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Enzyme Nomenclature
Information on EC 1.14.13.92 - phenylacetone monooxygenase
Word Map on EC 1.14.13.92
- 1.14.13.92
-
baeyer-villiger
-
bvmos
-
enantioselectivity
-
biocatalytic
- ketone
-
scope
- cyclohexanone
-
thermobifida
- fusca
-
sulfoxidations
- synthesis
-
biocatalyst
-
iterative
-
prochiral
-
desymmetrization
-
criegee
-
flavin-containing
-
redesign
-
alicyclic
-
peroxyflavin
-
structure-inspired
- cyclopentanone
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.92
-
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RECOMMENDED NAME
GeneOntology No.
phenylacetone monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O
-
-
-
-
phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O
reaction mechanism
-
phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O
reaction mechanism and catalytic cycle, rapid binding of NADPH is followed by a transfer of the (4R)-hydride from NADPH to the FAD cofactor. The reduced PAMO is rapidly oxygenated by molecular oxygen, yielding a C4a-peroxyflavin. The peroxyflavin enzyme intermediate, possibly a Criegee intermediate or a C4a-hydroxyflavin form, reacts with phenylacetone to form benzylacetate, residue R337 is important in catalysis, overview
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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).
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CAS REGISTRY NUMBER
COMMENTARY
1005768-90-0
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
(2R,3S)-3-methyl-2-pentylcyclopentanone + NADPH + H+ + O2
?
-
less than 5% conversion
-
-
?
(R)-1-acetoxy-phenylacetone + NADPH + O2
(R)-1-hydroxy-1-phenylacetone + NADP+ + H2O
-
-
-
-
?
(R)-2-acetoxyphenylacetonitrile + NADPH + H+ + O2
?
-
enantioselective reaction
-
-
?
(R)-3-(4-bromophenyl)butan-2-one + NADPH + H+ + O2
?
-
enantioselective reaction
-
-
?
(S)-1-(3-trifluoromethylphenyl)ethyl acetate + NADPH + H+ + O2
?
-
enantioselective reaction
-
-
?
1-bromo-indanone + NADPH + O2
6-bromoisochroman-1-one + NADP+ + H2O
-
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
-
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
-
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
-
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
-
more than 99% conversion
-
-
?
1-[3-(methylselanyl)phenyl]ethanone + NADPH + H+ + O2
1-(3-(methylseleninyl)phenyl)ethanone + NADP+ + H2O
-
76% conversion
-
-
?
1-[4-(benzylselanyl)phenyl]ethanone + NADPH + H+ + O2
1-(4-(benzylseleninyl)phenyl)ethanone + NADP+ + H2O
-
more than 99% conversion
-
-
?
1-[4-(methylselanyl)phenyl]ethanone + NADPH + H+ + O2
1-(4-(methylseleninyl)phenyl)ethanone + NADP+ + H2O
-
more than 99% conversion
-
-
?
2-decanone + NADPH + O2
methyl nonanoate + octyl acetate + NADP+ + H2O
-
-
-
-
?
2-dodecanone + NADPH + O2
nonyl acetate + methyl decanoate + NADP+ + H2O
-
-
-
-
?
2-indanone + NADPH + O2
3,4-dihydrocoumarin + NADP+ + H2O
-
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
-
mutant P3 prefers the R-isomer
-
-
?
2-phenylcyclohexanone + NADPH + O2
7-phenyloxepan-2-one + NADP+ + H2O
-
molecular modeling of the Criegee intermediate, the wild-type enzyme prefers the S-isomer, while mutants P1-P3 all prefer the R-isomer
-
-
?
3-(3-trifluoromethylphenyl)butan-2-one + NADPH + H+ + O2
?
-
enantioselective reaction
-
-
?
3-(4-chlorophenyl)cyclobutanone + NADPH + H+ + O2
?
-
about 40% conversion
-
-
?
3-octanone + NADPH + O2
ethyl hexanoate + pentyl propanoate + NADP+ + H2O
-
-
-
-
?
