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Information on EC 1.14.13.84 - 4-hydroxyacetophenone monooxygenase and Organism(s) Pseudomonas fluorescens and UniProt Accession Q93TJ5
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1.14.13.84 4-hydroxyacetophenone monooxygenaseIUBMB Comments
Contains FAD. The enzyme from Pseudomonas fluorescens ACB catalyses the conversion of a wide range of acetophenone derivatives. Highest activity occurs with compounds bearing an electron-donating substituent at the para position of the aromatic ring . In the absence of substrate, the enzyme can act as an NAD(P)H oxidase (EC 1.6.3.1).
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Word Map
- 1.14.13.84
-
baeyer-villiger
- fluorescens
- ketones
-
bvmos
- acetophenones
- cyclohexanone
-
nadph-dependent
-
biocatalytic
- putida
-
enantioselectivity
- resin
-
base-catalysed
-
stabilised
-
ring-substituted
-
characterise
- fad
- flavoproteins
- synthesis
- 4-fluorophenol
-
fluorophenyl
- fluoride
-
flavin-containing
-
synthons
- 4-fluorocatechol
- sulfides
- lactones
-
fluorinated
-
noncovalent
The taxonomic range for the selected organisms is: Pseudomonas fluorescens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
hapmo, 4-hydroxyacetophenone monooxygenase, arylketone monooxygenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HAPMO
additional information
-
the enzyme is a BaeyerVilliger monooxygenase
HAPMO
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(4-hydroxyphenyl)ethan-1-one + NADPH + H+ + O2 = 4-hydroxyphenyl acetate + NADP+ + H2O
reaction mechanism
-
(4-hydroxyphenyl)ethan-1-one + NADPH + H+ + O2 = 4-hydroxyphenyl acetate + NADP+ + H2O
enantioselectivity
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
(4-hydroxyphenyl)ethan-1-one,NADPH:oxygen oxidoreductase (ester-forming)
Contains FAD. The enzyme from Pseudomonas fluorescens ACB catalyses the conversion of a wide range of acetophenone derivatives. Highest activity occurs with compounds bearing an electron-donating substituent at the para position of the aromatic ring [1]. In the absence of substrate, the enzyme can act as an NAD(P)H oxidase (EC 1.6.3.1).
CAS REGISTRY NUMBER
COMMENTARY
156621-13-5
-
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
(4-hydroxyphenyl)ethan-1-one + NADPH + O2
4-hydroxyphenyl acetate + NADP+ + H2O
1 unit enzyme oxidizes 1 micromol substrate to product per minute at pH 9.0, 25°C in the presence of NADPH
-
-
?
1-indanone + NADPH + H+ + O2
3,4-dihydrocoumarin + NADP+ + H2O
50 mM Tris-HCl, pH 9.0, 20°C, auxiliary enzymatic system (glucose-6-phosphate with glucose-6-phosphate dehydrogenase) is used to regenerate NADPH
after 72 h 26% conversion without cosolvent, with 5% 2-octanole 39% conversion, with 5% hexane 44% conversion, conversion with 5% hexane at pH 8.0 is 39%, at pH 9.0 44%, at pH 10.0 47%, at pH 10.5 21%
-
?
1-tetralone + NADPH + H+ + O2
4,5-dihydro-1-benzoxepin-2(3H)-one + NADP+ + H2O
50 mM Tris-HCl, pH 9.0, 20°C, auxiliary enzymatic system (glucose-6-phosphate with glucose-6-phosphate dehydrogenase) is used to regenerate NADPH
after 96 h only 5% of the expected product conversion without cosolvent, with 5% tBuOMe 7% conversion, with 5% toluene 26% conversion, with 5% 2-octanol 25% conversion, with 5% hexane 15% conversion
-
?
2-indanone + NADPH + H+ + O2
3-isochromanone + NADP+ + H2O
50 mM Tris-HCl, pH 9.0, 20°C, auxiliary enzymatic system (glucose-6-phosphate with glucose-6-phosphate dehydrogenase) is used to regenerate NADPH
after 72 h no product without cosolvent, only with 5% hexane or 5% CH2Cl2 10% conversion
-
?
4-aminoacetophenone + NADPH + H+ + O2
1-(4-aminophenyl)ethanol + NADP+ + H2O
strictly NADPH-dependent
-
?
