Information on EC 1.14.13.92 - phenylacetone monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.92
-
RECOMMENDED NAME
GeneOntology No.
phenylacetone monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
phenylacetone,NADPH:oxygen oxidoreductase
A flavoprotein (FAD). NADH cannot replace NADPH as coenzyme. In addition to phenylacetone, which is the best substrate found to date, this Baeyer-Villiger monooxygenase can oxidize other aromatic ketones [1-(4-hydroxyphenyl)propan-2-one, 1-(4-hydroxyphenyl)propan-2-one and 3-phenylbutan-2-one], some alipatic ketones (e.g. dodecan-2-one) and sulfides (e.g. 1-methyl-4-(methylsulfanyl)benzene).
CAS REGISTRY NUMBER
COMMENTARY hide
1005768-90-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain KT2440, BVMO gene
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2-methylphenyl)acetone + NADPH + O2
? + NADP+ + O2
show the reaction diagram
-
-
-
-
?
(2R,3S)-3-methyl-2-pentylcyclopentanone + NADPH + H+ + O2
?
show the reaction diagram
-
less than 5% conversion
-
-
?
(R)-1-acetoxy-phenylacetone + NADPH + O2
(R)-1-hydroxy-1-phenylacetone + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
(R)-2-acetoxyphenylacetonitrile + NADPH + H+ + O2
?
show the reaction diagram
-
enantioselective reaction
-
-
?
(R)-3-(4-bromophenyl)butan-2-one + NADPH + H+ + O2
?
show the reaction diagram
-
enantioselective reaction
-
-
?
(S)-1-(3-trifluoromethylphenyl)ethyl acetate + NADPH + H+ + O2
?
show the reaction diagram
-
enantioselective reaction
-
-
?
(S)-nicotine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
1-bromo-indanone + NADPH + O2
6-bromoisochroman-1-one + NADP+ + H2O
show the reaction diagram
-
substrate was only accepted by phenylacetone monooxygenase of Pseudomonas fluorescens but not of Thermobifida fusca, reaction was performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH
-
-
?
1-indanone + NADPH + O2
3,4-dihydrocoumarin + NADP+ + H2O
show the reaction diagram
-
substrate was only accepted by phenylacetone monooxygenase of Pseudomonas fluorescens but not of Thermobifida fusca, reaction was performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH
-
-
?
1-indanone + NADPH + O2
3-isochromanone + NADP+ + H2O
show the reaction diagram
-
reaction product is only synthesized by the mutant M446G of phenylacetone monooxygenase of Thermobifida fusca, reaction is performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH
-
-
?
1-tetralone + NADPH + O2
4,5-dihydro-1-benzoxepin-2(3H)-one + NADP+ + H2O
show the reaction diagram
-
substrate was accepted by phenylacetone monooxygenase of Pseudomonas fluorescens but not of Thermobifida fusca, reaction was performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH
-
-
?
1-[3-(benzylselanyl)phenyl]ethanone + NADPH + H+ + O2
1-(3-(benzylseleninyl)phenyl)ethanone + NADP+ + H2O
show the reaction diagram
-
more than 99% conversion
-
-
?
1-[3-(methylselanyl)phenyl]ethanone + NADPH + H+ + O2
1-(3-(methylseleninyl)phenyl)ethanone + NADP+ + H2O
show the reaction diagram
-
76% conversion
-
-
?
1-[4-(benzylselanyl)phenyl]ethanone + NADPH + H+ + O2
1-(4-(benzylseleninyl)phenyl)ethanone + NADP+ + H2O
show the reaction diagram
-
more than 99% conversion
-
-
?
1-[4-(methylselanyl)phenyl]ethanone + NADPH + H+ + O2
1-(4-(methylseleninyl)phenyl)ethanone + NADP+ + H2O
show the reaction diagram
-
more than 99% conversion
-
-
?
2-benzylcyclopentanone + NADPH + H+ + O2
?
show the reaction diagram
-
about 10% conversion
-
-
?
2-decanone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-decanone + NADPH + O2
methyl nonanoate + octyl acetate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-dodecanone + NADPH + O2
? + NADP+
show the reaction diagram
-
-
-
-
?
