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Information on EC 1.14.13.92 - phenylacetone monooxygenase
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1.14.13.92 phenylacetone monooxygenaseIUBMB Comments
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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Word Map
- 1.14.13.92
-
baeyer-villiger
-
scope
-
enantioselectivity
- ketone
-
bvmos
-
thermobifida
- fusca
- cyclohexanone
-
biocatalytic
- synthesis
-
sulfoxidations
-
biocatalyst
- cyclopentanone
-
quadruple
The enzyme appears in viruses and cellular organisms
Synonyms
pamo, phenylacetone monooxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Baeyer-Villiger monooxygenase
BVMO
M-PAMO
-
mutant M446G of phenylacetone monooxygenase, phenylacetone monooxygenase mutein
PAMO
additional information
PAMO
-
-
additional information
-
the enzyme belongs to the Baeyer-Villiger monooxygenases
additional information
-
the enzyme belongs to the Baeyer-Villiger monooxygenases
additional information
-
the enzyme belongs to the Baeyer-Villiger monooxygenases
additional information
-
the enzyme belongs to the Baeyer-Villiger monooxygenases
additional information
-
the enzyme belongs to the Baeyer-Villiger monooxygenases, BVMOs
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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
-
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
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
-
phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O
catalytic mechanism, via C4a-peroxyflavin and Criegee intermediates, of phenylacetone monooxygenases for the native substrate phenylacetone as well as for a linear non-native substrate 2-octanone, using molecular dynamics simulations, quantum mechanics and quantum mechanics/molecular mechanics calculations, and theoretical basis for the preference of the enzyme for the native aromatic substrate over non-native linear substrates, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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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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
-
?
cyclohexanone + NADPH + H+ + O2
epsilon-caprolactone + NADP+ + H2O
substrate of enzyme mutants, not of wild-type, overview
-
?
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
-
-
?
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
?
-
-
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 aqueous–organic 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
-
?
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 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
phenylacetone + NADPH + H+ + O2
benzyl acetate + NADP+ + H2O
-
-
-
-
?
phenylacetone + NADPH + H+ + O2
benzyl acetate + NADP+ + H2O
-
-
-
?
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
-
-
?
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
-
-
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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INHIBITOR
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
0.266
cyclohexanone
pH 8.0, 25°C, recombinant mutant S441G/A442P/L443T/S444Q
1000
Cyclopentanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
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
Michaelis-Menten kinetics
-
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
-
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
-
all substrates show a turnover between 1.2 s-1 and 3.6 s-1
-
2.3
2-Octanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.3
2-phenylcyclohexanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.156
cyclohexanone
pH 8.0, 25°C, recombinant mutant S441G/A442P/L443T/S444Q
1.6
Cyclopentanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.26
phenylacetone
-
25°C, pH 8.5, in the presence of 0.006 mM bovine serum albumin
1.4
phenylacetone
-
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
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.37
2-phenylcyclohexanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.577
cyclohexanone
pH 8.0, 25°C, recombinant mutant S441G/A442P/L443T/S444Q
1.6
Cyclopentanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
35
phenylacetone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
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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
7.5
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
phenylacetone monooxygenase is the most stable and thermo-tolerant member of the Baeyer-Villiger monooxygenase family
additional information
molecular dynamics simulations and induced fit docking of wild-type and mutant enzymes with cyclohexanone
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Thermobifida fusca (strain YX)
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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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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 65000, SDS-PAGE, small amount of approx. 7% is present as a dimer
additional information
additional information
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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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A435Y
A442P
random/saturation mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 81% conversion rate
A442P/ L443I/S444Q
random and site-directed mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 43% conversion rate
A442P/ L443V/S444Q
random and site-directed mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 45% conversion rate
A442P/L443I
random/saturation mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 45% conversion rate
A442P/L443L/S444Q
random and site-directed mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 41% conversion rate
A442P/L443T/S444Q
random and site-directed mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 56% conversion rate
A442P/L443V
random/saturation mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 90% conversion rate
A442P/L443W
random/saturation mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 74% conversion rate
A442P/L443W/ S444Q
random and site-directed mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 33% conversion rate
H220E
-
site-directed mutagenesis, H220E mutant performs worse than wild-type PAMO with both coenzymes NADPH and NADH
H220N
-