4-fluoroacetophenone + NADPH + H+ + O2
4-fluorophenyl acetate + NADP+ + H2O
strictly NADPH-dependent, poor substrate
-
?
4-hydroxy-3-methylacetophenone + NADPH + H+ + O2
4-hydroxy-3-methylphenyl acetate + NADP+ + H2O
strictly NADPH-dependent
-
?
4-hydroxybenzaldehyde + NADPH + H+ + O2
?
strictly NADPH-dependent
-
?
4-hydroxypropiophenone + NADPH + H+ + O2
4-hydroxyphenyl propionate + NADP+ + H2O
strictly NADPH-dependent
-
?
4-methoxyacetophenone + NADPH + H+ + O2
4-methoxyphenyl acetate + NADP+ + H2O
strictly NADPH-dependent
-
?
4-methylacetophenone + NADPH + H+ + O2
4-methylphenyl acetate + NADP+ + H2O
strictly NADPH-dependent
-
?
5-bromo-1-indanone + NADPH + H+ + O2
5-bromo-3,4-dihydrochromen-2-one + NADP+ + H2O
50 mM Tris-HCl, pH 9.0, 20°C, auxiliary enzymatic system (glucose-6-phosphate with glucose-6-phosphate dehydrogenase) is used to regenerate NADPH
after 72 h lower activity than towards chlorine derivative, with 5% hexane 52% conversion
-
?
5-chloro-1-indanone + NADPH + H+ + O2
5-chloro-3,4-dihydrochromen-2-one + NADP+ + H2O
50 mM Tris-HCl, pH 9.0, 20°C, auxiliary enzymatic system (glucose-6-phosphate with glucose-6-phosphate dehydrogenase) is used to regenerate NADPH
after 72 h lower conversion without cosolvent than with 5% hexane (87% conversion)
-
?
5-methoxy-1-indanone + NADPH + H+ + O2
5-methoxy-3,4-dihydrochromen-2-one + NADP+ + H2O
50 mM Tris-HCl, pH 9.0, 20°C, auxiliary enzymatic system (glucose-6-phosphate with glucose-6-phosphate dehydrogenase) is used to regenerate NADPH
after 72 h with 5% hexane 32% conversion
-
?
6-chloro-1-indanone + NADPH + H+ + O2
7-chloro-3,4-dihydrochromen-2-one + NADP+ + H2O
50 mM Tris-HCl, pH 9.0, 20°C, auxiliary enzymatic system (glucose-6-phosphate with glucose-6-phosphate dehydrogenase) is used to regenerate NADPH
after 72 h higher conversion without cosolvent than with 5% hexane (56% conversion)
-
?
6-methoxy-1-indanone + NADPH + H+ + O2
6-methoxy-3,4-dihydrochromen-2-one + NADP+ + H2O
50 mM Tris-HCl, pH 9.0, 20°C, auxiliary enzymatic system (glucose-6-phosphate with glucose-6-phosphate dehydrogenase) is used to regenerate NADPH
after 72 h with 5% hexane 32% conversion
-
?
acetophenone + NADPH + H+ + O2
phenyl acetate + NADP+ + H2O
strictly NADPH-dependent
-
?
benzocyclobutanone + NADPH + H+ + O2
coumaranone + NADP+ + H2O
50 mM Tris-HCl, pH 9.0, 20°C, auxiliary enzymatic system (glucose-6-phosphate with glucose-6-phosphate dehydrogenase) is used to regenerate NADPH
after 72 h 87% conversion, with 5% hexane 93% conversion
-
?
1-bromo-indanone + NADPH + H+ + O2
6-bromoisochroman-1-one + NADP+ + H2O
-
substrate is only accepted by phenylacetone monooxygenase of Pseudomonas fluorescens but not 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 is only accepted by phenylacetone monooxygenase of Pseudomonas fluorescens but not 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 + H+ + O2
4,5-dihydro-1-benzoxepin-2(3H)-one + NADP+ + H2O
-
substrate is accepted by phenylacetone monooxygenase of Pseudomonas fluorescens but not of Thermobifida fusca, reaction is performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH
-
-
?
2,4-pentanedione + NADPH + H+ + O2
?
-
very poor substrate
-
?
2-chloro-thioanisole + NADPH + H+ + O2
2-chlorophenyl methyl (S)-sulfoxide + NADP+ + H2O
-
-
96% enantiomeric excess
-
?
