Information on EC 1.14.13.22 - cyclohexanone monooxygenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.14.13.22
-
RECOMMENDED NAME
GeneOntology No.
cyclohexanone monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cyclohexanone + NADPH + H+ + O2 = hexano-6-lactone + NADP+ + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
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oxygen ring insertion reaction
redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cyclohexanol degradation
Caprolactam degradation
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Microbial metabolism in diverse environments
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-
SYSTEMATIC NAME
IUBMB Comments
cyclohexanone,NADPH:oxygen oxidoreductase (lactone-forming)
A flavoprotein (FAD). In the catalytic mechanism of this enzyme, the nucleophilic species that attacks the carbonyl group is a peroxyflavin intermediate that is generated by reaction of the enzyme-bound flavin cofactor with NAD(P)H and oxygen [2]. This enzyme is able to catalyse a wide range of oxidative reactions, including enantioselective Baeyer-Villiger reactions [3], sulfoxidations [4], amine oxidations [5] and epoxidations [6].
CAS REGISTRY NUMBER
COMMENTARY hide
52037-90-8
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59088-27-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Acinetobacter sp. NCIMB 9871
strain NCIMB 9871
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Manually annotated by BRENDA team
strain CA1, low activity
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Manually annotated by BRENDA team
strain L661, gene chnB
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
inducible by cyclohexanone; strain KUFI-6N
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Manually annotated by BRENDA team
strain KUFI-6N
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
strain PA 09501
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Manually annotated by BRENDA team
strain PA 09501
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain Phi 1
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Manually annotated by BRENDA team
strain Phi 1
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-
Manually annotated by BRENDA team
strain Phi 2
SwissProt
Manually annotated by BRENDA team
strain Phi 2
SwissProt
Manually annotated by BRENDA team
strain Phi1
UniProt
Manually annotated by BRENDA team
strain Phi2
UniProt
Manually annotated by BRENDA team
strain TK6, gene chnB
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
flavoprotein that carries out the archetypical Baeyer-Villiger oxidation of a variety of cyclic ketones into lactones, size and shape of substrate binding pocket are adjustable to accommodate a diverse range of substrates
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-camphor + NADPH + O2
?
show the reaction diagram
(+)-dihydrocarvone + NADPH + O2
?
show the reaction diagram
(1aS,4aS,8aS)-8a-methylhexahydronaphthalene-1,6-dione + NADPH + O2
(5aR,9aS)-9a-methylhexahydrobenzo[b]oxepine-2,7-dione + NADP+ + H2O
show the reaction diagram
(1R)-bicyclo[2.2.1]heptane-2,5-dione + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
74.4% of the activity with cyclohexanone
-
-
?
(2R)-2-ethylcyclohexanone + NADPH + H+ + O2
(7S)-7-ethyloxepan-2-one + NADP+ + H2O
show the reaction diagram
(2R,6S)-2,6-dimethylcyclohexanone + NADPH + H+ + O2
cis-3, 7-dimethyl-2-oxepanone + NADP+ + H2O
show the reaction diagram
-
-
-
?
(2R,6S)-2,6-dimethylcyclohexanone + NADPH + O2 + H+
(3R,7S)-3,7-dimethyloxepan-2-one + NADP+ + H2O
show the reaction diagram
(2S)-2-(prop-2-en-1-yl)cyclohexanone + NADPH + H+ + O2
(7R)-7-(prop-2-en-1-yl)oxepan-2-one + NADP+ + H2O
show the reaction diagram
(3R)-3-(1-methylethenyl)cyclohexanone + NADPH + O2 + H+
(6S)-6-(1-methylethenyl)oxepan-2-one + NADP+ + H2O
show the reaction diagram
(4aR,8aS)-8a-methylhexahydronaphthalene-1,6(2H,5H)-dione + NADPH + O2
(5aR,9aS)-9a-methylhexahydrobenzo[b]oxepine-2,7-dione + (4aS,6S,8aR)-6-hydroxy-8a-methyloctahydronaphthalen-1-one + NADP+ + H2O
show the reaction diagram
(S)-dithiane sulfoxide + NADPH + O2
?
show the reaction diagram
-
recombinant enzyme in E. coli or Saccharomyces cerevisiae
-
-
?
