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(2-methylphenyl)acetone + NADPH + O2
? + NADP+ + O2
-
-
-
-
?
(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
-
-
?
(S)-nicotine + NADPH + O2
?
-
-
-
-
?
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-benzylcyclopentanone + NADPH + H+ + O2
?
-
about 10% conversion
-
-
?
2-decanone + NADPH + O2
? + NADP+ + H2O
2-decanone + NADPH + O2
methyl nonanoate + octyl acetate + NADP+ + H2O
-
-
-
-
?
2-dodecanone + NADPH + O2
? + NADP+
-
-
-
-
?
2-dodecanone + NADPH + O2
? + NADP+ + H2O
2-dodecanone + NADPH + O2
nonyl acetate + methyl decanoate + NADP+ + H2O
-
-
-
-
?
2-heptanone + NADPH + O2
pentyl acetate + NADP+ + H2O
-
-
-
-
?
2-hexanone + NADPH + O2
butyl acetate + 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-nonanone + NADPH + H+ + O2
?
-
less than 40% conversion
-
-
?
2-nonanone + NADPH + O2
? + NADP+ + H2O
2-octanone + NADPH + H+ + O2
?
-
-
-
-
?
2-octanone + NADPH + H+ + O2
? + NADP+ + H2O
-
-
-
-
?
2-octanone + NADPH + O2
heptyl acetate + NADP+ + H2O
-
-
-
-
?
2-phenylcyclohexanone + NADPH + H+ + O2
?
-
-
-
-
?
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
-
-
?
2-phenylpropionaldehyde + NADPH + H+ + O2
?
-
-
-
-
?
2-undecanone + NADPH + O2
? + NADP+ + H2O
-
-
-
-
?
3-(3-trifluoromethylphenyl)butan-2-one + NADPH + H+ + O2
?
-
enantioselective reaction
-
-
?
3-(4-chlorophenyl)cyclobutanone + NADPH + H+ + O2
?
-
about 40% conversion
-
-
?
3-benzylcyclobutanone + NADPH + H+ + O2
?
-
about 45% conversion
-
-
?
3-decanone + NADPH + O2
? + NADP+ + H2O
-
-
-
-
?
3-octanone + NADPH + H+ + O2
?
-
-
-
-
?
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-phenylcyclobutanone + NADPH + H+ + O2
?
-
about 70% conversion
-
-
?
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-decanone + NADPH + O2
? + NADP+ + H2O
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
-
?
benzocyclobutanone + NADPH + O2
2-coumaranone + NADP+ + H2O
benzylacetone + NADPH + O2
?
-
low activity
-
-
?
benzylacetone + NADPH + O2
? + NADP+ + H2O
bicyclohept-2-en-6-one + NADPH + O2
3-oxabicyclo[3.3.0]oct-6-en-2-one + NADP+ + H2O
-
-
-
-
?
bicyclohept-2-en-6-one + NADPH + O2
? + NADP+ + O2
-
-
-
-
?
bicyclo[2.2.1]heptan-2-one + NADPH + H+ + O2
?
-
about 5% conversion
-
-
?
bicyclo[3.2.0]hept-2-en-6-one + NADPH + H+ + O2
?
-
-
-
-
?
cyclohexanone + NADPH + H+ + O2
?
-
-
-
-
?
cyclohexanone + NADPH + H+ + O2
epsilon-caprolactone + NADP+ + H2O
-
substrate of enzyme mutants, not of wild-type, overview
-
-
?
cyclopentanone + NADPH + H+ + O2
?
-
-
-
-
?
diketone + NADPH + O2
(R)-1-acetoxy-phenylacetone + NADP+ + H2O
-
-
-
-
?
ethionamide + NADPH + O2
? + NADP+ + H2O
-
-
-
-
?
ethionamide + NADPH + O2
? + NADP+ + O2
-
-
-
-
?
methyl 4-tolylsulfide + NADPH + O2
? + NADP+ + O2
-
-
-
-
?
methyl-p-tolylsulfide + NADPH + O2
? + NADP+ + H2O
-
-
-
-
?
N,N-dimethylbenzylamine + NADPH + O2
N,N-dimethylbenzylamine N-oxide + NADP+ + H2O
-
-
-
-
?
phenylacetone + NADPH + H+ + O2
benzyl acetate + NADP+ + H2O
phenylacetone + NADPH + O2
benzyl acetate + NADP+ + H2O
phenylboronic acid + NADPH + O2
?
-
formation of phenol
-
-
?
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
?
thioanisole + NADPH + H+ + O2
methyl phenyl sulfoxide + NADP+ + H2O
-
-
-
-
?
thioanisole + NADPH + H+ + O2
thioanisole sulfoxide + NADP+ + H2O
-
enantioselective reaction
mainly (R)-sulfoxide
-
?
additional information
?
-
2-decanone + NADPH + O2