2-chloro-thioanisole + NADPH + H+ + O2
2-chlorophenyl methyl sulfoxide + NADP+ + H2O
-
-
-
-
?
2-chloroethyl phenyl sulfide + NADPH + H+ + O2
2-chloroethyl phenyl (S)-sulfoxide + NADP+ + H2O
-
-
81% enantiomeric excess
-
?
2-hydroxyacetophenone + NADPH + H+ + O2
2-hydroxyphenyl acetate + NADP+ + H2O
-
-
-
?
3-chloro-2-butanone + NADPH + H+ + O2
?
-
very poor substrate
-
?
3-chloro-thioanisole + NADPH + H+ + O2
3-chlorophenyl methyl (S)-sulfoxide + NADP+ + H2O
-
-
99% enantiomeric excess
-
?
3-chloro-thioanisole + NADPH + H+ + O2
3-chlorophenyl methyl sulfoxide + NADP+ + H2O
-
-
-
-
?
3-hydroxyacetophenone + NADPH + H+ + O2
3-hydroxyphenyl acetate + NADP+ + H2O
-
-
-
?
4-acetylpyridine + NADPH + H+ + O2
?
-
very poor substrate
-
?
4-amino-thioanisole + NADPH + H+ + O2
4-aminophenyl methyl sulfoxide + NADP+ + H2O
-
-
-
-
?
4-amino-thioanisole + NADPH + H+ + O2
4-[(S)-methylsulfinyl]aniline + NADP+ + H2O
-
-
99% enantiomeric excess
-
?
4-chloro-thioanisole + NADPH + H+ + O2
4-chlorophenyl methyl (S)-sulfoxide + NADP+ + H2O
-
-
96% enantiomeric excess
-
?
4-chloro-thioanisole + NADPH + H+ + O2
4-chlorophenyl methyl sulfoxide + NADP+ + H2O
-
-
-
-
?
4-cyano-thioanisole + NADPH + H+ + O2
4-cyanophenyl methyl sulfoxide + NADP+ + H2O
-
-
-
-
?
4-cyano-thioanisole + NADPH + H+ + O2
4-[(S)-methylsulfinyl]benzonitrile + NADP+ + H2O
-
-
96% enantiomeric excess
-
?
4-hydroxy-3-methylacetophenone + NADPH + H+ + O2
4-hydroxy-3-methylphenyl acetate + NADP+ + H2O
-
-
-
r
4-hydroxyacetophenone + NADH + H+ + O2
4-hydroxyphenyl acetate + NAD+ + H2O
-
700fold preference for NADPH over NADH
-
?
4-methoxy-thioanisole + NADPH + H+ + O2
4-methoxyphenyl methyl (S)-sulfoxide + NADP+ + H2O
-
-
99% enantiomeric excess
-
?
4-methoxy-thioanisole + NADPH + H+ + O2
4-methoxyphenyl methyl sulfoxide + NADP+ + H2O
-
-
-
-
?
4-methyl-thioanisole + NADPH + H+ + O2
4-methylphenyl methyl sulfoxide + NADP+ + H2O
-
-
-
-
?
4-methyl-thioanisole + NADPH + H+ + O2
methyl 4-methylphenyl (S)-sulfoxide + NADP+ + H2O
-
-
99% enantiomeric excess
-
?
4-nitro-thioanisole + NADPH + H+ + O2
4-nitrophenyl methyl sulfoxide + NADP+ + H2O
-
-
-
-
?
4-nitro-thioanisole + NADPH + H+ + O2
methyl 4-nitrophenyl (S)-sulfoxide + NADP+ + H2O
-
-
87% enantiomeric excess
-
?
6-methoxy-1-indanone + NADPH + H+ + O2
? + NADP+ + H2O
-
substrate is only accepted by phenylacetone monooxygenase of Pseudomonas fluorescens but not of Thermobifida fusca, reaction is performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH
-
-
?
benzaldehyde + NADPH + H+ + O2
phenyl formate + NADP+ + H2O
-
-
-
?
benzocyclobutanone + NADPH + H+ + O2
2-coumaranone + NADP+ + H2O
-
reaction is performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH
-
-
?
benzyl 1-methylethyl sulfide + NADPH + H+ + O2
benzyl 1-methylethyl (R)-sulfoxide + NADP+ + H2O
-
-
82% enantiomeric excess
-
?