1,2-cyclohexandione + NADPH + H+ + O2
? + NADP+ + H2O
show the reaction diagram
1,3-cyclohexandione + NADPH + H+ + O2
? + NADP+ + H2O
show the reaction diagram
1,3-dithiane + NADPH + O2
(R)-1,3-dithiane-1-oxide + NADP+ + H2O
show the reaction diagram
1,4-cyclohexandione + NADPH + H+ + O2
? + NADP+ + H2O
show the reaction diagram
1,4-dioxaspiro[4.5]decan-8-one + NADPH + H+ + O2
1,4,8-trioxa-spiro[4,6]undecan-9-one + NADP+ + H2O
show the reaction diagram
-
-
-
?
1,4-dioxaspiro[4.5]decan-8-one + NADPH + O2 + H+
1,4,8-trioxaspiro[4.6]undecan-9-one + NADP+ + H2O
show the reaction diagram
1-oxa-2-oxocycloheptane + NADPH + O2
?
show the reaction diagram
-
oxidation
-
-
?
1-phenyl-2-propanone + NADPH + O2
?
show the reaction diagram
2,2,6-trimethylcyclohexanone + NADPH + H+ + O2
3,7,7-trimethyloxepan-2-one + NADP+ + H2O
show the reaction diagram
-
-
-
?
2,2,6-trimethylcyclohexanone + NADPH + O2 + H+
3,7,7-trimethyloxepan-2-one + NADP+ + H2O
show the reaction diagram
2-hexyl-cyclopentanone + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
2-hexylcyclopentanone + NADPH + H+ + O2
6-hexyl-tetrahydro-pyran-2-one + NADP+ + H2O
show the reaction diagram
-
-
-
?
2-hexylcyclopentanone + NADPH + O2 + H+
6-hexyltetrahydro-2H-pyran-2-one + NADP+ + H2O
show the reaction diagram
-
82% conversion at 20 h
-
?
2-hydroxycyclobutanone + NADPH + H+ + O2
1-oxa-2-oxo-3-hydroxycyclopentane + NADP+ + H2O
show the reaction diagram
67.3% of the activity with cyclohexanone
-
-
?
2-hydroxycyclohexanone + NADPH + O2
1-oxa-2-oxo-3-hydroxycycloheptane + NADP+ + H2O
show the reaction diagram
2-hydroxyethyl methyl sulfide + NADPH + O2
2-hydroxyethyl methyl sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-methyl-cyclohexanone + NADPH + H+ + O2
1-oxa-2-oxo-3-methyl-cycloheptane + NADP+ + H2O
show the reaction diagram
2-methyl-cyclohexanone + NADPH + H+ + O2
1-oxa-2-oxo-3-methylcycloheptane + NADP+ + H2O
show the reaction diagram
2-methyl-cyclopentanone + NADPH + H+ + O2
1-oxa-2-oxo-3-methyl-cyclohexane + NADP+ + H2O
show the reaction diagram
2-methyl-cyclopentanone + NADPH + H+ + O2
1-oxa-2-oxo-3-methylcyclohexane + NADP+ + H2O
show the reaction diagram
2-methylcyclohexanone + NADPH + O2
1-oxa-2-oxo-3-methylcycloheptane + NADP+ + H2O
show the reaction diagram
2-methylcyclohexanone + NADPH + O2 + H+
7-methyloxepan-2-one + NADP+ + H2O
show the reaction diagram
-
-
-
?
2-methylcyclohexyl boronic acid + NADPH + O2
2-methylcyclohexanol + BO3- + NADP+ + H2O
show the reaction diagram
-
racemic substrate
-
?
2-norbornanone + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
2-phenyl-1-ethanal + NADPH + O2
?
show the reaction diagram
2-phenylcyclohexanone + NADPH + H+ + O2
1-oxa-2-oxo-3-phenylcycloheptane + NADP+ + H2O
show the reaction diagram
11% of the activity with cyclohexanone
-
-
?
2-phenylcyclohexanone + NADPH + H+ + O2
3-phenyloxepan-2-one + NADP+ + H2O
show the reaction diagram
-
-
-
?
2-phenylcyclohexanone + NADPH + O2
1-oxa-2-oxo-3-phenylcycloheptane + NADP+ + H2O
show the reaction diagram
-
slight
-
-
?
2-phenylcyclohexanone + NADPH + O2 + H+
7-phenyloxepan-2-one + NADP+ + H2O
show the reaction diagram
-
51% conversion at 20 h
-
?
2-phenylethyl methyl sulfide + NADPH + O2
2-phenylethyl methyl sulfoxide
show the reaction diagram
-
-
-
?
2-phenylpropyl methyl sulfide + NADPH + O2
2-phenylpropyl methyl sulfoxide
show the reaction diagram
-
-
-
?