2-dodecanone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-dodecanone + NADPH + O2
nonyl acetate + methyl decanoate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-heptanone + NADPH + O2
pentyl acetate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-hexanone + NADPH + O2
butyl acetate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-indanone + NADPH + O2
3,4-dihydrocoumarin + NADP+ + H2O
show the reaction diagram
-
substrate is only accepted by the mutant M446G of phenylacetone monooxygenase of Thermobifida fusca, reaction is performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH
-
-
?
2-methylphenylcyclohexanone + NADPH + O2
7-benzyloxepan-2-one + NADP+ + H2O
show the reaction diagram
-
mutant P3 prefers the R-isomer
-
-
?
2-nonanone + NADPH + H+ + O2
?
show the reaction diagram
-
less than 40% conversion
-
-
?
2-nonanone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-octanone + NADPH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
2-octanone + NADPH + O2
heptyl acetate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-phenylcyclohexanone + NADPH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
2-phenylcyclohexanone + NADPH + O2
7-phenyloxepan-2-one + NADP+ + H2O
show the reaction diagram
-
molecular modeling of the Criegee intermediate, the wild-type enzyme prefers the S-isomer, while mutants P1-P3 all prefer the R-isomer
-
-
?
2-phenylpropionaldehyde + NADPH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
2-undecanone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
3-(3-trifluoromethylphenyl)butan-2-one + NADPH + H+ + O2
?
show the reaction diagram
-
enantioselective reaction
-
-
?
3-(4-chlorophenyl)cyclobutanone + NADPH + H+ + O2
?
show the reaction diagram
-
about 40% conversion
-
-
?
3-benzylcyclobutanone + NADPH + H+ + O2
?
show the reaction diagram
-
about 45% conversion
-
-
?
3-decanone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
3-octanone + NADPH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
3-octanone + NADPH + O2
ethyl hexanoate + pentyl propanoate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
3-phenyl-2-butanone + NADPH + H+ + O2
(R)-3-phenylbutan-2-one + (S)-1-phenyethyl acetate
show the reaction diagram
-
enantioselective reaction
-
-
?
3-phenylcyclobutanone + NADPH + H+ + O2
?
show the reaction diagram
-
about 70% conversion
-
-
?
3-phenylpenta-2,4-dione + NADPH + O2
(R)-phenylacetylcarbinol + NADP+ + H2O
show the reaction diagram
-
-
the product is a well-known precursor in the synthesis of ephedrine and pseudoephedrine
-
?
4-decanone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
4-heptanone + NADPH + O2
propanyl butanoate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
4-hydroxyacetophenone + NADPH + O2
acetic acid 4-hydroxyphenyl ester + NADP+ + O2
show the reaction diagram
-
-
-
-
?
4-phenylcyclohexanone + NADPH + O2
4-phenyl-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
6-methoxy-1-indanone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
substrate was only accepted by phenylacetone monooxygenase of Pseudomonas fluorescens but not of Thermobifida fusca, reaction was performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH
-
-
?
alpha-acetylphenylacetonitrile + NADPH + H+ + O2
(R)-2-acetoxyphenylacetonitrile + NADP+ + H2O
show the reaction diagram
-
enantioselective reaction
enantiopure product formation
-
?
benzocyclobutanone + NADPH + O2
2-coumaranone + NADP+ + H2O
show the reaction diagram
benzylacetone + NADPH + O2
?
show the reaction diagram
-
low activity
-
-
?
benzylacetone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
bicyclohept-2-en-6-one + NADPH + O2
3-oxabicyclo[3.3.0]oct-6-en-2-one + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
bicyclohept-2-en-6-one + NADPH + O2
? + NADP+ + O2
show the reaction diagram
-
-
-
-
?
bicyclo[2.2.1]heptan-2-one + NADPH + H+ + O2
?
show the reaction diagram
-
about 5% conversion
-
-
?
bicyclo[3.2.0]hept-2-en-6-one + NADPH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
cyclohexanone + NADPH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
cyclopentanone + NADPH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
diketone + NADPH + O2
(R)-1-acetoxy-phenylacetone + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
ethionamide + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
ethionamide + NADPH + O2
? + NADP+ + O2
show the reaction diagram
-
-
-
-
?
methyl 4-tolylsulfide + NADPH + O2
? + NADP+ + O2
show the reaction diagram
-
-
-
-
?