benzyl butyl sulfide + NADPH + H+ + O2
benzyl butyl (R)-sulfoxide + NADP+ + H2O
-
-
77% enantiomeric excess
-
?
benzyl ethyl sulfide + NADPH + H+ + O2
benzyl ethyl (S)-sulfoxide + NADP+ + H2O
-
-
81% enantiomeric excess
-
?
benzyl methyl sulfide + NADPH + H+ + O2
benzyl methyl (S)-sulfoxide + NADP+ + H2O
-
-
85% enantiomeric excess
-
?
benzyl propyl sulfide + NADPH + H+ + O2
benzyl propyl (R)-sulfoxide + NADP+ + H2O
-
-
65% enantiomeric excess
-
?
bicyclohept-2-en-6-one + NADPH + H+ + O2
?
-
enantioselectivity, preferably converts (1R,5S)-bicyclohept-2-en-6-one with an enantiomeric ratio (E) of 20
-
?
butyl phenyl sulfide + NADPH + H+ + O2
butyl phenyl (S)-sulfoxide + NADP+ + H2O
-
-
71% enantiomeric excess
-
?
butyrophenone + NADPH + H+ + O2
phenyl butyrate + NADP+ + H2O
-
-
-
?
chloromethyl phenyl sulfide + NADPH + H+ + O2
chloromethyl phenyl (R)-sulfoxide + NADP+ + H2O
-
-
76% enantiomeric excess
-
?
cyclopropyl phenyl sulfide + NADPH + H+ + O2
cyclopropyl phenyl (S)-sulfoxide + NADP+ + H2O
-
-
97% enantiomeric excess
-
?
ethenyl phenyl sulfide + NADPH + H+ + O2
ethenyl phenyl (S)-sulfoxide + NADP+ + H2O
-
-
98% enantiomeric excess
-
?
ethyl phenyl sulfide + NADPH + H+ + O2
ethyl phenyl (S)-sulfoxide + NADP+ + H2O
-
-
99% enantiomeric excess
-
?
isobutyrophenone + NADPH + H+ + O2
phenyl isobutyrate + NADP+ + H2O
-
-
-
?
methyl (phenylsulfanyl)methyl ether + NADPH + H+ + O2
methoxymethyl phenyl (R)-sulfoxide + NADP+ + H2O
-
-
98% enantiomeric excess
-
?
methyl 2-phenylethyl sulfide + NADPH + H+ + O2
methyl 2-phenylethyl (R)-sulfoxide + NADP+ + H2O
-
-
51% enantiomeric excess
-
?
methyl 3-phenylpropyl sulfide + NADPH + H+ + O2
methyl 3-phenylpropyl (R)-sulfoxide + NADP+ + H2O
-
-
57% enantiomeric excess
-
?
methyl 4-tolyl sulfide + NADPH + H+ + O2
?
-
enantioselectivity, HAPMO is efficient and highly selective in the asymmetric formation of the corresponding (S)-sulfoxide
-
?
methyl naphthalen-2-yl sulfide + NADPH + H+ + O2
methyl naphthalen-2-yl (S)-sulfoxide + NADP+ + H2O
-
-
95% enantiomeric excess
-
?
methylphenyl sulfide + NADPH + H+ + O2
?
-
enantioselectivity, HAPMO is efficient and highly selective in the asymmetric formation of the corresponding (S)-sulfoxide
-
?
phenyl prop-2-en-1-yl sulfide + NADPH + H+ + O2
phenyl prop-2-en-1-yl (S)-sulfoxide + NADP+ + H2O
-
-
98% enantiomeric excess
-
?
phenyl propyl sulfide + NADPH + H+ + O2
phenyl propyl (S)-sulfoxide + NADP+ + H2O
-
-
97% enantiomeric excess
-
?
phenylacetone + NADPH + H+ + O2
benzyl acetate + NADP+ + H2O
-
reaction is performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH
-
-
?
propiophenone + NADPH + H+ + O2
phenyl propionate + NADP+ + H2O
-
-
-
?
rac-2-methyl-1-indanone + NADPH + H+ + O2
(R)-3-methyl-3,4-dihydrocoumarin + NADP+ + H2O
-
low conversion and selectivity
-
-
?
thioanisole + NADPH + H+ + O2
methyl phenyl (S)-sulfoxide + NADP+ + H2O
-
-
99% enantiomeric excess
-
?
thioanisole + NADPH + H+ + O2
methyl phenyl sulfoxide + NADP+ + H2O
-
-
-
-
?