2-propylcyclohexanone + NADPH + O2 + H+
(7S)-7-propyloxepan-2-one + NADP+ + H2O
show the reaction diagram
-
-
-
?
2-thiacyclohexanone + NADPH + O2
1-oxa-2-oxo-3-thiacycloheptane + NADP+ + H2O
show the reaction diagram
-
substrate inactivates enzyme after a few turnovers
-
-
?
3,3,5-trimethylcyclohexanone + NADPH + H+ + O2
4,6,6-trimethyloxepan-2-one + 4,4,6-trimethyloxepan-2-one + NADP+ + H2O
show the reaction diagram
-
-
-
?
3,3,5-trimethylcyclohexanone + NADPH + O2 + H+
4,6,6-trimethyloxepan-2-one + 4,4,6-trimethyloxepan-2-one + NADP+ + H2O
show the reaction diagram
-
91% conversion at 20 h, 1/1 isomer with 98% enantiomeric excess
-
?
3,4-dihydronaphthalen-2(1H)-one + NADPH + H+ + O2
8,9-dihydro-5H-7-oxa-benzocyclo-hepten-6-one + NADP+ + H2O
show the reaction diagram
-
-
-
?
3,4-dihydronaphthalen-2(1H)-one + NADPH + O2 + H+
4,5-dihydro-3-benzoxepin-2(1H)-one + NADP+ + H2O
show the reaction diagram
-
more than 95% conversion one isomer
-
?
3,5-dimethylcyclohexanone + NADPH + H+ + O2
4,6-dimethyloxepan-2-one + NADP+ + H2O
show the reaction diagram
3-(1,3-benzodioxol-5-yl)cyclobutanone + NADPH + H+ + O2
4-(1,3-benzodioxol-5-yl)dihydrofuran-2(3H)-one + NADP+ + H2O
show the reaction diagram
3-(3,4,5-trimethoxyphenyl)cyclobutanone + NADPH + H+ + O2
4-(3,4,5-trimethoxyphenyl)dihydrofuran-2(3H)-one + NADP+ + H2O
show the reaction diagram
less than 50% conversion, 96% enantiomeric excess, (-)-product
-
-
?
3-methylcyclohexanone + NADPH + O2 + H+
(4S)-4-methyloxepan-2-one + (6R)-6-methyloxepan-2-one + NADP+ + H2O
show the reaction diagram
-
-
-
?
4,4-dimethylcyclohexanone + NADPH + H+ + O2
5,5-dimethyloxepan-2-one + NADP+ + H2O
show the reaction diagram
50-90% conversion
-
-
?
4-allyl-cyclohexanone + NADPH + O2
4-allyl-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
4-bromocyclohexanone + NADPH + O2
4-bromo-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
4-chlorocyclohexanone + NADPH + O2
4-chloro-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
4-ethoxy-cyclohexanone + NADPH + O2
4-ethoxy-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
4-ethyl-cyclohexanone + NADPH + O2
4-ethyl-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
4-ethylcyclohexanone + NADPH + O2 + H+
(5S)-5-ethyloxepan-2-one + NADP+ + H2O
show the reaction diagram
-
98% enantiomeric excess
-
?
4-hydroxy-cyclohexanone + NADPH + O2
4-hydroxy-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
4-hydroxycyclohexanone + NADPH + O2
1-oxa-2-oxo-5-hydroxycycloheptane + NADP+ + H2O
show the reaction diagram
4-iodocyclohexanone + NADPH + O2
4-iodo-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
4-methoxy-cyclohexanone + NADPH + O2
4-methoxy-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
4-methyl-cyclohexanone + NADPH + O2
4-methyl-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
4-methylcyclohexanone + NADPH + O2
1-oxa-2-oxo-5-methylcycloheptane + NADP+ + H2O
show the reaction diagram
4-methylcyclohexanone + NADPH + O2 + H+
(5S)-5-methyloxepan-2-one + NADP+ + H2O
show the reaction diagram
-
98% enantiomeric excess
-
?
4-n-propyl-cyclohexanone + NADPH + O2
4-n-propyl-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
4-phenylcyclohexanone + NADPH + H+ + O2
5-phenyloxepan-2-one + NADP+ + H2O
show the reaction diagram
less than 50% conversion, 97% enantiomeric excess, (-)-product
-
-
?
4-tert-butylcyclohexanone + NADPH + H+ + O2
5-t-butyl-2-oxepanone + NADP+ + H2O
show the reaction diagram
-
-
-
?
