2 is a product, too
?
4-methylbenzoate + NADH + O2
4-carboxybenzylalcohol + NAD+ + H2O
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p-toluate, partial uncoupler
in the uncoupled part of the reaction, p-toluate is not hydroxylated and H2O2 is a product, too
?
4-methylbenzoate + NADH + O2
4-carboxybenzylalcohol + NAD+ + H2O
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p-toluate, partial uncoupler
in the uncoupled part of the reaction, p-toluate is not hydroxylated and H2O2 is a product, too
?
additional information
?
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substrate binding induces a large type I spin-state shift, highest shifts are observed with benzoic acids and benzaldehydes containing a substitutent at the 4-position. Palustrisredoxin A is the natural electron transfer cofactor protein
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?
additional information
?
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CYP199A2 shows a strong preference for para-substituted benzoate over identically substituted ortho- and meta- benzoates, and para-substituted benzenes, benzyl alcohols and benzaldehydes, a cytochrome P450 enzyme, the substrate binding pocket is hydrophobic, with Ser97 and Ser247 being the only polar residues, substrate binding and substrate channeling mechanism and structure, overview
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?
additional information
?
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CYP199A2 is a heme monooxygenase that catalyses the oxidation of para-substituted benzoic acids, the hydroxylation and desaturation of 4-ethylbenzoic acid, and thus may play a role in lignin degradation
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?
additional information
?
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CYP199A2 activity is reconstituted by a class I electron transfer chain consisting of the associated [2Fe-2S] ferredoxin palustrisredoxin, Pux, and a flavoprotein palustrisredoxin reductase, PuR. Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system, overview
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?
additional information
?
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the enzyme performs regioselective oxidation of indole- and quinolinecarboxylic acids, it oxidizes 2-naphthoic acid and 4-ethylbenzoic acid, substrate specificity and regioselectivity of CYP199A2, overview. CYP199A2 does not exhibit any activity towards indole and indole-3-carboxylic acid, whereas this enzyme oxidizes indole-2-carboxylic acid, indole-5-carboxylic acid, and indole-6-carboxylic acid. Indole-2-carboxylic acid is converted to 5- and 6-hydroxyindole-2-carboxylic acids at a ratio of 59:41. In contrast, the indole-6-carboxylic acid oxidation generates only one product, 2-indolinone-6-carboxylic acid. The oxidation product of quinoline-6-carboxylic acid is 3-hydroxyquinoline-6-carboxylic acid
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?
additional information
?
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CYP199A2 oxidizes para-substituted benzoic acids with almost total NADH-to-product conversion with the highest activity being observed in the oxidative demethylation of 4-methoxybenzoate. Exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
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?
additional information
?
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CYP199A2 oxidizes para-substituted benzoic acids with almost total NADH-to-product conversion with the highest activity being observed in the oxidative demethylation of 4-methoxybenzoate. Exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
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?
additional information
?
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CYP199A2 oxidizes para-substituted benzoic acids with almost total NADH-to-product conversion with the highest activity being observed in the oxidative demethylation of 4-methoxybenzoate. Exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
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?
additional information
?
-
exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
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?
additional information
?
-
exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
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-
?
additional information
?
-
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exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
-
-
?
additional information
?
-
substrate specficities of wild-type and F185 mutants, overview. The enzyme exhibits oxidation activity for aromatic carboxylic acids, including 2-naphthoic acid, 4-ethylbenzoic acid, and indole-and quinolinecarboxylic acids. No activity of the wild-type enzyme with cinnamic acid
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-
?
additional information
?
-
no activity with 4-methoxybenzyl alcohol, 4-methylbenzenesulfonic acid, 4-methylbenzenesulfinic acid, 4-methoxynitrobenzene, 4-methoxyphenol, and 4-methoxybenzoic acid methyl ester
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-
?
additional information
?
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CYP199A2 is a heme monooxygenase that catalyses the oxidation of para-substituted benzoic acids, the hydroxylation and desaturation of 4-ethylbenzoic acid, and thus may play a role in lignin degradation
-
-
?
additional information
?
-
-
CYP199A2 activity is reconstituted by a class I electron transfer chain consisting of the associated [2Fe-2S] ferredoxin palustrisredoxin, Pux, and a flavoprotein palustrisredoxin reductase, PuR. Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system, overview
-
-
?
additional information
?
-
CYP199A2 oxidizes para-substituted benzoic acids with almost total NADH-to-product conversion with the highest activity being observed in the oxidative demethylation of 4-methoxybenzoate. Exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
-
-
?
additional information
?
-
exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
-
-
?
additional information
?
-
no activity with 4-methoxybenzyl alcohol, 4-methylbenzenesulfonic acid, 4-methylbenzenesulfinic acid, 4-methoxynitrobenzene, 4-methoxyphenol, and 4-methoxybenzoic acid methyl ester
-
-
?
additional information
?