? + NADP+ + H2O
-
-
-
-
?
2-decanone + NADPH + O2
? + NADP+ + H2O
-
-
-
-
?
2-dodecanone + NADPH + O2

? + NADP+ + H2O
-
-
-
-
?
2-dodecanone + NADPH + O2
? + NADP+ + H2O
-
-
-
-
?
2-nonanone + NADPH + O2

? + NADP+ + H2O
-
-
-
-
?
2-nonanone + NADPH + O2
? + NADP+ + H2O
-
-
-
-
?
4-decanone + NADPH + O2

? + NADP+ + H2O
-
-
-
-
?
4-decanone + NADPH + O2
? + NADP+ + H2O
-
best substrate
-
-
?
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
-
-
?
benzylacetone + NADPH + O2

? + NADP+ + H2O
-
-
-
-
?
benzylacetone + NADPH + O2
? + 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
-
-
671189, 675467, 677171, 684245, 685231, 690110, 726716, 726793, 727379, 728163, 728164, 744548, 745991 -
-
?
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

?
-
-
-
-
?
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 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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0.83
(2-methylphenyl)acetone
-
30°C, pH 7.5, 0.1 mM NADPH
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
0.266 - 0.698
cyclohexanone
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
additional information
additional information
-
0.2
2-dodecanone

-
25°C, pH 8.5
0.26
2-dodecanone
-
30°C, pH 7.5, 0.1 mM NADPH
0.25
2-Octanone

-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
2
2-Octanone
-
wild type enzyme, at pH 7.5 and 37°C
0.07
2-phenylcyclohexanone

-
mutant P3
0.5
2-phenylcyclohexanone
-
mutant P2
0.8
2-phenylcyclohexanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
2.3
2-phenylcyclohexanone
-
mutant P1
4
2-phenylcyclohexanone
-
wild type enzyme, at pH 7.5 and 37°C
0.36
benzylacetone

-
30°C, pH 7.5, 0.1 mM NADPH
0.52
benzylacetone
-
25°C, pH 8.5
0.266
cyclohexanone

-
pH 8.0, 25°C, recombinant mutant S441G/A442P/L443T/S444Q
0.698
cyclohexanone
-
pH 8.0, 25°C, recombinant mutant A442P/L443V
1000
Cyclopentanone

-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
1200
Cyclopentanone
-
wild type enzyme, at pH 7.5 and 37°C
0.0006
NADPH

-
pH 8.0, 30°C, recombinant mutant H220N
0.0007
NADPH
-
pH 8.0, 30°C, recombinant mutant H220A; pH 8.0, 30°C, recombinant wild-type PAMO
0.0007
NADPH
-
at pH 9.0 and 20°C
0.0011
NADPH
-
pH 8.0, 30°C, recombinant mutant K336N
0.0014
NADPH
-
pH 8.0, 30°C, recombinant mutant T218A
0.0017
NADPH
-
pH 8.0, 30°C, recombinant mutant H220Q; pH 8.0, 30°C, recombinant mutant H220T
0.0023
NADPH
-
pH 8.0, 30°C, recombinant mutant H220W
0.0024
NADPH
-
pH 8.0, 30°C, recombinant mutant H220Q/K336N
0.011
NADPH
-
pH 8.0, 30°C, recombinant mutant H220Q/K336H; pH 8.0, 30°C, recombinant mutant K336H
0.02
NADPH
-
pH 8.0, 30°C, recombinant mutant H220F
0.036
NADPH
-
pH 8.0, 30°C, recombinant mutant H220D
0.17
NADPH
-
pH 8.0, 30°C, recombinant mutant H220E
0.32
NADPH
-
pH 8.0, 30°C, recombinant mutant R217A
0.85
NADPH
-
pH 8.0, 30°C, recombinant mutant R217L
0.04
phenylacetone

