Any feedback?
Information on EC 1.14.13.92 - phenylacetone monooxygenase and Organism(s) Thermobifida fusca and UniProt Accession Q47PU3
for references in articles please use BRENDA:EC1.14.13.92Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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).
Specify your search results
Word Map
- 1.14.13.92
-
baeyer-villiger
- ketone
-
enantioselectivity
-
bvmos
-
thermobifida
-
biocatalytic
- cyclohexanone
- fusca
- synthesis
-
sulfoxidations
-
biocatalyst
- phosphite
- cyclopentanone
The taxonomic range for the selected organisms is: Thermobifida fusca
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pamo, phenylacetone monooxygenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PAMO
-
M-PAMO
-
mutant M446G of phenylacetone monooxygenase, phenylacetone monooxygenase mutein
PAMO
-
-
additional information
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
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O
the reaction mechanism of BVMO, and particularly PAMO, with native substrate phenylacetone proceeds via the formation of a Criegee intermediate with anionic character, which is subsequently rearranged via the migration of alkyl group to yield the product ester, reaction mechanism, overview. Modeling of the reaction intermediate C4a-peroxyflavin
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
phenylacetone,NADPH:oxygen oxidoreductase
A flavoprotein (FAD). NADH cannot replace NADPH as coenzyme. In addition to phenylacetone, which is the best substrate found to date, this Baeyer-Villiger monooxygenase can oxidize other aromatic ketones [1-(4-hydroxyphenyl)propan-2-one, 1-(4-hydroxyphenyl)propan-2-one and 3-phenylbutan-2-one], some alipatic ketones (e.g. dodecan-2-one) and sulfides (e.g. 1-methyl-4-(methylsulfanyl)benzene).
CAS REGISTRY NUMBER
COMMENTARY
1005768-90-0
-
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
2-methylcyclohexanone + NADPH + H+ + O2
? + NADP+ + H2O
no activity with wild-type PAMO, but low to increased activity with enzyme mutants
-
-
?
2-phenylcyclohexanone + NADPH + H+ + O2
? + NADP+ + H2O
very low activity with wild-type PAMO, significantly increased activity with enzyme mutant P253F/G254A/R258M/L443F
-
-
?
4-methylcyclohexanone + NADPH + H+ + O2
? + NADP+ + H2O
no activity with wild-type PAMO, but low to increased activity with enzyme mutants
-
-
?
cycloheptanone + NADPH + H+ + O2
? + NADP+ + H2O
no activity with wild-type PAMO, but low to increased activity with enzyme mutants
-
-
?
thioanisole + NADPH + H+ + O2
?
the asymmetric oxidation of thioanisole to sulfoxide is accompanied by the overoxidation to achiral sulfone
-
-
?
(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-indanone + NADPH + H+ + O2
1-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-[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-indanone + NADPH + H+ + O2
3-isochromanone + 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-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-hydroxyacetophenone + NADPH + O2
acetic acid 4-hydroxyphenyl ester + NADP+ + O2
-
-
-
-
?
4-phenylcyclohexanone + NADPH + O2
4-phenyl-hexano-6-lactone + NADP+ + H2O
-
-
-
-
?
alpha-acetylphenylacetonitrile + NADPH + H+ + O2
(R)-2-acetoxyphenylacetonitrile + NADP+ + H2O
-
enantioselective reaction
enantiopure product formation
-
?
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
-
-
?
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
-
-
-
-
?
phenylacetone + NADPH + H+ + O2
benzyl acetate + 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
-
?
cyclohexanone + NADPH + H+ + O2
epsilon-caprolactone + NADP+ + H2O
substrate of enzyme mutants, not of wild-type, overview
-
-
?
cyclohexanone + NADPH + H+ + O2
epsilon-caprolactone + NADP+ + H2O
no activity with wild-type PAMO, but low to increased activity with enzyme mutants
-
-
?
cyclopentanone + NADPH + H+ + O2
5-valerolactone + NADP+ + H2O
-
-
-
?
cyclopentanone + NADPH + H+ + O2
5-valerolactone + NADP+ + H2O
very low activity with wild-type PAMO, significantly increased activity with enzyme mutant P253F/G254A/R258M/L443F
-
-
?
