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

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The expected taxonomic range for this enzyme is: Proteobacteria

EC NUMBER
COMMENTARY hide
1.14.99.15
-
RECOMMENDED NAME
GeneOntology No.
4-methoxybenzoate monooxygenase (O-demethylating)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-methoxybenzoate + AH2 + O2 = 4-hydroxybenzoate + formaldehyde + A + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dealkylation
-
-
-
-
N-demethylation
-
-
-
-
O-demethylation
-
-
-
-
oxidation
oxidative demethylation
redox reaction
-
-
-
-
reduction
S-demethylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Benzoate degradation
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
37256-78-3
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-naphthoic acid + AH2 + O2
5-hydroxy-2-naphthoic acid + A + H2O
show the reaction diagram
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
-
-
?
2-naphthoic acid + AH2 + O2
7-hydroxy-2-naphthoic acid + A + H2O
show the reaction diagram
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
-
-
?
2-naphthoic acid + AH2 + O2
8-hydroxy-2-naphthoic acid + A + H2O
show the reaction diagram
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
-
-
?
3,4-dimethoxybenzoate + NADH + O2
4-hydroxy-3-methoxybenzoate + NAD+ + H2O + formaldehyde
show the reaction diagram
-
-
-
-
?
3,4-methylenedioxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O + formaldehyde
show the reaction diagram
3-chlorobenzoic acid + NADH + O2
? + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
show the reaction diagram
3-methoxybenzoate + NADH + O2
3-hydroxybenzoate + NAD+ + H2O + formaldehyde
show the reaction diagram
3-nitro-4-methoxybenzoate + NADH + O2
3-nitro-4-hydroxybenzoate + NAD+ + H2O + formaldehyde
show the reaction diagram
-
-
-
-
?
3-phenyl-4-methoxybenzoate + NADH + O2
3-phenyl-4-hydroxybenzoate + NAD+ + H2O + formaldehyde
show the reaction diagram
4-aminobenzoate + NADH + O2
4-amino-3-hydroxybenzoate + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
4-chlorobenzaldehyde + NADH + O2
4-chlorobenzoate + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
4-chlorobenzoic acid + NADH + O2
? + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
4-coumaric acid + AH2 + O2
caffeic acid + A + H2O
show the reaction diagram
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
-
-
?
4-ethoxybenzoate + NADH + O2
4-hydroxybenzoate + acetaldehyde + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
4-ethylbenzoate + AH2 + O2
4-(1-hydroxyethyl)-benzoate + 4-vinylbenzoate + A + H2O
show the reaction diagram
-
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-ethylbenzoate + AH2 + O2
?
show the reaction diagram
4-ethylbenzoic acid + NADH + O2
? + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
4-Hydroxy-3-methoxybenzoate + NADH + O2
?
show the reaction diagram
-
vanillate, partial uncoupler
-
-
?
4-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
show the reaction diagram
4-isopropylbenzoic acid + NADH + O2
? + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
show the reaction diagram
4-methoxybenzoate + NADH + O2
4-hydroxybenzoate + NAD+ + H2O + formaldehyde
show the reaction diagram
-
-
-
-
?
4-methoxybenzoate + reduced ferredoxin + O2
4-hydroxybenzoate + formaldehyde + ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
show the reaction diagram
4-methoxybenzoate + reduced putidaredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized putidaredoxin + H2O
show the reaction diagram
-
very low activity with putidaredoxin
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-
?
4-methoxybenzoic acid + NADH + O2
4-hydroxybenzoate + formaldehyde + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
4-methylbenzoate + NADH + O2
4-carboxybenzylalcohol + NAD+ + H2O
show the reaction diagram
4-methylbenzoic acid + NADH + O2
? + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
4-methylmercaptobenzoate + NADH + O2
?
show the reaction diagram
-
-
-
-
?
4-methylsalicylic acid + NADH + O2
? + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
4-t-butylbenzoic acid + NADH + O2
? + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
4-trifluoromethylbenzoate + NADH + O2
?
show the reaction diagram
-
-
-
-
?
4-vinylbenzoate + NADH + O2
4-glycylbenzoate + NAD+ + H2O
show the reaction diagram
-
external dioxygenase reaction by substrate induced modulation
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-
?
alkylbenzoates
?
show the reaction diagram
-
-
-
-
?
benzoate + NADH + O2
?
show the reaction diagram
-
-
-
-
?
benzoic acid + NADH + O2
? + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
cinnamic acid + AH2 + O2
? + A + H2O
show the reaction diagram
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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-
?