-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.059
phenylacetone
-
30°C, pH 7.5, 0.1 mM NADPH
0.059
phenylacetone
-
wild-type enzyme
0.061
phenylacetone
-
25°C, pH 8.5
0.08
phenylacetone
-
wild type enzyme, 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
2.5
phenylacetone
-
mutant P3
3
phenylacetone
-
mutant P1
4
phenylacetone
-
mutant P2
additional information
additional information

-
steady-state 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
-
steady-state kinetics with NADPH and NADH cofactors, overview
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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2
(2-methylphenyl)acetone
-
30°C, pH 7.5, 0.1 mM NADPH
0.023 - 0.23
2-dodecanone
0.07 - 0.5
2-phenylcyclohexanone
0.34
4-hydroxyacetophenone
-
30°C, pH 7.5, 0.1 mM NADPH
0.021 - 1.8
benzylacetone
1.1
bicyclohept-2-en-6-one
-
30°C, pH 7.5, 0.1 mM NADPH
0.156 - 0.304
cyclohexanone
0.027
Ethionamide
-
25°C, pH 8.5
2.1
methyl 4-tolylsulfide
-
30°C, pH 7.5, 0.1 mM NADPH
additional information
additional information
-
all substrates show a turnover between 1.2 s-1 and 3.6 s-1
-
0.023
2-dodecanone

-
25°C, pH 8.5
0.23
2-dodecanone
-
30°C, pH 7.5, 0.1 mM NADPH
1
2-Octanone

-
wild type enzyme, at pH 7.5 and 37°C
2.3
2-Octanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.07
2-phenylcyclohexanone

-
wild type enzyme, at pH 7.5 and 37°C
0.25
2-phenylcyclohexanone
-
mutant P3
0.3
2-phenylcyclohexanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.31
2-phenylcyclohexanone
-
mutant P1
0.5
2-phenylcyclohexanone
-
mutant P2
0.021
benzylacetone

-
25°C, pH 8.5
1.8
benzylacetone
-
30°C, pH 7.5, 0.1 mM NADPH
0.156
cyclohexanone

-
pH 8.0, 25°C, recombinant mutant S441G/A442P/L443T/S444Q
0.304
cyclohexanone
-
pH 8.0, 25°C, recombinant mutant A442P/L443V
0.9
Cyclopentanone

-
wild type enzyme, at pH 7.5 and 37°C
1.6
Cyclopentanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.8
NADPH

-
pH 8.0, 30°C, recombinant mutant H220W; pH 8.0, 30°C, recombinant mutant R217L
1
NADPH
-
pH 8.0, 30°C, recombinant mutant H220Q/K336N
1.2
NADPH
-
pH 8.0, 30°C, recombinant mutant H220D; pH 8.0, 30°C, recombinant mutant H220E; pH 8.0, 30°C, recombinant mutant K336H
1.6
NADPH
-
pH 8.0, 30°C, recombinant mutant K336N
1.9
NADPH
-
pH 8.0, 30°C, recombinant mutant H220F; pH 8.0, 30°C, recombinant mutant H220Q/K336H
2.2
NADPH
-
pH 8.0, 30°C, recombinant mutant R217A
2.7
NADPH
-
pH 8.0, 30°C, recombinant mutant H220Q
2.9
NADPH
-
pH 8.0, 30°C, recombinant mutant H220T
3.1
NADPH
-
pH 8.0, 30°C, recombinant wild-type PAMO
3.3
NADPH
-
pH 8.0, 30°C, recombinant mutant H220A
3.6
NADPH
-
pH 8.0, 30°C, recombinant mutant H220N
3.8
NADPH
-
pH 8.0, 30°C, recombinant mutant T218A
0.017
phenylacetone

-
25°C, pH 8.5
0.22
phenylacetone
-
mutant P3
0.25
phenylacetone
-
mutant P1
0.26
phenylacetone
-
25°C, pH 8.5, in the presence of 0.006 mM bovine serum albumin
0.4
phenylacetone
-
mutant P2
1.4
phenylacetone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
1.9
phenylacetone
-
30°C, pH 7.5, 0.1 mM NADPH
1.9
phenylacetone
-
wild-type enzyme
3
phenylacetone
-
wild type enzyme, at pH 7.5 and 37°C
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0.008 - 0.37
2-phenylcyclohexanone
0.436 - 0.577
cyclohexanone
0.48
2-Octanone