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 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
-
-
?
additional information
?
-
substrate specificity of wild-type and mutant enzymes, 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
?
-
binding of cyclopentanone and 2-phenylcyclohexanone, which are the typical substrates of CPMO in group I and CHMO in group III, respectively, is analyzed with wild-type and mutant PAMO enzymes. Substrate binding analysis, overview. Residue R337 establishes a cationn-i interaction with the substrate
-
-
-
additional information
?
-
for wild-type TfPAMO, the uncoupling side activity at different pHs ranges from 5.0 to 7.8%. Formation of hydrogen peroxide is rather constant (around 4.0 microM), while formation of superoxide is almost absent at low pH of 6.0, reaching 3.0 microM at high pH of 9.0-10.0
-
-
-
additional information
?
-
the enzyme produces H2O2 in a side uncoupling reaction. The enzyme access tunnels, which may serve as exit paths for H2O2 from the active site to the bulk, are predicted by using the CAVER and/or protein energy landscape exploration (PELE) software for the phenylacetone monooxygenase variant (PAMO_C65D) from Thermobifida fusca. The simplified mechanism of flavin-dependent monooxygenases (e.g. BVMOs) consists of NAD(P)H-dependent reduction of the flavin prosthetic group, followed by activation of molecular oxygen as a (hydro)peroxyflavin, and substrate oxygenation. The catalytic cycle is closed after elimination of water and reformation of the oxidized flavin. Alternatively, the (hydro)peroxyflavin can eliminate H2O2 spontaneously (uncoupling reaction) into the oxidized flavin
-
-
-
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
?
-
-
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
-
-
?
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
-
-
-
?
phenylacetone + NADPH + H+ + O2
benzyl acetate + NADP+ + H2O
-
-
-
?
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
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
additional information
no detrimental effect of the accumulation of superoxide on biocatalysis is demonstrated
-
additional information
-
effects of a range of solvents on the biocatalytic properties of the biocatalyst, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
glucose does not improve the catalytic conversion by the enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.25
2-Octanone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
0.8
2-phenylcyclohexanone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
44
2-phenylcyclohexanone
recombinant wild-type enzyme, pH 7.4, 25°C
0.266
cyclohexanone
pH 8.0, 25°C, recombinant mutant S441G/A442P/L443T/S444Q
1000
Cyclopentanone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
1.4
phenylacetone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
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
0.04
phenylacetone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
steady-state kinetics of wild-type and mutant enzymes
-
additional information
additional information
steady-state kinetics of wild-type and mutant enzymes
-
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 kinetic analysis of wild-type and mutant enzymes
-
additional information
additional information
-
steady-state kinetics with NADPH and NADH cofactors, overview
-
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
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
0.07
2-phenylcyclohexanone
recombinant wild-type enzyme, pH 7.4, 25°C
0.3
2-phenylcyclohexanone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
0.156
cyclohexanone
pH 8.0, 25°C, recombinant mutant S441G/A442P/L443T/S444Q
1.6
Cyclopentanone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
0.04
phenylacetone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
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
1.6
Cyclopentanone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
1.4
phenylacetone
-
mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.2
2-Octanone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
0.0016
2-phenylcyclohexanone
recombinant wild-type enzyme, pH 7.4, 25°C
0.375
2-phenylcyclohexanone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
0.577
cyclohexanone
pH 8.0, 25°C, recombinant mutant S441G/A442P/L443T/S444Q
0.0016
Cyclopentanone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
0.029
phenylacetone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
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
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