methyl-p-tolylsulfide + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N,N-dimethylbenzylamine + NADPH + O2
N,N-dimethylbenzylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
phenylacetone + NADPH + H+ + O2
benzyl acetate + NADP+ + H2O
show the reaction diagram
phenylacetone + NADPH + O2
benzyl acetate + NADP+ + H2O
show the reaction diagram
phenylboronic acid + NADPH + O2
?
show the reaction diagram
-
formation of phenol
-
-
?
rac-2-ethylcyclohexanone + NADPH + O2
benzyl acetate + NADP+ + H2O
show the reaction diagram
-
substrate is only accepted by mutants of phenylacetone monooxygenase, reaction is performed in presence of 2 U secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus and isopropanol to recover NADPH
-
-
?
rac-3-methyl-4-phenylbutan-2-one + NADH + H+ + O2
(2R)-1-phenylpropan-2-yl acetate + NAD+ + H2O
show the reaction diagram
-
enantioselective reaction by PAMO
-
-
?
rac-3-methyl-4-phenylbutan-2-one + NADPH + H+ + O2
(2R)-1-phenylpropan-2-yl acetate + NADP+ + H2O
show the reaction diagram
-
enantioselective reaction by PAMO
-
-
?
rac-bicyclo [3.2.0]hept-2-en-6-one + NADPH + O2
?
show the reaction diagram
-
activity and stereoselectivity of wild-type and mutant enzymes, overview
-
-
?
thioanisole + NADH + H+ + O2
thioanisole sulfoxide + NAD+ + H2O
show the reaction diagram
-
low activity, less enantioselective reaction
-
-
?
thioanisole + NADPH + H+ + O2
?
show the reaction diagram
thioanisole + NADPH + H+ + O2
methyl phenyl sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
thioanisole + NADPH + H+ + O2
thioanisole sulfoxide + NADP+ + H2O
show the reaction diagram
-
enantioselective reaction
mainly (R)-sulfoxide
-
?
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
2-decanone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-dodecanone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-nonanone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-undecanone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
3-decanone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
4-decanone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
phenylacetone + NADPH + H+ + O2
benzyl acetate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
substrate specificity and reaction mechanism, the enzyme shows high specificity towards short-chain aliphatic ketones, some open-chain ketones are converted to the alkylacetates, while for others formation of the ester products with oxygen on the other side of the keto group can also be detected yielding the corresponding methyl or ethyl esters, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-NADPD
-
deuterated cofactor derivative, the overall rate of catalysis is largely determined by the rate of hydride transfer upon replacement of NADPH by (R)-NADPD as the coenzyme, overview
NADH
-
poor activity with NADH, kinetics, binding mode, overview
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,4-dioxane
-
33% inhibition at 10% concentration as co-solvent, 53% inhibition at 30%
2-Octanone
-
substrate inhibition
3-acetyl-NADP+
-
0.5 mM, 50% inhibition
3-amino-NADP+
-
0.05 mM, 74% inhibition
acetone
-
45% inhibition at 10% concentration as co-solvent inpresence of substrate, 93% in absence of substrate
acetonitrile
-
88.5% inhibition at 30% concentration as co-solvent
Benzyl acetate
-
product inhibition
ethanol
-
45% inhibition at 10% concentration as co-solvent
hexane
-
enzyme activity is markedly reduced at concentrations of hexane below 5% and over 30%
Isopropanol
-
52% inhibition at 30% concentration as co-solvent
methanol
-
40% inhibition at 30% concentration as co-solvent
n-Propanol
-
80% inhibition at 30% concentration as co-solvent
NADP+
-
product inhibition, remains bound during catalysis
phenylacetone
-
substrate inhibition
additional information
-
effects of a range of solvents on the biocatalytic properties of the biocatalyst, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bovine serum albumin
-
2 mg7ml, 930% activation
-
hexane
-
enzyme activity is highest at concentrations of hexane between 5% and 30%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.83
(2-methylphenyl)acetone
-
30°C, pH 7.5, 0.1 mM NADPH
0.2 - 0.26
2-dodecanone
0.25 - 2
2-Octanone
0.07 - 4
2-phenylcyclohexanone
2.2
4-hydroxyacetophenone
-
30°C, pH 7.5, 0.1 mM NADPH
0.36 - 0.52
benzylacetone
15
bicyclohept-2-en-6-one
-
30°C, pH 7.5, 0.1 mM NADPH
1000 - 1200
Cyclopentanone
0.34
Ethionamide
-
25°C, pH 8.5
0.86
methyl 4-tolylsulfide
-
30°C, pH 7.5, 0.1 mM NADPH
0.0006 - 0.85
NADPH
0.04 - 4
phenylacetone
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
(2-methylphenyl)acetone
Thermobifida fusca
-
30°C, pH 7.5, 0.1 mM NADPH
0.023 - 0.23
2-dodecanone
1 - 2.3
2-Octanone
0.07 - 0.5
2-phenylcyclohexanone
0.34
4-hydroxyacetophenone
Thermobifida fusca
-
30°C, pH 7.5, 0.1 mM NADPH
0.021 - 1.8
benzylacetone
1.1
bicyclohept-2-en-6-one
Thermobifida fusca
-
30°C, pH 7.5, 0.1 mM NADPH
0.9 - 1.6
Cyclopentanone
0.027
Ethionamide
Mycobacterium tuberculosis
-
25°C, pH 8.5
2.1
methyl 4-tolylsulfide
Thermobifida fusca
-
30°C, pH 7.5, 0.1 mM NADPH
0.8 - 3.8
NADPH
0.017 - 3
phenylacetone
additional information
additional information
Thermobifida fusca
-
all substrates show a turnover between 1.2 s-1 and 3.6 s-1
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.48 - 9.2
2-Octanone
5474
0.008 - 0.37
2-phenylcyclohexanone
4760
0.8 - 1.6
Cyclopentanone
2478
1 - 6000
NADPH
5
35 - 37.5
phenylacetone
3713
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
7.5 - 9
-
assay at
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
-
pH profile, and dependence of the enantioselectivity of the reaction, overview
7 - 9
-
more than 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 30
-
biotransformation assay
25 - 30
-
assay at
27
-
assay at
30
-
assay at
40
-
assay at
70
-
4fold higher activity when compared with the activity at 25°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 58
-
at 58C 75% of enzyme activity remains, at 60C activity is nearly zero, at 45C enzyme is fully active
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
-
1 * 65000, SDS-PAGE, small amount of approx. 7% is present as a dimer
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 65000, SDS-PAGE, small amount of approx. 7% is present as a dimer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals are grown at 20°C by vapor diffusion, hanging drops are formed by mixing equal volumes of 18 mg/ml protein in 5 mM FAD and 50 mM sodium phosphate, pH 7.0, and of a well solution consisting of 1.5 M ammonium sulfate and 500 mM lithium chloride, crystals diffract to 1.7 A resolution
-
PAMO crystal structure analysis, comparison to cyclohexanone monooxygenase, EC 1.14.13.22
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52
-
50% loss of activity after 24 h and 48 h in the absence and presence of FAD, respectively
60
-
the wild type enzyme has a melting temperature of 60°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
detergents stabilize the enzyme, best by Tween-20 at 0.1% v/v
-
PAMO that has been activated at 50°C can be stored for several days at room temperature without any loss in activity
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-pentanol
-
as a sacrificial substrate
cyclohexane
-
stabilizes the enzyme, best organic solvent, inactivation of the enzyme within 5 min
isopropanol
-
the most effective stoichiometric sacrificial electron donor, optimal at 5% v/v
Methanol
-
methanol induces a significant increase of enzyme activity (up to 5fold), which is optimal at 20% (v/v)
methyl tert-butyl ether
-
stabilizes the enzyme, inactivation of the enzyme within below 5 min
additional information
-
the initial activity of wild type enzyme is not affected by 10% (v/v) 1,4-dioxane
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose, hydroxyapatite, Superdex 200
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli
-
recombinant His-tagged wild-type and mutant PAMOs from Escherichia coli strain TOP10 by nickel affinity chromatography
-
recombinant PAMO
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
BVMO gene, functional expression in Escherichia coli strains JM109 and BL21(DE3) as soluble protein
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli Top10 cells
-
expression in Escherichia coli
expression of His-tagged wild-type and mutant enzymes in Escherichia coli
-
expression of His-tagged wild-type and mutant PAMOs in Escherichia coli strain TOP10
-
overexpressed in Escherichia coli
-
overexpressed via plasmid in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A435Y
-
the mutant is active only with bicyclo[3.2.0]hept-2-en-6-one; the mutant shows less than 3% of wild type activity
A442G
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the mutant shows 75% of wild type activity
C65V
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the mutant shows 94% of wild type activity
C65V/I67T
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the mutant shows 47% of wild type activity
C65V/I67T/Q152F/S441A/A442G
-
the mutant shows 31% of wild type activity
C65V/I67T/Q93W
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the mutant shows 54% of wild type activity
H220A
-
site-directed mutagenesis
H220D
-
site-directed mutagenesis
H220E
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site-directed mutagenesis, H220E mutant performs worse than wild-type PAMO with both coenzymes NADPH and NADH
H220F
-
site-directed mutagenesis
H220N
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site-directed mutagenesis, the mutant shows about 3fold improvement in the catalytic efficiency with NADH while the catalytic efficiency with NADPH is hardly affected
H220Q