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
-
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
-
the mutant shows less than 3% of wild type activity
I67T/L338P/A435Y/A442G/L443F/S444C
-
the mutant shows less than 3% of wild type activity
L153G
L443V
random/saturation mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 53% conversion rate
L443V/S444M
random/saturation mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 53% conversion rate
L443V/S444Q
L443V/S444T
random/saturation mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 57% conversion rate
M446G
P253F/G254A/R258M/L443F
-
the mutant shows the same thermostability as the wild type enzyme while it displays an extended substrate spectrum
P440F
-
higher subtrate variability, temperature optimum at 50C with range from 45-56C
P440H
-
higher subtrate variability, temperature optimum at 50C with range from 45-56C
P440I
-
higher subtrate variability, temperature optimum at 50C with range from 45-56C
P440L
-
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
Q93N/P94D/P440F
random/saturation mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at low rate
Q93W/S441A/A442G/S444C/M446G/L447P
-
the mutant shows 40% of wild type activity
R337A
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
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
-
the mutant shows 41% of wild type activity
S441D/A442E
random/saturation mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 73% conversion rate
S441G/A442P/L443T/S444Q
site-directed mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at about 90% conversion rate
S441G/A442T
random/saturation mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 48% conversion rate
S441H
random/saturation mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 34% conversion rate
S441H/A442P
random/saturation mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 78% conversion rate
V54I/C65V/I67T/Q93W/I339S/S441A/A442G/S444C/M446G/L447P
-
the mutant shows 5% of wild type activity
V54I/C65V/I67T/Q93W/Q152F/I339S/S441A/A442G/S444C/M446G/L447P
-
the mutant shows less than 3% of wild type activity
V54I/C65V/I67T/Q93W/Q152F/L153G/I339S/S441A/A442G/S444C/M446G/L447P
-
the mutant shows less than 3% of wild type activity
W501A
-
the mutant shows reduced activity compared to the wild type enzyme
additional information
L443V/S444Q
random/saturation mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 40-45% conversion rate
L443V/S444Q
random/saturation mutagenesis, the mutant is active with cyclohexanone, in contrast to the wild-type enzyme, and catalyzes its conversion to epsilon-caprolactone at 59% conversion rate
M446G
-
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
M446G
-
the mutant shows 49% of wild type activity and is able to convert 1-indanone to 1-isochromanone
additional information
-
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
-
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
additional information
directed evolution of phenylacetone monooxygenase as an active catalyst for the Baeyer-Villiger conversion of cyclohexanone to caprolactone using iterative saturation mutagenesis, mutant screening, overview. Molecular dynamics simulations and induced fit docking of wild-type and mutant enzymes with cyclohexanone. The mutants are used in the whole cell system of Escherichia coli cells
additional information
rational engineering of enzyme PAMO for wide applications in industrial biocatalysis, in particular, in the biotransformation of long-chain aliphatic oils into potential biodiesels
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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
recombinant His-tagged wild-type and mutant PAMOs from Escherichia coli strain TOP10 by nickel affinity chromatography
-
recombinant PAMO
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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
expression of His-tagged wild-type and mutant PAMOs in Escherichia coli strain TOP10
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
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
-
the enzyme is useful for kinetic resolution of a set of racemic substituted 3-phenylbutan-2-ones and synthesis of enantiopure compounds, overview
synthesis
usage of the enzyme for asymmetric sulfooxidation of thioanisole and of racemic 2-phenylpropionaldehyde in a Baeyer-Villiger oxidation reaction
synthesis
phenylacetone monooxygenase (PAMO) is an exceptionally robust Baeyer-Villiger monooxygenase, which makes it ideal for potential industrial applications, usage as an active catalyst for the Baeyer-Villiger conversion of cyclohexanone to caprolactone, which is important as monomer in polymer science
synthesis
phenylacetone monooxygenase (PAMO) is the most stable and thermo-tolerant member of the Baeyer-Villiger monooxygenase family, and the engineered enzyme is useful for the synthesis of industrially relevant compounds, in particular, in the biotransformation of long-chain aliphatic oils into potential biodiesels
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fraaije, M.W.; Wu, J.; Heuts, D.P.; van Hellemond, E.W.; Spelberg, J.H.; Janssen, D.B.
Discovery of a thermostable Baeyer-Villiger monooxygenase by genome mining
Appl. Microbiol. Biotechnol.
66
393-400
2005
Thermobifida fusca
brenda
Fraaije, M.W.; Kamerbeek, N.M.; Heidekamp, A.J.; Fortin, R.; Janssen, D.B.
The prodrug activator EtaA from Mycobacterium tuberculosis is a Baeyer-Villiger monooxygenase
J. Biol. Chem.
279
3354-3360
2004
Mycobacterium tuberculosis
brenda
Malito, E.; Alfieri, A.; Fraaije, M.W.; Mattevi, A.
Crystal structure of a Baeyer-Villiger monooxygenase
Proc. Natl. Acad. Sci. USA
101
13157-13162
2004
Thermobifida fusca (Q47PU3), Thermobifida fusca
brenda
Bocola, M.; Schulz, F.; Leca, F.; Vogel, A.; Fraaije, M.W.; Reetz, M.T.
Converting phenylacetone monooxygenase into phenylcyclohexanone monooxygenase by rational design: towards practical Baeyer-Villiger monooxygenases
Adv. Synth. Catal.
347
979-986
2005
Thermobifida fusca
-
brenda
Schulz, F.; Leca, F.; Hollmann, F.; Reetz, M.T.
Towards practical biocatalytic Baeyer-Villiger reactions: applying a thermostable enzyme in the gram-scale synthesis of optically active lactones in a two-liquid-phase system
Beilstein J. Org. Chem.
1
10
2005
Thermobifida fusca
brenda
De Gonzalo, G.; Ottolina, G.; Zambianchi, F.; Fraaije, M.W.; Carrea, G.