3-phenyl-2-butanone + NADPH + H+ + O2
(R)-3-phenylbutan-2-one + (S)-1-phenyethyl acetate
-
enantioselective reaction
-
-
?
3-phenylpenta-2,4-dione + NADPH + O2
(R)-phenylacetylcarbinol + NADP+ + H2O
-
-
the product is a well-known precursor in the synthesis of ephedrine and pseudoephedrine
-
?
4-heptanone + NADPH + O2
propanyl butanoate + NADP+ + H2O
-
-
-
-
?
4-hydroxyacetophenone + NADPH + O2
acetic acid 4-hydroxyphenyl ester + NADP+ + O2
-
-
-
-
?
4-phenylcyclohexanone + NADPH + O2
4-phenyl-hexano-6-lactone + NADP+ + H2O
-
-
-
-
?
6-methoxy-1-indanone + NADPH + O2
? + NADP+ + H2O
-
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
-
enantioselective reaction
enantiopure product formation
-
?
bicyclohept-2-en-6-one + NADPH + O2
3-oxabicyclo[3.3.0]oct-6-en-2-one + NADP+ + H2O
-
-
-
-
?
bicyclo[2.2.1]heptan-2-one + NADPH + H+ + O2
?
-
about 5% conversion
-
-
?
N,N-dimethylbenzylamine + NADPH + O2
N,N-dimethylbenzylamine N-oxide + NADP+ + H2O
-
-
-
-
?
rac-2-ethylcyclohexanone + NADPH + O2
benzyl acetate + NADP+ + H2O
-
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
-
enantioselective reaction by PAMO
-
-
?
rac-3-methyl-4-phenylbutan-2-one + NADPH + H+ + O2
(2R)-1-phenylpropan-2-yl acetate + NADP+ + H2O
-
enantioselective reaction by PAMO
-
-
?
rac-bicyclo [3.2.0]hept-2-en-6-one + NADPH + O2
?
-
activity and stereoselectivity of wild-type and mutant enzymes, overview
-
-
?
thioanisole + NADH + H+ + O2
thioanisole sulfoxide + NAD+ + H2O
-
low activity, less enantioselective reaction
-
-
?
thioanisole + NADPH + H+ + O2
methyl phenyl sulfoxide + NADP+ + H2O
-
-
-
-
?
thioanisole + NADPH + H+ + O2
thioanisole sulfoxide + NADP+ + H2O
-
enantioselective reaction
mainly (R)-sulfoxide
-
?
benzocyclobutanone + NADPH + O2
2-coumaranone + NADP+ + H2O
-
reaction was performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH
-
-
?
benzocyclobutanone + NADPH + O2
2-coumaranone + NADP+ + H2O
-
reaction is performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH
-
-
?
phenylacetone + NADPH + H+ + O2
benzyl acetate + NADP+ + H2O
-
-
-
-
?
phenylacetone + NADPH + H+ + O2
benzyl acetate + NADP+ + H2O
-
-
-
?
phenylacetone + NADPH + H+ + O2
benzyl acetate + NADP+ + H2O
-
-
-
-
?
phenylacetone + NADPH + H+ + O2
benzyl acetate + NADP+ + H2O
-
enantioselective reaction, regulation mechanism, overview
-
-
?
phenylacetone + NADPH + O2
benzyl acetate + NADP+ + H2O
-
reaction was performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH
-
-
?
phenylacetone + NADPH + O2
benzyl acetate + NADP+ + H2O
-
reaction is performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH
-
-
?
phenylacetone + NADPH + O2
benzyl acetate + NADP+ + H2O
-
reaction is performed in presence of 2 U secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus and isopropanol to recover NADPH
-
-
?
thioanisole + NADPH + H+ + O2
?
-
the asymmetric oxidation of thioanisole to sulfoxide is accompanied by the overoxidation to achiral sulfone
-
-
?
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
-
-
-
additional information
?
-
-
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, no activity with 2-octanone and 2-tridecanone
-
-
-
additional information
?
-
-
enzyme activity in a variety of different aqueousorganic media using organic sulfides as substrates, enantioselectivity, overview
-
-
-
additional information
?
