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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
- ketone
-
enantioselectivity
-
bvmos
-
thermobifida
-
biocatalytic
- cyclohexanone
- fusca
- synthesis
-
sulfoxidations
-
biocatalyst
- phosphite
- cyclopentanone
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
-
-
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
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
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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 + 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-indanone + NADPH + H+ + 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-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 + 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-methylcyclohexanone + NADPH + H+ + O2
? + NADP+ + H2O
no activity with wild-type PAMO, but low to increased activity with enzyme mutants
-
-
?
2-methylphenylcyclohexanone + NADPH + O2
7-benzyloxepan-2-one + NADP+ + H2O
-
mutant P3 prefers the R-isomer
-
-
?
2-phenylcyclohexanone + NADPH + H+ + O2
? + NADP+ + H2O
very low activity with wild-type PAMO, significantly increased activity with enzyme mutant P253F/G254A/R258M/L443F
-
-
?
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-methylcyclohexanone + NADPH + H+ + O2
? + NADP+ + H2O
no activity with wild-type PAMO, but low to increased activity with enzyme mutants
-
-
?
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
-
-
?
cycloheptanone + NADPH + H+ + O2
? + NADP+ + H2O
no activity with wild-type PAMO, but low to increased activity with enzyme mutants
-
-
?
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
-
-
?
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
-
-
-
?
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
?
-
substrate specificity of wild-type and mutant enzymes, overview
-
-
-
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
-
-
?
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
-
-
?
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
-
-
-
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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
-
-
-
?
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
-
additional information
no detrimental effect of the accumulation of superoxide on biocatalysis is demonstrated
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hexane
-
enzyme activity is highest at concentrations of hexane between 5% and 30%
additional information
glucose does not improve the catalytic conversion by the enzyme
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Urogenital Abnormalities
A single procalcitonin level does not predict adverse outcomes of women with pyelonephritis.
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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
0.25
2-Octanone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C