4-hydroxyacetophenone + NADPH + H+ + O2
4-hydroxyphenyl acetate + NADP+ + H2O
-
-
-
?
4-hydroxyacetophenone + NADPH + H+ + O2
4-hydroxyphenyl acetate + NADP+ + H2O
strictly NADPH-dependent, tight coupling between NADPH oxidation and substrate oxygenation
product is instable
?
4-hydroxyacetophenone + NADPH + H+ + O2
4-hydroxyphenyl acetate + NADP+ + H2O
catalyzes the first step in the degradation of 4-hydroxyacetophenone
-
?
4-hydroxyacetophenone + NADPH + H+ + O2
4-hydroxyphenyl acetate + NADP+ + H2O
the enzyme catalyzes the first committed step in th 4-hydroxyacetophenone catabolism, pathway overview
-
-
?
(4-hydroxyphenyl)ethan-1-one + NADPH + O2
4-hydroxyphenyl acetate + NADP+ + H2O
-
-
-
?
(4-hydroxyphenyl)ethan-1-one + NADPH + O2
4-hydroxyphenyl acetate + NADP+ + H2O
-
-
-
-
?
(4-hydroxyphenyl)ethan-1-one + NADPH + O2
4-hydroxyphenyl acetate + NADP+ + H2O
-
Baeyer-Villiger oxidation, stereospecific reaction, regioselectivity
-
-
?
4-aminoacetophenone + NADPH + H+ + O2
1-(4-aminophenyl)ethanol + NADP+ + H2O
-
-
-
?
4-aminoacetophenone + NADPH + H+ + O2
1-(4-aminophenyl)ethanol + NADP+ + H2O
-
best substrate
-
?
4-fluoroacetophenone + NADPH + H+ + O2
4-fluorophenyl acetate + NADP+ + H2O
-
-
-
?
4-fluoroacetophenone + NADPH + H+ + O2
4-fluorophenyl acetate + NADP+ + H2O
-
-
-
?
4-hydroxyacetophenone + NADPH + H+ + O2
4-hydroxyphenyl acetate + NADP+ + H2O
-
-
-
-
?
4-hydroxyacetophenone + NADPH + H+ + O2
4-hydroxyphenyl acetate + NADP+ + H2O
-
700fold preference for NADPH over NADH, Arg-440 plays an important role in catalysis
-
?
4-hydroxyacetophenone + NADPH + H+ + O2
4-hydroxyphenyl acetate + NADP+ + H2O
-
NADPH- and oxygen-dependent Baeyer-Villiger oxidation, good substrate
-
?
4-hydroxyacetophenone + NADPH + H+ + O2
4-hydroxyphenyl acetate + NADP+ + H2O
-
physiological substrate
-
?
4-hydroxyacetophenone + NADPH + H+ + O2
4-hydroxyphenyl acetate + NADP+ + H2O
-
enantiospecific reaction, overview
-
-
?
4-hydroxybenzaldehyde + NADPH + H+ + O2
4-hydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzaldehyde + NADPH + H+ + O2
4-hydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxypropiophenone + NADPH + H+ + O2
4-hydroxyphenyl propionate + NADP+ + H2O
-
-
-
?
4-hydroxypropiophenone + NADPH + H+ + O2
4-hydroxyphenyl propionate + NADP+ + H2O
-
good substrate
-
?
4-methoxyacetophenone + NADPH + H+ + O2
4-methoxyphenyl acetate + NADP+ + H2O
-
-
-
?
4-methoxyacetophenone + NADPH + H+ + O2
4-methoxyphenyl acetate + NADP+ + H2O
-
-
-
?
4-methylacetophenone + NADPH + H+ + O2
4-methylphenyl acetate + NADP+ + H2O
-
-
-
?
4-methylacetophenone + NADPH + H+ + O2
4-methylphenyl acetate + NADP+ + H2O
-
-
-
?
acetophenone + NADPH + H+ + O2
phenyl acetate + NADP+ + H2O
-
-
-
?
acetophenone + NADPH + H+ + O2
phenyl acetate + NADP+ + H2O
-
-
-
?
additional information
?