Biocatalytic properties of Baeyer-Villiger monooxygenases in aqueous-organic media
J. Mol. Catal. B
39
91-97
2006
Thermobifida fusca
-
brenda
de Gonzalo, G.; Torres Pazmino, D.E.; Ottolina, G.; Fraaije, M.W.; Carrea, G.
Oxidations catalyzed by phenylacetone monooxygenase from Thermobifida fusca
Tetrahedron
16
3077-3083
2005
Thermobifida fusca
-
brenda
Rehdorf, J.; Kirschner, A.; Bornscheuer, U.T.
Cloning, expression and characterization of a Baeyer-Villiger monooxygenase from Pseudomonas putida KT2440
Biotechnol. Lett.
29
1393-1398
2007
Pseudomonas putida, Pseudomonas putida KT 2240
brenda
Zambianchi, F.; Fraaije, M.W.; Carrea, G.; de Gonzalo, G.; Rodriguez, C.; Gotor, V.; Ottolina, G.
Titration and assignment of residues that regulate the enantioselectivity of phenylacetone monooxygenase
Adv. Synth. Catal.
349
1327-1331
2007
Thermobifida fusca (Q47PU3)
-
brenda
Torres Pazmino, D.E.; Baas, B.J.; Janssen, D.B.; Fraaije, M.W.
Kinetic mechanism of phenylacetone monooxygenase from Thermobifida fusca
Biochemistry
47
4082-4093
2008
Thermobifida fusca (Q47PU3), Thermobifida fusca
brenda
Rodriguez, C.; de Gonzalo, G.; Torres Pazmino, D.E.; Fraaije, M.W.; Gotor, V.
Selective Baeyer-Villiger oxidation of racemic ketones in aqueous-organic media catalyzed by phenylacetone monooxygenase
Tetrahedron Asymmetry
19
197-203
2008
Thermobifida fusca
-
brenda
Rioz-Martinez, A.; De Gonzal, D.G.; Torres Pazmino, D.; Fraaije, M.; Gotor, V.
Enzymatic Baeyer-Villiger oxidation of benzo-fused ketones: Formation of regiocomplementary lactones
Eur. J. Org. Chem.
2009
2526-2532
2009
Pseudomonas fluorescens, Thermobifida fusca
-
brenda
Reetz, M.T.; Wu, S.
Laboratory evolution of robust and enantioselective Baeyer-Villiger monooxygenases for asymmetric catalysis
J. Am. Chem. Soc.
131
15424-15432
2009
Thermobifida fusca
brenda
Dudek, H.M.; Torres Pazmino, D.E.; Rodriguez, C.; de Gonzalo, G.; Gotor, V.; Fraaije, M.W.
Investigating the coenzyme specificity of phenylacetone monooxygenase from Thermobifida fusca
Appl. Microbiol. Biotechnol.
88
1135-1143
2010
Thermobifida fusca
brenda
Dudek, H.M.; de Gonzalo, G.; Pazmino, D.E.; Stepniak, P.; Wyrwicz, L.S.; Rychlewski, L.; Fraaije, M.W.
Mapping the substrate binding site of phenylacetone monooxygenase from Thermobifida fusca by mutational analysis
Appl. Environ. Microbiol.
77
5730-5738
2011
Thermobifida fusca
brenda
Dudek, H.M.; Fink, M.J.; Shivange, A.V.; Dennig, A.; Mihovilovic, M.D.; Schwaneberg, U.; Fraaije, M.W.
Extending the substrate scope of a Baeyer-Villiger monooxygenase by multiple-site mutagenesis
Appl. Microbiol. Biotechnol.
98
4009-4020
2013
Thermobifida fusca
brenda
de Gonzalo, G.; Rodriguez, C.; Rioz-Martinez, A.; Gotor, V.
Improvement of the biocatalytic properties of one phenylacetone monooxygenase mutant in hydrophilic organic solvents
Enzyme Microb. Technol.
50
43-49
2012
Thermobifida fusca
brenda
Andrade, L.; Pedrozo, E.; Leite, H.; Brondani, P.
Oxidation of organoselenium compounds. A study of chemoselectivity of phenylacetone monooxygenase
J. Mol. Catal. B
73
63-66
2011
Thermobifida fusca
-
brenda
Rodriguez, C.; De Gonzalo, G.; Gotor, V.
Optimization of oxidative bioconversions catalyzed by phenylacetone monooxygenase from Thermobifida fusca
J. Mol. Catal. B
74
138-143
2012
Thermobifida fusca
-
brenda
Parra, L.P.; Acevedo, J.P.; Reetz, M.T.
Directed evolution of phenylacetone monooxygenase as an active catalyst for the Baeyer-Villiger conversion of cyclohexanone to caprolactone
Biotechnol. Bioeng.
112
1354-1364
2015
Thermobifida fusca (Q47PU3)
brenda
Carvalho, A.T.P.; Dourado, D.F.A.R.; Skvortsov, T.; de Abreu, M.; Ferguson, L.J.; Quinn, D.J.; Moody, T.S.; Huang, M.
Catalytic mechanism of phenylacetone monooxygenases for non-native linear substrates
Phys. Chem. Chem. Phys.
19
26851-26861
2017
Thermobifida fusca (Q47PU3)
brenda
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