-
wild type enzyme, at pH 7.5 and 37°C
9.2
2-Octanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.008
2-phenylcyclohexanone

-
wild type enzyme, at pH 7.5 and 37°C
0.37
2-phenylcyclohexanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.436
cyclohexanone

-
pH 8.0, 25°C, recombinant mutant A442P/L443V
0.577
cyclohexanone
-
pH 8.0, 25°C, recombinant mutant S441G/A442P/L443T/S444Q
0.8
Cyclopentanone

-
wild type enzyme, at pH 7.5 and 37°C
1.6
Cyclopentanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
1
NADPH

-
pH 8.0, 30°C, recombinant mutant R217L
7
NADPH
-
pH 8.0, 30°C, recombinant mutant H220E; pH 8.0, 30°C, recombinant mutant R217A
33
NADPH
-
pH 8.0, 30°C, recombinant mutant H220D
95
NADPH
-
pH 8.0, 30°C, recombinant mutant H220F
110
NADPH
-
pH 8.0, 30°C, recombinant mutant K336H
170
NADPH
-
pH 8.0, 30°C, recombinant mutant H220Q/K336H
300
NADPH
-
pH 8.0, 30°C, recombinant mutant H220W
420
NADPH
-
pH 8.0, 30°C, recombinant mutant H220Q/K336N
1500
NADPH
-
pH 8.0, 30°C, recombinant mutant K336N
1600
NADPH
-
pH 8.0, 30°C, recombinant mutant H220Q
1700
NADPH
-
pH 8.0, 30°C, recombinant mutant H220T
2700
NADPH
-
pH 8.0, 30°C, recombinant mutant T218A
4000
NADPH
-
pH 8.0, 30°C, recombinant wild-type PAMO
5000
NADPH
-
pH 8.0, 30°C, recombinant mutant H220A
6000
NADPH
-
pH 8.0, 30°C, recombinant mutant H220N
35
phenylacetone

-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
37.5
phenylacetone
-
wild type enzyme, at pH 7.5 and 37°C
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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
-
the mutant shows 75% of wild type activity
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
C65V
-
the mutant shows 94% of wild type activity
C65V/I67T
-
the mutant shows 47% of wild type activity
C65V/I67T/Q152F/S441A/A442G
-
the mutant shows 31% of wild type activity
C65V/I67T/Q93W
-
the mutant shows 54% of wild type activity
H220A
-
site-directed mutagenesis
H220D
-
site-directed mutagenesis
H220E
-
site-directed mutagenesis, H220E mutant performs worse than wild-type PAMO with both coenzymes NADPH and NADH
H220F
-
site-directed mutagenesis
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
H220Q/K336H
-
site-directed mutagenesis
H220Q/K336N
-
site-directed mutagenesis
H220T
-
site-directed mutagenesis
H220W
-
site-directed mutagenesis
I339S
-
the mutant shows 81% of wild type activity
I67T
-
the mutant shows 16% of wild type activity
I67T/L338P
-
the mutant shows less than 3% of wild type activity
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
K336H
-
site-directed mutagenesis
K336N
-
site-directed mutagenesis
L153G
-
inactive; the mutant shows less than 3% of wild type activity
L338P
-
the mutant shows 59% of wild type activity
L443F
-
the mutant shows 65% of wild type activity
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
-
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; 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
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
L447P
-
the mutant shows 85% of wild type activity
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
Q152F
-
the mutant shows 35% of wild type activity
Q152F/A442G
-
the mutant shows 37% of wild type activity
Q152F/S441A/A442G
-
the mutant shows 33% of wild type activity
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
-
the mutant shows 65% of wild type activity
Q93W/A442G/S444C/M446G/L447P
-
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
-
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
-
the mutant shows 73% of wild type activity
S441A/A442G
-
the mutant shows 56% of wild type activity
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
S444C
-
the mutant shows 66% of wild type activity
T218A
-
site-directed mutagenesis
V54I
-
the mutant shows 65% of wild type activity
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
M446G

-
enzyme has altered activity and substrate specificity
M446G
-
the mutant shows 49% of wild type activity and is able to convert 1-indanone to 1-isochromanone
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
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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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