-
-
substrate selectivity and stereospecificity of wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
-
the recombinant His-tagged enzyme is active with a large range of sulfides and ketones, as well as with several sulfoxides, an amine and an organoboron compound, high enantioselectivity dependeing on the substrate, substrate specificity, overview
-
-
-
additional information
?
-
-
PAMO is an FAD-containing Baeyer-Villiger monooxygenase
-
-
-
additional information
?
-
-
PAMO is an FAD-containing Baeyer-Villiger monooxygenase, two different residues are responsible for the pH effects on PAMO enantioselectivity, protonation of Arg337 and the FAD:C4a-hydroperoxide/FAD:C4a-peroxide equilibrium are the major factors responsible for the fine-tuning of PAMO enantioselectivity in Baeyer-Villiger oxidation and sulfooxidation, respectively
-
-
-
additional information
?
-
-
determination of enantioselectivity of wild-type and mutant enzymes with different substrates and cofactors, overview. Residue K336 has a significant and beneficial effect on the enantioselectivity of Baeyer-Villiger oxidations and sulfoxidations
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
phenylacetone + NADPH + H+ + O2
benzyl acetate + NADP+ + H2O
-
-
-
-
?
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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
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
FAD
-
residue R337, which is conserved in other Baeyer-Villiger monooxygenases, is positioned close to the flavin cofactor
NADPH
-
PAMO is a type I Baeyer-Villiger monooxygenase, that strongly prefers NADPH over NADH as an electron donor, the function of NADPH in catalysis cannot be easily replaced by NADH. The conserved R217 is essential for binding the adenine moiety of the nicotinamide coenzyme while it also contributes to the recognition of the 2'-phosphate moiety of NADPH, binding mode, overview. T218 and K336 do not have a strong effect on the coenzyme specificity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,4-dioxane
-
33% inhibition at 10% concentration as co-solvent, 53% inhibition at 30%
acetone
-
45% inhibition at 10% concentration as co-solvent inpresence of substrate, 93% in absence of substrate
hexane
-
enzyme activity is markedly reduced at concentrations of hexane below 5% and over 30%
additional information
-
effects of a range of solvents on the biocatalytic properties of the biocatalyst, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hexane
-
enzyme activity is highest at concentrations of hexane between 5% and 30%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.25
2-Octanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.8
2-phenylcyclohexanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
1000
Cyclopentanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.0007
NADPH
-
pH 8.0, 30°C, recombinant mutant H220A; pH 8.0, 30°C, recombinant wild-type PAMO
0.0017
NADPH
-
pH 8.0, 30°C, recombinant mutant H220Q; pH 8.0, 30°C, recombinant mutant H220T
0.011
NADPH
-
pH 8.0, 30°C, recombinant mutant H220Q/K336H; pH 8.0, 30°C, recombinant mutant K336H
0.04
phenylacetone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.28
phenylacetone
-
25°C, pH 8.5, in the presence of 0.006 mM bovine serum albumin
additional information
additional information
-
detailed steady-state and pre-steady-state kinetic analysis of the reductive and the oxidative half-reaction of wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state kinetics with NADPH and NADH cofactors, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Thermobifida fusca
-
all substrates show a turnover between 1.2 s-1 and 3.6 s-1
-
2.3
2-Octanone
Thermobifida fusca
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.3
2-phenylcyclohexanone
Thermobifida fusca
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
1.6
Cyclopentanone
Thermobifida fusca
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.8
NADPH
Thermobifida fusca
-
pH 8.0, 30°C, recombinant mutant H220W; pH 8.0, 30°C, recombinant mutant R217L
1.2
NADPH
Thermobifida fusca
-
pH 8.0, 30°C, recombinant mutant H220D; pH 8.0, 30°C, recombinant mutant H220E; pH 8.0, 30°C, recombinant mutant K336H
1.9
NADPH
Thermobifida fusca
-
pH 8.0, 30°C, recombinant mutant H220F; pH 8.0, 30°C, recombinant mutant H220Q/K336H
0.26
phenylacetone
Mycobacterium tuberculosis
-
25°C, pH 8.5, in the presence of 0.006 mM bovine serum albumin
1.4
phenylacetone
Thermobifida fusca
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.2
2-Octanone
Thermobifida fusca
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
5474
0.37
2-phenylcyclohexanone
Thermobifida fusca
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
4760
1.6
Cyclopentanone
Thermobifida fusca
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
2478
7
NADPH
Thermobifida fusca
-
pH 8.0, 30°C, recombinant mutant H220E; pH 8.0, 30°C, recombinant mutant R217A
5
35
phenylacetone
Thermobifida fusca
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
3713
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
catalytic efficiency of wild-type and mutant PAMO in in vitro catalysis with two-liquid phases, overview
additional information
-