4-tert-butylcyclohexanone + NADPH + O2
1-oxa-2-oxo-5-tert-butylcycloheptane + NADP+ + H2O
show the reaction diagram
-
slight
-
-
?
4-tert-butylcyclohexanone + NADPH + O2 + H+
(5S)-5-tert-butyloxepan-2-one + NADP+ + H2O
show the reaction diagram
-
88% conversion at 20 h, 99% enantiomeric excess
-
?
4a-methyltetrahydro-1aH-naphtho[1,8a-b]oxirene-2,5(3H,6H)-dione + NADPH + O2
(1R,3S,7S)-7-methyl-2,8-dioxatricyclo[5.5.0.01,3]dodecane-4,9-dione + NADP+ + H2O
show the reaction diagram
allyl methyl sulfide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
bicyclo[3.2.0]hept-2-en-6-one + NADPH + O2
(1R,5S)-3-oxabicyclo-[3.3.0]oct-6-en-3-one + (1S,5R)-2-oxabicyclo-[3.3.0]oct-6-en-3-one + NADP+ + H2O
show the reaction diagram
bicyclo[3.2.0]hept-2-en-6-one + NADPH + O2
3,3a,6,6a-tetrahydro-1H-cyclopenta[c]furan-1-one + NADP+ + H2O
show the reaction diagram
63% of the activity with cyclohexanone
-
-
?
bicyclo[3.2.0]hept-2-en-6-one + NADPH + O2
?
show the reaction diagram
butanal + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
cis-hex-2-enyl phenyl selenide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
cuprizone + NADPH + O2
?
show the reaction diagram
cyclobutanone + NADPH + H+ + O2
1-oxa-2-oxo-cyclopentane + NADP+ + H2O
show the reaction diagram
cyclobutanone + NADPH + H+ + O2
dihydrofuran-2(3H)-one + NADP+ + H2O
show the reaction diagram
65% of the activity with cyclohexanone
-
-
?
cyclobutanone + NADPH + O2
1-oxa-2-oxo-cyclopentane + NADP+ + H2O
show the reaction diagram
cyclobutyl methyl ketone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
17.5% of the activity with cyclohexanone
-
-
?
cyclodecanone + NADPH + H+ + O2
1-oxa-2-oxo-cycloundecane + NADP+ + H2O
show the reaction diagram
cyclodecanone + NADPH + O2
1-oxa-2-oxocycloendecane + NADP+ + H2O
show the reaction diagram
-
low activity
-
-
?
cycloheptanone + NADPH + H+ + O2
1-oxa-2-oxo-cyclooctane + NADP+ + H2O
show the reaction diagram
cycloheptanone + NADPH + O2
1-oxa-2-oxo-cyclooctane + NADP+ + H2O
show the reaction diagram
cyclohexan-1,2-dione + NADPH + O2
1-oxa-2,3-dioxo-cycloheptane + NADP+ + H2O
show the reaction diagram
cyclohexan-1,4-dione + NADPH + O2
1-oxa-2,5-dioxo-cycloheptane + NADP+ + H2O
show the reaction diagram
cyclohexanone + NADPH + H+ + O2
epsilon-caprolactone + NADP+ + H2O
show the reaction diagram
cyclohexanone + NADPH + H+ + O2
hexano-6-lactone + NADP+ + H2O
show the reaction diagram
cyclohexanone + NADPH + O2
1-oxa-2-oxocycloheptane + NADP+ + H2O
show the reaction diagram
cyclohexanone + NADPH + O2
6-hexanolide + NADP+ + H2O
show the reaction diagram
cyclohexanone + NADPH + O2
epsilon-caprolactone + NADP+ + H2O
show the reaction diagram
cyclohexanone + NADPH + O2
hexano-6-lactone + NADP+ + H2O
show the reaction diagram
cyclohexyl methyl ketone + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
15.7% of the activity with cyclohexanone
-
-
?
cyclohexyl methyl sulfide + NADPH + O2
cyclohexyl methyl sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
-
?
cyclooctanone + NADPH + H+ + O2
1-oxa-2-oxo-cyclononane + NADP+ + H2O
show the reaction diagram
cyclooctanone + NADPH + O2
1-oxa-2-oxo-cyclononane + NADP+ + H2O
show the reaction diagram
cyclopentanone + NADPH + H+ + O2
1-oxa-2-oxo-cyclohexane + NADP+ + H2O
show the reaction diagram
cyclopentanone + NADPH + O2
1-oxa-2-oxo-cyclohexane + NADP+ + H2O
show the reaction diagram
cyclopentyl methyl sulfide + NADPH + O2
cyclopentyl methyl sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
-
?