pH profile, and dependence of the enantioselectivity of the reaction, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
phenylacetone monooxygenase (PAMO) catalyzes oxidation of ketones with molecular oxygen and NADPH with the formation of esters
additional information
evolution
phenylacetone monooxygenase is the most stable and thermo-tolerant member of the Baeyer-Villiger monooxygenase family
evolution
phenylacetone monooxygenase from Thermobifida fusca (TfPAMO) is a thermostable Baeyer-Villiger monooxygenase from the NAD(P)H/FAD-dependent oxidoreductase family
evolution
phenylacetone monooxygenase, PAMO, is a NADPH-dependent Baeyer-Villiger monooxygenase
evolution
the enzyme belongs to the group II of Baeyer-Villiger monooxygenases (BMVOs)
evolution
the enzyme belongs to the group II of Baeyer-Villiger monooxygenases (BMVOs). The prototype of the BVMO enzyme family is the Thermobifida fusca phenylacetone monooxygenase (PAMO). Phenylacetone monooxygenase is the most stable and thermo-tolerant member of the Baeyer-Villiger monooxygenases family, but it has very limited substrate scope compared with other BVMOs such as CPMO in group I or CHMO in group III
additional information
molecular dynamics simulations and induced fit docking of wild-type and mutant enzymes with cyclohexanone
additional information
construction of an enzyme structure model exhibiting most of the conserved motifs of the BVMOs, including the FAD binding domain, the NADP(H) binding domain, the flexible linkers, and the signature motif, overview
additional information
enzyme molecular docking and molecular dynamics, computational modeling, overview
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65000
-
1 * 65000, SDS-PAGE, small amount of approx. 7% is present as a dimer
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 65000, SDS-PAGE, small amount of approx. 7% is present as a dimer
additional information
additional information
model of the three-dimensional structure of PAMO, overview
additional information
-
structure analysis, the enzyme exhibits a two-domain architecture, and a bulge loop region
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
no posttranslational modification in the PAMO proteins expressed in Escherichia coli cells
additional information
-
no posttranslational modification in the PAMO proteins expressed in Escherichia coli cells
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
C65D
C65D/M446I/Y495I
site-directed mutagenesis, the M446I and Y495I mutations do not have significant influence on the NADPH oxidation activities. The triple mutant, which shows the greatest stability to H2O2, exhibits the highest catalytic activity (kcat) for NADPH oxidation. Thus, the oxidative stability is not markedly related to the NADPH oxidation and H2O2 generation rates
C65D/M446I/Y517I
site-directed mutagenesis, the M446I mutation does not have significant influence on the NADPH oxidation activities. The residual activity of this triple mutant variant remains unchanged during incubation with externally added H2O2. The variant completely loses the catalytic activity after 1 hour when H2O2 is generated in situ from NADPH oxidation. This fast deactivation of the C65D/M446I/Y517I variant leads to oxidation of only 10% of NADPH added. The Y517I mutation in C65D/M446I variant appears to result in blocking of the H2O2 exit and entrance path. The H2O2 generated in the active site might remain there, oxidizing amino acid residues in vicinity of the active site. The low catalytic activity of the C65D/M446I/Y517I variant for NADPH oxidation suggests that the Y517I mutation results in not only blocking of the H2O2 migration path but also modification of the active site structure
I67A
site-directed mutagenesis, the mutant shows no activity with cyclohexanone like the wild-type enzyme
I67A/P440F
site-directed mutagenesis, the mutant shows high activity with cyclohexanone, 95.1% conversion after 4 h
I67C
site-directed mutagenesis, the mutant shows no activity with cyclohexanone like the wild-type enzyme
I67C/P440F
site-directed mutagenesis, the mutant shows high activity with cyclohexanone, 92.4% conversion after 4 h
I67C/P440F/A442F/L443D
site-directed mutagenesis, the mutant shows moderate activity with cyclohexanone
I67C/P440Y
site-directed mutagenesis, the mutant shows moderate activity with cyclohexanone
I67G
site-directed mutagenesis, the mutant shows no activity with cyclohexanone like the wild-type enzyme
I67G/P440F
site-directed mutagenesis, the mutant shows high activity with cyclohexanone, 87.5% conversion after 4 h
I67Y
site-directed mutagenesis, the mutant shows no activity with cyclohexanone like the wild-type enzyme