-
-
no activity with 4-methoxybenzyl alcohol, 4-methylbenzenesulfonic acid, 4-methylbenzenesulfinic acid, 4-methoxynitrobenzene, 4-methoxyphenol, and 4-methoxybenzoic acid methyl ester
-
-
?
additional information
additional information
-
-
-
uncoupling substrates are not oxygenized, NAD+ and H2O2 being the only products of the reaction
?
additional information
additional information
-
-
overview: substrates that are not oxygenized while NADH-oxidation and O2-consumption are catalyzed, such as: benzoate, 3-chlorobenzoate, 4-chlorobenzoate, 2-hydroxybenzoate, 4-bromobenzoate, 2-aminobenzoate, 3-aminobenzoate, 4-trifluoromethylbenzoate, 4-tert-butylbenzoate
uncoupling substrates are not oxygenized, NAD+ and H2O2 being the only products of the reaction
?
additional information
additional information
-
-
overview: substrates that are not oxygenized while NADH-oxidation and O2-consumption are catalyzed, such as: benzoate, 3-chlorobenzoate, 4-chlorobenzoate, 2-hydroxybenzoate, 4-bromobenzoate, 2-aminobenzoate, 3-aminobenzoate, 4-trifluoromethylbenzoate, 4-tert-butylbenzoate
uncoupling substrates are not oxygenized, NAD+ and H2O2 being the only products of the reaction
?
additional information
additional information
-
-
overview: substrates that are not oxygenized while NADH-oxidation and O2-consumption are catalyzed, such as: benzoate, 3-chlorobenzoate, 4-chlorobenzoate, 2-hydroxybenzoate, 4-bromobenzoate, 2-aminobenzoate, 3-aminobenzoate, 4-trifluoromethylbenzoate, 4-tert-butylbenzoate
uncoupling substrates are not oxygenized, NAD+ and H2O2 being the only products of the reaction
?
additional information
additional information
-
-
overview: substrates that are not oxygenized while NADH-oxidation and O2-consumption are catalyzed, such as: benzoate, 3-chlorobenzoate, 4-chlorobenzoate, 2-hydroxybenzoate, 4-bromobenzoate, 2-aminobenzoate, 3-aminobenzoate, 4-trifluoromethylbenzoate, 4-tert-butylbenzoate
uncoupling substrates are not oxygenized, NAD+ and H2O2 being the only products of the reaction
?
additional information
additional information
-
-
overview: substrates that are not oxygenized while NADH-oxidation and O2-consumption are catalyzed, such as: benzoate, 3-chlorobenzoate, 4-chlorobenzoate, 2-hydroxybenzoate, 4-bromobenzoate, 2-aminobenzoate, 3-aminobenzoate, 4-trifluoromethylbenzoate, 4-tert-butylbenzoate
uncoupling substrates are not oxygenized, NAD+ and H2O2 being the only products of the reaction
?
additional information
additional information
-
-
overview: substrates being absolutely planar aromatic rings with a directly bound dissociable carboxy group are oxygenated under stoichiometric consumption of O2 and NADH
uncoupling substrates are not oxygenized, NAD+ and H2O2 being the only products of the reaction
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-methoxybenzoate + NADH + O2
4-hydroxybenzoate + NAD+ + H2O + formaldehyde
-
-
-
-
?
4-methoxybenzoate + reduced ferredoxin + O2
4-hydroxybenzoate + formaldehyde + ferredoxin + H2O
-
-
-
-
?
4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
-
?
4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
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4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
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additional information
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CYP199A2 activity is reconstituted by a class I electron transfer chain consisting of the associated [2Fe-2S] ferredoxin palustrisredoxin, Pux, and a flavoprotein palustrisredoxin reductase, PuR. Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system, overview
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additional information
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CYP199A2 activity is reconstituted by a class I electron transfer chain consisting of the associated [2Fe-2S] ferredoxin palustrisredoxin, Pux, and a flavoprotein palustrisredoxin reductase, PuR. Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
Phe at position 185 is situated directly above, and only 6.35 A from, the heme iron
palustrisredoxin
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CYP199A2 activity is reconstituted by a class I electron transfer chain consisting of the associated [2Fe-2S] ferredoxin palustrisredoxin, Pux, and a flavoprotein palustrisredoxin reductase, PuR. Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system, overview. Interaction of CYP199A2 with PuxB mutants, structure of PuxB A105R, and with ferredoxin, detailed overview. RPA3956, PuxB, from strain CGA009 is a vertebrate-type [2Fe-2S] ferredoxin with the characteristic cysteine in ferredoxins involved in Fe-S cluster biogenesis, PuxB also supports substrate oxidation by CYP199A2
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palustrisredoxin
i.e. Pux, RPA1872, with [2Fe-2S] cluster
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additional information
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PuxB, 2Fe-2S ferredoxin, palustrisredoxin B, supports substrate oxidation by CYP199A2
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additional information
the CYP enzyme surface closest to the heme (proximal surface) is the probable ferredoxin binding site
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additional information
the CYP enzyme surface closest to the heme (proximal surface) is the probable ferredoxin binding site
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additional information
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the CYP enzyme surface closest to the heme (proximal surface) is the probable ferredoxin binding site
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
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both enzyme components are iron-sulfur proteins
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-tert-Butylbenzoate
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competitive inhibitor of the O-demethylation of 3-nitro-4-methoxybenzoate, hinders O2-binding or O2-activation
Cl-
addition of chloride to the phosphate buffered samples weakens substrate binding, chloride binding site structure, overview; addition of chloride to the phosphate buffered samples weakens substrate binding, chloride binding site structure, overview
Oxidized putidamonooxin
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60% inhibition with 3-nitro-4-methoxybenzoate as substrate, fully reactivated by Fe2+ and sulfhydryl-reagents
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Putidamonooxin
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essential part of the enzyme system, O2-activating 2Fe-2S-protein, identified by EPR and Mössbauer spectroscopy
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE