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Information on EC 1.14.99.15 - 4-methoxybenzoate monooxygenase (O-demethylating) and Organism(s) Rhodopseudomonas palustris and UniProt Accession Q6N8N2
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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 taxonomic range for the selected organisms is: Rhodopseudomonas palustris
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
cyp199a2, cyp199a4, 4-methoxybenzoate monooxygenase, 4-methoxybenzoate o-demethylase, 4-methoxybenzoate monooxygenase (o-demethylating), 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-methoxybenzoate 4-monooxygenase (O-demethylating)
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4-methoxybenzoate O-demethylase
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
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oxidation
reduction
O-demethylation
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S-demethylation
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-
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N-demethylation
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dealkylation
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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.
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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-
?
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-ethylbenzoate + AH2 + O2
?
computational docking study
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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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-
-
?
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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-
?
4-chlorobenzaldehyde + NADH + O2
4-chlorobenzoate + NAD+ + H2O
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-
-
-
?
4-ethylbenzoate + AH2 + O2
4-(1-hydroxyethyl)-benzoate + 4-vinylbenzoate + A + H2O
-
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-methoxyacetophenone + AH2 + O2
4-hydroxyacetophenone + formaldehyde + A + H2O
low activity
-
-
?
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-methoxybenzoate + reduced ferredoxin + O2
4-hydroxybenzoate + formaldehyde + ferredoxin + H2O
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?
4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
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?
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
-
-
?
4-methoxyphenylboronic acid + AH2 + O2
4-hydroxyphenylboronic acid + formaldehyde + A + H2O
low activity
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
-
?
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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-
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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
?
-
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
?
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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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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
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?
additional information
?
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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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?
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 + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
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-
-
?
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
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-
-
-
?
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
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
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-
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
palustrisredoxin
i.e. Pux, RPA1872, with [2Fe-2S] cluster
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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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heme
Phe at position 185 is situated directly above, and only 6.35 A from, the heme iron
additional information
the CYP enzyme surface closest to the heme (proximal surface) is the probable ferredoxin binding site
-
additional information
the CYP enzyme surface closest to the heme (proximal surface) is the probable ferredoxin binding site
-
additional information
-
the CYP enzyme surface closest to the heme (proximal surface) is the probable ferredoxin binding site
-
additional information
-
PuxB, 2Fe-2S ferredoxin, palustrisredoxin B, supports substrate oxidation by CYP199A2
-
additional information
the CYP enzyme surface closest to the heme (proximal surface) is the probable ferredoxin binding site
-
additional information
the CYP enzyme surface closest to the heme (proximal surface) is the probable ferredoxin binding site
-
additional information
-
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+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cl-
addition of chloride to the phosphate buffered samples weakens substrate binding, chloride binding site structure, overview
Cl-
addition of chloride to the phosphate buffered samples weakens substrate binding, chloride binding site structure, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
steady-state kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
30
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the superfamily of heme-dependent cytochrome P450 monooxygenases
physiological function
CYP199A2 is involved in the degradation of ligninolic compounds by the organism
evolution
the enzyme belongs to the superfamily of heme-dependent cytochrome P450 monooxygenases
physiological function
-
CYP199A2 catalyzes the oxidative demethylation of 4-methoxybenzoic acid and the hydroxylation and desaturation of 4-ethylbenzoic acid, and thus may play a role in lignin degradation by this organism
additional information
additional information
substrate-enzyme structure, the enzyme possesses a clearly defined substrate access channel that is formed between the BC loop and the G and G' helices, overview. The 4-methoxybenzoate-bound enzyme has a closed conformation, in contrast to the substrate-free form of CYP199A2 where an obvious substrate access channel is observed. The switch from an open to a closed conformation arises from pronounced residue side-chain movements and alterations of ion pair and hydrogen bonding interactions at the entrance of the access channel. A chloride ion bound just inside the protein surface caps the entrance to the active site and protects the substrate and the heme from the external solvent. The substrate is held in place via hydrophobic and hydrogen bond interactions. The methoxy group is located over the heme iron, accounting for the high activity and selectivity of the enzyme for oxidative demethylation of 4-methoxybenzoate