I67Y/P440F
site-directed mutagenesis, the mutant shows high activity with cyclohexanone, 97.8% conversion after 4 h
I67Y/P440Y
site-directed mutagenesis, the mutant shows high activity with cyclohexanone
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
P253F/G254A/R258M/L443F
site-directed mutagenesis, the engineered mutant quadruple enzyme variant P253F/G254A/R258M/L443F exhibits significantly improved activity towards 2-octanone compared to wild-type. A remarkable movement of L289 is crucial for a reshaping of the active site of the quadruple variant so as to prevent the aliphatic substrate from moving away from the C4a-peroxyflavin, thus enabling it to keep a catalytically relevant pose during the oxygenation process, substrate specificity compared to wild-type
P440F
site-directed mutagenesis, the mutant shows high activity with cyclohexanone, 50.2% conversion after 4 h
P440H
site-directed mutagenesis, the mutant shows low activity with cyclohexanone
P440I
site-directed mutagenesis, the mutant shows low activity with cyclohexanone
P440W
site-directed mutagenesis, the mutant shows high acticity with cyclohexanone
P440Y
site-directed mutagenesis, the mutant shows low activity with cyclohexanone
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
R258A
site-directed mutagenesis, when the substrate 2-octanone binds to the R258A mutant, a significant change in the position of the hexyl tail of the substrate is observed, altered substrate specificity compared to wild-type
R258M
site-directed mutagenesis, the R258M mutation significantly affects pose of 2-octanone, since the hexyl tail moves towards M258, substrate specificity compared to wild-type
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
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
A435Y
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
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
Q93W/S441A/A442G/S444C/M446G/L447P
-
the mutant shows 40% of wild type activity
S441A/A442G/S444C/M446G/L447P
-
the mutant shows 41% 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
additional information
C65D
site-directed mutagenesis, the engineered TfPAMO variant acts as an NADPH oxidase, it shows an extremely high rate of uncoupling compared with the wild-type enzyme. The mutant is not effective in stabilizing the C(4alpha)-peroxyflavin intermediate. For TfPAMO C65D, hydrogen peroxide and superoxide levels are highest at pH 9.0
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
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
additional information
a rational approach is used to improve the robustness of enzymes, in particular, Baeyer-Villiger monooxygenases (BVMOs) against H2O2. The enzyme access tunnels, which may serve as exit paths for H2O2 from the active site to the bulk, are predicted by using the CAVER and/or protein energy landscape exploration (PELE) software for mutant PAMO_C65D from Thermobifida fusca. The amino acid residues, which are susceptible to oxidation by H2O2 (e.g. methionine and tyrosine) and located in vicinity of the predicted H2O2 migration paths, are substituted with less reactive or inert amino acids (e.g. leucine and isoleucine), leading to design of H2O2-resistant enzyme variants
additional information
addition of the dimerization-docking and anchoring domain (RIDD-RIAD) system to the C-terminus of the NADPH-dependent Baeyer-Villiger monooxygenase phenylacetone monooxygenase (PAMO) and the NADPH-regenerating enzyme (phosphite dehydrogenase, PTDH, EC 1.20.1.1) allowing self-assembly based on specific protein-protein interactions between both peptides and allow tuning of the ratio of the targeted enzymes as the RIAD peptide binds to two RIDD peptides. Several RIDD/RIAD-tagged PAMO and PTDH variants are successfully overproduced in Escherichia coli and subsequently purified. Complementary tagged enzymes are mixed and analyzed for their oligomeric state, stability, and activity. Complexes are formed in the case of some specific combinations (PAMORIAD-PTDHRIDD and PAMORIAD/RIAD-PTDHRIDD). These enzyme complexes display similar catalytic activity when compared with the PTDH-PAMO fusion enzyme. The thermostability of PAMO in these complexes is retained while PTDH displays somewhat lower thermostability
additional information
expanding the substrate scope of a thermostable phenylacetone monooxygenase (PAMO) to cyclohexanone by using site-directed mutagenesis. Several mutants are found to be active with cyclohexanone for which wild-type PAMO shows no activity. There is possible additive or cooperative effect existing between I67 and P440. Based on the thermostable PAMO scaffold, a chimeric PAMO-CHMO enzyme mutant is created, which shows no activity on cyclohexanone