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site-directed mutagenesis, the mutant shows about 3fold improvement in the catalytic efficiency with NADH while the catalytic efficiency with NADPH is hardly affected
H220Q/K336H
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site-directed mutagenesis
H220Q/K336N
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site-directed mutagenesis
H220T
-
site-directed mutagenesis
H220W
-
site-directed mutagenesis
I339S
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the mutant shows 81% of wild type activity
I67T
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the mutant shows 16% of wild type activity
I67T/L338P
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the mutant shows less than 3% of wild type activity
I67T/L338P/A435Y/A442G
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the mutant shows less than 3% of wild type activity
I67T/L338P/A435Y/A442G/L443F/S444C
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the mutant shows less than 3% of wild type activity
K336H
-
site-directed mutagenesis
K336N
-
site-directed mutagenesis
L153G
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inactive; the mutant shows less than 3% of wild type activity
L338P
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the mutant shows 59% of wild type activity
L443F
-
the mutant shows 65% of wild type activity
L447P
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the mutant shows 85% of wild type activity
P253F/G254A/R258M/L443F
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the mutant shows the same thermostability as the wild type enzyme while it displays an extended substrate spectrum
P440F
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higher subtrate variability, temperature optimum at 50C with range from 45-56C
P440H
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higher subtrate variability, temperature optimum at 50C with range from 45-56C
P440I
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higher subtrate variability, temperature optimum at 50C with range from 45-56C
P440L
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higher subtrate variability, temperature optimum at 50C with range from 45-56C
P440N
-
higher subtrate variability, temperature optimum at 50C with range from 45-56C
P440T
-
higher subtrate variability, temperature optimum at 50C with range from 45-56C
P440Y
-
higher subtrate variability, temperature optimum at 50C with range from 45-58C
Q152F
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the mutant shows 35% of wild type activity
Q152F/A442G
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the mutant shows 37% of wild type activity
Q152F/S441A/A442G
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the mutant shows 33% of wild type activity
Q93W
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the mutant shows 65% of wild type activity
Q93W/A442G/S444C/M446G/L447P
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the mutant shows 38% of wild type activity
Q93W/S441A/A442G/S444C/M446G/L447P
-
the mutant shows 40% of wild type activity
R217A
-
site-directed mutagenesis
R217L
-
site-directed mutagenesis
R337A
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site-directed mutagenesis, the mutant is still able to form and stabilize the C4a-peroxyflavin intermediate, but loses the ability to convert phenylacetone or benzyle methylsulfide
R337K
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site-directed mutagenesis, the mutant is still able to form and stabilize the C4a-peroxyflavin intermediate, but loses the ability to convert phenylacetone or benzyle methylsulfide
S441A
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the mutant shows 73% of wild type activity
S441A/A442G
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the mutant shows 56% of wild type activity
S441A/A442G/S444C/M446G/L447P
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the mutant shows 41% of wild type activity
S444C
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the mutant shows 66% of wild type activity
T218A
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site-directed mutagenesis
V54I
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the mutant shows 65% of wild type activity
V54I/C65V/I67T/Q93W/I339S/S441A/A442G/S444C/M446G/L447P
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the mutant shows 5% of wild type activity
V54I/C65V/I67T/Q93W/Q152F/I339S/S441A/A442G/S444C/M446G/L447P
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the mutant shows less than 3% of wild type activity
V54I/C65V/I67T/Q93W/Q152F/L153G/I339S/S441A/A442G/S444C/M446G/L447P
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the mutant shows less than 3% of wild type activity
W501A
-
the mutant shows reduced activity compared to the wild type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
Show AA Sequence (271 entries)
Please use the Sequence Search for a specific query.