L-perillic acid + NADH + O2
? + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
N,N'-dimethyl-4-aminobenzoate + NADH + O2
4-aminobenzoate + NAD+ + H2O + formaldehyde
show the reaction diagram
-
-
-
-
?
N-methyl-4-aminobenzoate + NADH + O2
4-aminobenzoate + NAD+ + H2O + formaldehyde
show the reaction diagram
veratrate + AH2 + O2
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
show the reaction diagram
4-methoxybenzoate + NADH + O2
4-hydroxybenzoate + NAD+ + H2O + formaldehyde
show the reaction diagram
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-
-
-
?
4-methoxybenzoate + reduced ferredoxin + O2
4-hydroxybenzoate + formaldehyde + ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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can replace NADH with 40% efficiency
palustrisredoxin
palustrisredoxin A
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-
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reduced ferredoxin
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-
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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-
2,2'-dipyridyl
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3-Methoxybenzoate
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4-(2-Pyridylazo)resorcinol
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-
4-tert-Butylbenzoate
-
competitive inhibitor of the O-demethylation of 3-nitro-4-methoxybenzoate, hinders O2-binding or O2-activation
4-trifluoromethylbenzoate
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
8-hydroxyquinoline
-
-
Bathocuproinedisulfonate
-
-
bathophenanthrolinedisulfate
Benzoate
-
competitive inhibition
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
Cumylhydroperoxide
-
-
diethyldithiocarbamate
-
-
Iodosobenzene
-
-
Oxidized putidamonooxin
-
60% inhibition with 3-nitro-4-methoxybenzoate as substrate, fully reactivated by Fe2+ and sulfhydryl-reagents
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p-chloromercuribenzoate
Thenoyl trifluoroacetone
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-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Putidamonooxin
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0003 - 0.0007
3-Nitro-4-methoxybenzoate
0.029
4-hydroxybenzoate
-
-
0.00007 - 0.0014
4-Methoxybenzoate
0.0058
4-methylaminobenzoate
-
-
0.0062 - 0.009
4-Methylbenzoate
0.0144 - 0.024
4-trifluoromethylbenzoate
0.0367 - 0.055
Benzoate
0.077
N-methyl-4-aminobenzoate
-
-
0.00063 - 0.008
NADH
0.14
NADPH
-
reconstituted enzyme
0.0019 - 0.055
O2
0.03
Putidamonooxin
-
-
-
additional information
additional information
-
steady-state kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
37.9
4-Methoxybenzoate
Rhodopseudomonas palustris
Q2IU02
pH 7.4, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
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4-hyroxybenzoate, reductase
0.004
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4-hydroxybenzoate, monooxygenase
0.008
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3-methoxybenzoate, 4-methoxybenzoate, cell-free extract
0.009
-
N,N-dimethyl-4-aminobenzoate
0.018
-
superoxide anion instead of substrate, putidamonooxin
0.021
-
4-hydroxy-3-methoxybenzoate
0.023
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3-hydroxybenzoate, reconstituted enzyme
0.024
-
4-ethoxybenzoate, N-methyl-4-aminobenzoate
0.025
-
3,4-dimethoxybenzoate
0.04
-
4-methoxybenzoate, cell-free extract
0.055
-
4-hyxdroxybenzoate
0.077
-
4-hydroxybenzoate, reconstituted enzyme
0.11
-
3-methoxybenzoate
0.178
-
N-methyl-4-aminobenzoate
0.192
-
3-nitro-4-methoxybenzoate, putidamonooxin
0.27
-
4-methoxybenzoate, putidamonooxin
0.314
-
4-ethoxybenzoate, piperonylate
0.345
-
3,4-dimethoxybenzoate
0.36
-
4-methoxybenzoate
21.96
-
4-methoxybenzoate
194.5
-
3-phenyl-4-[2H3]-methoxybenzoate, product formation, reaction in H2O
207.8
-
4-trifluoromethylbenzoate, oxygen uptake, reaction in D2O
239.8
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3-phenyl-4-[2H3]-methoxybenzoate, product formation, reaction in D2O
265.6
-
benzoate, oxygen uptake, reaction in D2O
295.1
-
benzoate, oxygen uptake, reaction in H2O
303.9
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3-phenyl-4-[1H3]-methoxybenzoate, product formation, reaction in H2O
305.2
-
4-methylbenzoate, NADH oxidation, reaction in H2O
310.1
-