additional information
rational engineering of PAMO for wide applications in industrial biocatalysis, in particular, in the biotransformation of long-chain aliphatic oils into potential biodiesels
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
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
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
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by one-step nickel affinity chromatography to near-homogeneity
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type and mutant enzymes in Escherichia coli
gene pamO, recombinant expression of His-tagged enzyme in three different forms (C, N, and L) concerning the position of His-tag in Escherichia coli strain BL21(DE3), the His-tag locates at the N- and C-termini of the enzyme (PAMO N and PAMO C, respectively), PAMO L describes a construct with the His-tag distanced from the enzyme C-terminus with an additional 19-amino acid sequence, the enzyme forms do not show great differences in catalytic activity. No use of the arabinose promoter in the expression system
recombinant 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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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
synthesis
phenylacetone monooxygenase (PAMO) catalyzes oxidation of ketones with molecular oxygen and NADPH with the formation of esters. PAMO demonstrates high catalytic constants in the oxidation of benzylacetone and other structurally similar aromatic ketones and can be used in the synthesis of flavoring substances, since the ester formed by benzylacetone oxidation has a pronounced fruity smell
synthesis
the enzyme is an ideal candidate for the synthesis of industrially relevant ester or lactone compounds. But its limited substrate scope has largely limited its industrial applications. The engineered mutant quadruple enzyme variant P253F/G254A/R258M/L443F exhibits significantly improved activity towards 2-octanone
synthesis
the H2O2-resistant enzyme variants are robust biocatalysts for synthetic applications
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
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
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
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
-
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
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
-
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
-
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)
-
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
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
-
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
-
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
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
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
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
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
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
-
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
-
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)
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)
Gran-Scheuch, A.; Parra, L.; Fraaije, M.
Systematic assessment of uncoupling in flavoprotein oxidases and monooxygenases
ACS Sust. Chem. Eng.
FEHLT
0000
2021
Thermobifida fusca (Q47PU3)
-
Seo, E.; Kim, M.; Park, S.; Park, S.; Oh, D.; Bornscheuer, U.; Park, J.
Enzyme access tunnel engineering in Baeyer-Villiger monooxygenases to improve oxidative stability and biocatalyst performance
Adv. Synth. Catal.
364
555-564
2022
Thermobifida fusca (Q47PU3)
-
Parshin, P.D.; Pometun, A.A.; Martysuk, U.A.; Kleymenov, S.Y.; Atroshenko, D.L.; Pometun, E.V.; Savin, S.S.; Tishkov, V.I.
Effect of His6-tag position on the expression and properties of phenylacetone monooxygenase from Thermobifida fusca
Biochemistry (Moscow)
85
575-582
2020
Thermobifida fusca (Q47PU3), Thermobifida fusca
Purwani, N.N.; Martin, C.; Savino, S.; Fraaije, M.W.
Modular assembly of phosphite dehydrogenase and phenylacetone monooxygenase for tuning cofactor regeneration
Biomolecules
11
905
2021
Thermobifida fusca (Q47PU3)
Yang, G.; Cang, R.; Shen, L.; Xue, F.; Huang, H.; Zhang, Z.
Expanding the substrate scope of phenylacetone monooxygenase from Thermobifida fusca towards cyclohexanone by protein engineering
Catal. Commun.
119
159-163
2019
Thermobifida fusca (Q47PU3)
-
EXTERNAL LINKS (specific for EC-Number 1.14.13.92)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