substrate specificity, diverse substrates, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
-
pH profile, and dependence of the enantioselectivity of the reaction, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 58
-
at 58C 75% of enzyme activity remains, at 60C activity is nearly zero, at 45C enzyme is fully active
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65000
-
1 * 65000, SDS-PAGE, small amount of approx. 7% is present as a dimer
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 65000, SDS-PAGE, small amount of approx. 7% is present as a dimer
additional information
additional information
-
structure analysis, the enzyme exhibits a two-domain architecture, and a bulge loop region
additional information
-
model of the three-dimensional structure of PAMO, overview
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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
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52
-
50% loss of activity after 24 h and 48 h in the absence and presence of FAD, respectively
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PAMO that has been activated at 50°C can be stored for several days at room temperature without any loss in activity
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli
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recombinant His-tagged wild-type and mutant PAMOs from Escherichia coli strain TOP10 by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
BVMO gene, functional expression in Escherichia coli strains JM109 and BL21(DE3) as soluble protein
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expression in Escherichia coli
expression of His-tagged wild-type and mutant enzymes in Escherichia coli
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expression of His-tagged wild-type and mutant PAMOs in Escherichia coli strain TOP10
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A435Y
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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
H220E
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site-directed mutagenesis, H220E mutant performs worse than wild-type PAMO with both coenzymes NADPH and NADH
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
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
M446G
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
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higher subtrate variability, temperature optimum at 50C with range from 45-56C
P440T
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higher subtrate variability, temperature optimum at 50C with range from 45-56C
P440Y
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higher subtrate variability, temperature optimum at 50C with range from 45-58C
Q93W/S441A/A442G/S444C/M446G/L447P
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the mutant shows 40% of wild type activity
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/A442G/S444C/M446G/L447P
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the mutant shows 41% 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
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the mutant shows reduced activity compared to the wild type enzyme
additional information
M446G
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the mutant shows 49% of wild type activity and is able to convert 1-indanone to 1-isochromanone
M446G
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the mutant retains wild type thermostability and produces an altered substrate binding pocket, leading to substantial changes in substrate specificity and enantioselectivity towards sulfides and ketones
additional information
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construction of three mutants P1-P3 by elimination of a bulge loop region, involving residues Ser441, Ala442, and Leu443, leading to enhanced substrate enantioselectivity of Baeyer-Villiger reactions while maintaining high thermal stability, overview
additional information
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engineering of three highly stereoselective mutants of the thermally stable phenylacetone monooxygenase as practical catalysts for enantioselective Baeyer-Villiger oxidations of several ketones on a preparative scale under in vitro conditions, optimization of the method including a coupled cofactor-regeneration system, reaction mechanism, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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the thermally stable phenylacetone monooxygenase and engineered mutants can be used as a practical catalysts for enantioselective Baeyer-Villiger oxidations of several ketones on a preparative scale under in vitro conditions, overview
synthesis
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usage of the enzyme for asymmetric sulfooxidation of thioanisole and of racemic 2-phenylpropionaldehyde in a Baeyer-Villiger oxidation reaction
synthesis
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the enzyme is useful for kinetic resolution of a set of racemic substituted 3-phenylbutan-2-ones and synthesis of enantiopure compounds, overview
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.92)
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