-
-
catalyzes the Baeyer-Villiger oxidation of aromatic compounds, converts a wide range of acetophenones via a Baeyer-Villiger rearrangement reaction into the corresponding phenyl acetates, the highest catalytic efficiency is observed with compounds bearing an electron donating substituent at the para position of the aromatic ring, in the absence of substrate the enzyme can act as an NADPH oxidase forming hydrogen peroxide, not: cyclohexanone, cyclopentanone, NADH
-
?
additional information
?
-
catalyzes the Baeyer-Villiger oxidation of aromatic compounds, converts a wide range of acetophenones via a Baeyer-Villiger rearrangement reaction into the corresponding phenyl acetates, the highest catalytic efficiency is observed with compounds bearing an electron donating substituent at the para position of the aromatic ring, in the absence of substrate the enzyme can act as an NADPH oxidase forming hydrogen peroxide, not: cyclohexanone, cyclopentanone, NADH
-
?
additional information
?
-
the enzyme is active with a wide range of aromatic and aliphatic ketones
-
-
?
additional information
?
-
-
the enzyme is active with a wide range of aromatic and aliphatic ketones
-
-
?
additional information
?
-
no reaction with 2-tetralone or 4-methoxy-1-indanone as substrate, no effect of changed conditions (pH, temperature, organic cosolvents)
-
-
?
additional information
?
-
-
a broad range of carbonylic compounds that are structurally more or less similar to 4-hydroxyacetophenone are substrates, catalyzes Baeyer-Villiger reaction with aromatic ketones and aldehydes, enzyme is capable of enantioselective formation of lactones from ketones and is also able to catalyze stereoselective sulfoxidation reactions by using aromatic sulfides, enantioselectivity, not: 2-nitroacetophenone, 4-nitroacetophenone, benzophenone, benzoin, 2-acetonaphthone, 3-acetylpyridine, benzoic acid, methyl 4-hydroxybenzoate, benzamide, N,N-dimethylaniline, phenylacetone, 1-indanone, 4-hydroxy-1-indanone, 1,3-indanone, 4-chromanone, cyclopentanone, cyclohexanone, progesterone, dihydrocarvone, acetone, butanone, 4-heptanone
-
?
additional information
?
-
-
catalyzes Baeyer-Villiger oxidation reactions on various ketones, oxidizes a variety of aromatic ketones and sulfides
-
?
additional information
?
-
-
substrate specificity, regioselectivity, the enzyme preferably and stereospecifically catalyzes Baeyer-Villiger oxidations of of ketones bearing a cyclobutanone structural motif, e.g. oxidation of several prochiral cyclobutanones to antipodal butyrolactones, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes Baeyer-Villiger oxidations of a wide range of ketones, thereby generating esters or lactones, overview
-
-
?
additional information
?
-
-
the recombinant enzyme is highly enantioselective in the synthesis of chiral phenyl and benzyl sulfoxides, oxidation of aromatic sulfides, substrate specificity and enantioselectivity, overview
-
-
?
additional information
?
-
-
a Bayer-Villinger monooxygenase, substrate specificity with several racemic cyclic and linear ketones, as well as 2-phenylpropionaldehyde, high enantioselectivites can be obtained in the kinetic resolution processes depending on the substrate structure and the reaction conditions, overview
-
-
?
additional information
?
-
-
no activity with a racemic 2-methyl-1-tetralone
-
-
?
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
(4-hydroxyphenyl)ethan-1-one + NADPH + O2
4-hydroxyphenyl acetate + NADP+ + H2O
1 unit enzyme oxidizes 1 micromol substrate to product per minute at pH 9.0, 25°C in the presence of NADPH
-
-
?
(4-hydroxyphenyl)ethan-1-one + NADPH + O2
4-hydroxyphenyl acetate + NADP+ + H2O
-
-
-
-
?
4-hydroxyacetophenone + NADPH + H+ + O2
4-hydroxyphenyl acetate + NADP+ + H2O
catalyzes the first step in the degradation of 4-hydroxyacetophenone
-
?
4-hydroxyacetophenone + NADPH + H+ + O2
4-hydroxyphenyl acetate + NADP+ + H2O
the enzyme catalyzes the first committed step in th 4-hydroxyacetophenone catabolism, pathway overview
-
-
?
4-hydroxyacetophenone + NADPH + H+ + O2
4-hydroxyphenyl acetate + NADP+ + H2O
-
-
-
-
?