additional information
substrate-enzyme structure, the enzyme possesses a clearly defined substrate access channel that is formed between the BC loop and the G and G' helices, overview. The 4-methoxybenzoate-bound enzyme has a closed conformation, in contrast to the substrate-free form of CYP199A2 where an obvious substrate access channel is observed. The switch from an open to a closed conformation arises from pronounced residue side-chain movements and alterations of ion pair and hydrogen bonding interactions at the entrance of the access channel. A chloride ion bound just inside the protein surface caps the entrance to the active site and protects the substrate and the heme from the external solvent. The substrate is held in place via hydrophobic and hydrogen bond interactions. The methoxy group is located over the heme iron, accounting for the high activity and selectivity of the enzyme for oxidative demethylation of 4-methoxybenzoate
additional information
-
substrate-enzyme structure, the enzyme possesses a clearly defined substrate access channel that is formed between the BC loop and the G and G' helices, overview. The 4-methoxybenzoate-bound enzyme has a closed conformation, in contrast to the substrate-free form of CYP199A2 where an obvious substrate access channel is observed. The switch from an open to a closed conformation arises from pronounced residue side-chain movements and alterations of ion pair and hydrogen bonding interactions at the entrance of the access channel. A chloride ion bound just inside the protein surface caps the entrance to the active site and protects the substrate and the heme from the external solvent. The substrate is held in place via hydrophobic and hydrogen bond interactions. The methoxy group is located over the heme iron, accounting for the high activity and selectivity of the enzyme for oxidative demethylation of 4-methoxybenzoate
additional information
the 4-methoxybenzoate-bound enzyme has a closed conformation. The substrate is held in place via hydrophobic and hydrogen bond interactions. The methoxy group is located over the heme iron, accounting for the high activity and selectivity of the enzyme for oxidative demethylation of 4-methoxybenzoate, involvement of hydrophobic (Phe185) and hydrophilic (Arg92, Ser95 and Arg243) amino acid residues in the binding of para-substituted benzoates
additional information
the 4-methoxybenzoate-bound enzyme has a closed conformation. The substrate is held in place via hydrophobic and hydrogen bond interactions. The methoxy group is located over the heme iron, accounting for the high activity and selectivity of the enzyme for oxidative demethylation of 4-methoxybenzoate, involvement of hydrophobic (Phe185) and hydrophilic (Arg92, Ser95 and Arg243) amino acid residues in the binding of para-substituted benzoates
additional information
-
the 4-methoxybenzoate-bound enzyme has a closed conformation. The substrate is held in place via hydrophobic and hydrogen bond interactions. The methoxy group is located over the heme iron, accounting for the high activity and selectivity of the enzyme for oxidative demethylation of 4-methoxybenzoate, involvement of hydrophobic (Phe185) and hydrophilic (Arg92, Ser95 and Arg243) amino acid residues in the binding of para-substituted benzoates
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
site-directed mutagenesis, the mutant shows activity with cinnamic acid in contrast to the wild-type enzyme
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
site-directed mutagenesis, the mutant shows activity with cinnamic acid in contrast 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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) by two different steps of anion exchange chromatography, followed by gel filtration
recombinant His-tagged enzyme from Escherichia coli BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by two different steps of anion exchange chromatography, followed by gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant CYP199A2 in Escherichia coli strain BL21(DE3)
CYP199A2 gene RPA1871, coexpression with palustris redoxin gene from Rhodopseudomonas palustris and putidaredoxin reductase gene from Pseudomonas putida to provide the redox partners of CYP199A2 in Escherichia coli
-
overexpression of the His-tagged enzyme in Escherichia coli BL21(DE3)
-
wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
CYP199A2 may be a valuable biocatalyst for the regioselective oxidation of various aromatic carboxylic acids
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bell, S.G.; Hoskins, N.; Xu, F.; Caprotti, D.; Rao, Z.; Wong, L.L.
Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris
Biochem. Biophys. Res. Commun.
342
191-196
2006
Rhodopseudomonas palustris
Bell, S.G.; Xu, F.; Forward, I.; Bartlam, M.; Rao, Z.; Wong, L.L.
Crystal structure of CYP199A2, a para-substituted benzoic acid oxidizing cytochrome P450 from Rhodopseudomonas palustris
J. Mol. Biol.
383
561-574
2008
Rhodopseudomonas palustris
Bell, S.G.; Xu, F.; Johnson, E.O.; Forward, I.M.; Bartlam, M.; Rao, Z.; Wong, L.L.
Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system from Rhodopseudomonas palustris
J. Biol. Inorg. Chem.
15
315-328
2009
Rhodopseudomonas palustris, Rhodopseudomonas palustris CGA009
Furuya, T.; Kino, K.
Regioselective oxidation of indole- and quinolinecarboxylic acids by cytochrome P450 CYP199A2
Appl. Microbiol. Biotechnol.
85
1861-1868
2010
Rhodopseudomonas palustris
Furuya, T.; Arai, Y.; Kino, K.
Biotechnological production of caffeic acid by bacterial cytochrome P450 CYP199A2
Appl. Environ. Microbiol.
78
6087-6094
2012
Rhodopseudomonas palustris (Q6N8N2)
Bell, S.; Yang, W.; Tan, A.; Zhou, R.; Johnson, E.; Zhang, A.; Zhou, W.; Rao, Z.; Wong, L.
The crystal structures of 4-methoxybenzoate bound CYP199A2 and CYP199A4: Structural changes on substrate binding and the identification of an anion binding site
Dalton Trans.
41
8703-8714
2012
Rhodopseudomonas palustris (Q2IU02), Rhodopseudomonas palustris (Q6N8N2), Rhodopseudomonas palustris, Rhodopseudomonas palustris CGA009 (Q6N8N2), Rhodopseudomonas palustris HaA2 (Q2IU02)
Coleman, T.; Chao, R.R.; De Voss, J.J.; Bell, S.G.
The importance of the benzoic acid carboxylate moiety for substrate recognition by CYP199A4 from Rhodopseudomonas palustris HaA2
Biochim. Biophys. Acta
1864
667-675
2016
Rhodopseudomonas palustris (Q2IU02), Rhodopseudomonas palustris HaA2 (Q2IU02), Rhodopseudomonas palustris HaA2
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Release 2023.1 (January 2023)
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