3-phenyl-4-[2H3]-methoxybenzoate, oxygen uptake, reaction in D2O; 3-phenyl-4-[2H3]-methoxybenzoate, oxygen uptake, reaction in H2O
315.5
-
4-trifluoromethylbenzoate, NADH oxidation, reaction in D2O
317.2
-
4-methylbenzoate, NADH oxidation, reaction in D2O
317.4
-
3-phenyl-4-[1H3]-methoxybenzoate, product formation, reaction in D2O
326.7
-
3-phenyl-4-[1H3]-methoxybenzoate, oxygen uptake, reaction in H2O
329.2
-
3-phenyl-4-[1H3]-methoxybenzoate, oxygen uptake, reaction in D2O
339.1
-
benzoate, NADH oxidation, reaction in D2O
340.2
-
3-phenyl-4-[2H3]-methoxybenzoate, NADH oxidation, reaction in H2O
345
-
4-trifluoromethylbenzoate, oxygen uptake, reaction in H2O
345.6
-
benzoate, NADH oxidation, reaction in H2O
353.5
-
3-phenyl-4-[2H3]-methoxybenzoate, NADH oxidation, reaction in D2O
360.4
-
3-phenyl-4-[1H3]-methoxybenzoate, NADH oxidation, reaction in H2O
367
-
4-methylbenzoate, oxygen uptake, reaction in H2O
368
-
4-methylbenzoate, oxygen uptake, reaction in D2O
380.2
-
3-phenyl-4-[1H3]-methoxybenzoate, NADH oxidation, reaction in D2O
391.5
-
4-methoxybenzoate, oxygen uptake, reaction in D2O
394.1
-
4-methoxybenzoate, oxygen uptake, reaction in H2O
402.6
-
3-nitro-4-methoxybenzoate, NADH oxidation, reaction in D2O
409.7
-
4-trifluoromethylbenzoate, NADH oxidation, reaction in H2O
422.1
-
3-nitro-4-methoxybenzoate, NADH oxidation, reaction in H2O
432.4
-
3-nitro-4-methoxybenzoate, oxygen uptake, reaction in H2O
432.7
-
3-nitro-4-methoxybenzoate, oxygen uptake, reaction in D2O
442.2
-
4-methoxybenzoate, NADH oxidation, reaction in D2O
445
-
4-methoxybenzoate, NADH oxidation, reaction in H2O
450.9
-
3-nitro-4-methoxybenzoate, product formation, reaction in H2O
487.3
-
3-nitro-4-methoxybenzoate, product formation, reaction in D2O
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 9
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about half-maximal activity at pH 7.3 and 9.0, reductase
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
alpha2, 2 * 52000, putidamonooxin, SDS-PAGE
oligomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
30% carbohydrate in each of the 50000 Da subunits
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, 20C, 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, 20C, 2 weeks, X-ray diffraction structure determination and analysis at 2.6 A and 2.0 A resolution, respectively
purified recombinant CYP199A2, 16 C, 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
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
4-methoxybenzoate, stabilizes
-
ethanol, 5-15% v/v, stabilizes activity in buffer and crude extract
-
NADH, not NADPH or substrate stabilize the reductase
-
substrate or substrate analogues stabilize putidamomooxin by preventing loss of Fe2+
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
aerobic conditions, 0-4C, 50% activity lost within 24 h
-
438344
putidamonooxin and NADH-reductase, extremely O2-sensitive, GSH, DTT, 2-mercaptoethanol prevent putidamonooxin oxidation of putdamonooxin
-
438346
putidamonooxin and NADH-reductase, extremely O2-sensitive, purification and storage of the reductase under anaerobic conditions
-
438350
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, freeze-dried partially purified reductase stable for months without loss of activity, purified reductase is 3-4 weeks stable after addition of NADH in N2-atmosphere
-
0-4C, more than 24 days stable in crude extract under anaerobic conditions
-
4C, concentrated putidamonooxin stable for several months in N2-atmosphere with DTT and dithionite
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by two different steps of anion exchange chromatography, followed by 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
recombinant His-tagged enzyme from Escherichia coli BL21(DE3) by nickel affinity chromatography and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
expression in Escherichia coli strain BL21(DE3); wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
expression of wild-type and mutant CYP199A2 in Escherichia coli strain BL21(DE3)
-
overexpression of the His-tagged enzyme in Escherichia coli BL21(DE3)
-
ENGINEERING
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
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
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
CYP199A2 may be a valuable biocatalyst for the regioselective oxidation of various aromatic carboxylic acids