4-hydroxyacetophenone + NADPH + H+ + O2
4-hydroxyphenyl acetate + NADP+ + H2O
-
physiological substrate
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
FAD-dependent, each subunit contains a noncovalently bound FAD molecule, both molecules participate in the reduction reaction, molecular oxygen is able to reoxidize the flavin cofactor
FAD
-
required for activity, each subunit contains a non-covalently, tightly bound FAD cofactor, binding of FAD is important for the octameric conformation
NADPH
-
specific for NADPH as coenzyme, Arg-339 and Lys-439 are involved in coenzyme recognition, Arg-440 not, Lys-439 plays a role in recognizing the 2-phosphate of NADPH, 700fold preference for NADPH over NADH
additional information
-
complex formation between the cofactors NADPH or 3-aminopyridine adenine dinucleotide phosphate
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-Aminopyridine adenine dinucleotide phosphate
-
cofactor analogue, tight binding to the wild-type enzyme and mutant R440A
hexane
-
enzyme activity is markedly reduced at concentrations of hexane below 5% and over 30%
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hexane
-
enzyme activity is highest at concentrations of hexane between 5% and 30%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic resolution of the racemic carbonyl compounds, overview
-
0.3
NADH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439F mutant
0.52
NADH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439A mutant
0.78
NADH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439N mutant
1.28
NADH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439P mutant
1.44
NADH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, wild-type HAPMO
3
NADH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, R339A mutant
0.012
NADPH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, wild-type HAPMO
0.017
NADPH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439P mutant
0.078
NADPH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439N mutant
0.08
NADPH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439F mutant
0.2
NADPH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439A mutant
3
NADPH
-
above, pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, R339A mutant
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.19
NADH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, R339A mutant
0.7
NADH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439P mutant
1.7
NADH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, wild-type HAPMO
2.4
NADH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439A mutant
2.4
NADH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439F mutant
5.1
NADH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439N mutant
0.1
NADPH
-
above, pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, R339A mutant
0.2
NADPH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439P mutant
1
NADPH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439F mutant
1.6
NADPH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439A mutant
3.5
NADPH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439N mutant
10.1
NADPH
-
pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, wild-type HAPMO
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene hapA, formerly hapE, encoded in the gene cluster hapCDEFGHIBA
SwissProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
145100
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
2 * 70000, SDS-PAGE, 2 * 71884, sequence calculation
additional information
-
quaternary structure of wild-type and mutant enzymes, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G490A
strictly conserved glycine, dramatic effect of mutation on binding and oxidation of NADPH
H61T
-
the H61T mutant is purified as apo-enzyme and mainly exists as a dimeric species, the binding of FAD to the enzyme restores the octameric conformation
K439A
-
mutant with 100fold decrease in catalytic efficiency with NADPH, mainly caused by increased Km, 4fold increased efficiency with NADH
K439F
-
mutant with higher activity with NADH compared to wild-type HAPMO
K439N
-
mutant with higher activity with NADH compared to wild-type HAPMO
K439P
-
mutant with higher activity with NADH compared to wild-type HAPMO
R339A
R440A
R339A
-
mutant with largely decreased affinity for NADPH and decreased catalytic efficiency with NADH
R339A
-
site-directed mutagenesiss, the mutant shows decreased activity and affinity to NADPH compared to the wild-type enzyme, the mutant only weakly interacts with 3-aminopyridine adenine dinucleotide phosphate
R440A
-
totally inactive mutant, Arg-440 is crucial for completing the catalytic cycle
R440A
-
site-directed mutagenesiss, inactive mutant, the mutant shows highly increased affinity to NADPH compared to the wild-type enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the association with the coenzyme NADPH is crucial for enzyme stability, 3-aminopyridine adenine dinucleotide phosphate highly stabilizes the inactive dimeric state of the enzyme
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gne hapA, encoded in the hapCDEFGHIBA gene cluster, DNA and amino acid sequence determination and analysis
overexpression of recombinant enzyme in Escherichia coli BL21(DE3)pLysS
gene hapE, expression of wild-type and mutant enzymes in Escherichia coli
-
hapE, expression in Escherichia coli BL21(DE3)pLysS, sequence analysis
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
additional information
synthesis
-
the enzyme can be useful in the highly enantioselective in the synthesis of chiral phenyl and benzyl sulfoxides
synthesis
-
usage of the enzyme as biocatalyst for synthesis of chiral 3-alkyl-3,4-dihydroisocoumarins, evaluation, overview
additional information
-
as acylcatechols are valuable synthons for the fine chemical industry, HAPMO might develop as a useful biocatalytic tool
additional information
as acylcatechols are valuable synthons for the fine chemical industry, HAPMO might develop as a useful biocatalytic tool
additional information
-
potential of HAPMO for biotechnological applications
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kamerbeek, N.M.; Moonen, M.J.; van der Ven, J.G.; van Berkel, W.J.H.; Fraaije, M.W.; Janssen, D.B.
4- Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB: a novel flavoprotein catalyzing Baeyer-Villiger oxidation of aromatic compounds
Eur. J. Biochem.
268
2547-2557
2001
Pseudomonas fluorescens, Pseudomonas fluorescens (Q93TJ5), Pseudomonas fluorescens ACB, Pseudomonas fluorescens ACB (Q93TJ5)
Kamerbeek, N.M.; Olsthoorn, A.J.J.; Fraaije, M.W.; Janssen, D.B.
Substrate specificity and enantioselectivity of 4-hydroxyacetophenone monooxygenase
Appl. Environ. Microbiol.
69
419-426
2003
Pseudomonas fluorescens, Pseudomonas fluorescens ACB
Kamerbeek, N.M.; Fraaije, M.W.; Janssen, D.B.
Identifying determinants of NADPH specificity in Baeyer-Villiger monooxygenases
Eur. J. Biochem.
271
2107-2116
2004
Pseudomonas fluorescens, Pseudomonas fluorescens ACB
Mihovilovic, M.D.; Kapitan, P.; Rydz, J.; Rudroff, F.; Ogink, F.H.; Fraaije, M.W.
Biooxidation of ketones with a cyclobutanone structural motif by recombinant whole-cells expressing 4-hydroxyacetophenone monooxygenase
J. Mol. Catal. B
32
135-140
2005
Pseudomonas fluorescens, Pseudomonas fluorescens ACB
-
van den Heuvel, R.H.; Tahallah, N.; Kamerbeek, N.M.; Fraaije, M.W.; van Berkel, W.J.; Janssen, D.B.; Heck, A.J.
Coenzyme binding during catalysis is beneficial for the stability of 4-hydroxyacetophenone monooxygenase
J. Biol. Chem.
280
32115-32121
2005
Pseudomonas fluorescens, Pseudomonas fluorescens ACB
de Gonzalo, G.; Torres Pazmino, D.E.; Ottolina, G.; Fraaije, M.W.; Carrea, G.
4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB as an oxidative biocatalyst in the synthesis of optically active sulfoxides
Tetrahedron Asymmetry
17
130-135
2006
Pseudomonas fluorescens, Pseudomonas fluorescens ACB
-
Moonen, M.J.; Kamerbeek, N.M.; Westphal, A.H.; Boeren, S.A.; Janssen, D.B.; Fraaije, M.W.; van Berkel, W.J.
Elucidation of the 4-hydroxyacetophenone catabolic pathway in Pseudomonas fluorescens ACB
J. Bacteriol.
190
5190-5198
2008
Pseudomonas fluorescens (Q93TJ5), Pseudomonas fluorescens, Pseudomonas fluorescens ACB (Q93TJ5), Pseudomonas fluorescens ACB
Rodriguez, C.; De Gonzalo, G.; Fraaije, M.W.; Gotor, V.
Enzymatic kinetic resolution of racemic ketones catalyzed by Baeyer-Villiger monooxygenases
Tetrahedron Asymmetry
18
1338-1344
2007
Pseudomonas fluorescens
-
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.
15
2526-2532
2009
Pseudomonas fluorescens (Q93TJ5), Pseudomonas fluorescens ACB (Q93TJ5)
-
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
-
Rioz-Martinez, A.; de Gonzalo, G.; Torres Pazmino, D.E.; Fraaije, M.W.; Gotor, V.
Synthesis of chiral 3-alkyl-3,4-dihydroisocoumarins by dynamic kinetic resolutions catalyzed by a Baeyer-Villiger monooxygenase
J. Org. Chem.
75
2073-2076
2010
Pseudomonas fluorescens, Pseudomonas fluorescens ACB
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