D-fenchone + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
delta-thiovalerolactone + NADPH + O2
?
show the reaction diagram
-
substrate inactivates enzyme after a few turnovers
-
-
ir
dihydrocarvone + NADPH + O2
?
show the reaction diagram
dithiane + NADPH + H+ + O2
(R)-dithiane sulfoxide + NADP+ + H2O
show the reaction diagram
-
recombinant enzyme in E. coli or Saccharomyces cerevisiae
-
?
epsilon-thiocaprolactone + NADPH + O2
?
show the reaction diagram
-
substrate inactivates enzyme after a few turnovers
-
-
ir
ethyl 4-oxocyclohexanecarboxylate + NADPH + H+ + O2
ethyl 7-oxooxepane-4-carboxylate + NADP+ + H2O
show the reaction diagram
less than 50% conversion, 98% enantiomeric excess, (-)-product
-
-
?
ethyl p-tolyl sulfide + NADPH + O2
(S)-ethyl p-tolyl sulfoxide + NADP+ + H2O
show the reaction diagram
ethylene monothiocarbonate + NADPH + O2
?
show the reaction diagram
-
substrate inactivates enzyme after a few turnovers
-
-
?, ir
gamma-thiobutyrolactone + NADPH + O2
?
show the reaction diagram
-
substrate inactivates enzyme after a few turnovers
-
-
ir
iodide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
isopropyl methyl sulfide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
methyl phenyl sulfide + NADPH + H+ + O2
(R)-methyl phenyl sulfoxide + NADP+ + H2O
show the reaction diagram
n-butyl methyl sulfide + NADPH + O2
?
show the reaction diagram
-
recombinant enzyme in E. coli or Saccharomyces cerevisiae
-
-
?
n-butylboronic acid + NADPH + O2
n-butanol + BO3- + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N-methylbenzylamine + NADPH + O2
N-benzyl-N-methylhydroxylamine + NADP+ + H2O
show the reaction diagram
n-octylboronic acid + NADPH + O2
n-octanol + BO3- + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
norcamphor + NADPH + O2
?
show the reaction diagram
norcamphor + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
74.8% of the activity with cyclohexanone
-
-
?
octahydronaphthalen-1(2H)-one + NADPH + H+ + O2
octahydro-benzo[b]oxepin-2-one + octahydro-benzo[c]oxepin-1-one + NADP+ + H2O
show the reaction diagram
-
-
-
?
octahydronaphthalen-1(2H)-one + NADPH + O2 + H+
octahydro-1-benzoxepin-2(3H)-one + octahydro-2-benzoxepin-1(3H)-one + NADP+ + H2O
show the reaction diagram
-
100% conversion two isomers octahydro-1-benzoxepin-2(3H)-one + octahydro-2-benzoxepin-1(3H)-one with ratio 2/1
-
?
octahydronaphthalen-2(1H)-one + NADPH + H+ + O2
cis-octahydro-benzo[c]oxepin-3-one + trans-octahydro-benzo[c]oxepin-3-one + cis-octahydro-7-oxa-benzocyclohepten-6-one + NADP+ + H2O
show the reaction diagram
-
-
-
?
octahydronaphthalen-2(1H)-one + NADPH + O2 + H+
octahydro-3-benzoxepin-2(1H)-one + octahydro-2-benzoxepin-3(1H)-one + NADP+ + H2O
show the reaction diagram
-
66% conversion at 20 h, octahydro-2-benzoxepin-3(1H)-one is the major product
-
?
octyl methyl sulfide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
phenyl allyl selenide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
phenyl allyl sulfide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
phenyl methyl selenide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
phenyl propargyl selenide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
phenylboronic acid + NADPH + O2
phenol + BO3- + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
S-gamma-thiobutyrolactone + NADPH + O2
?
show the reaction diagram
-
substrate irreversibly inactivates enzyme after a few turnovers
-
-
?
syn-7-benzyloxymethyl-2-norbonen-5-one + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
tert-butyl ethyl sulfide + NADPH + O2
?
show the reaction diagram
-
low activity
-
-
?
tert-butyl methyl sulfide + NADPH + O2
?
show the reaction diagram
tert-butyl vinyl sulfide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
thiane + NADPH + O2
?
show the reaction diagram
thiane sulfoxide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
trans-hex-2-enyl phenyl selenide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
triethylphosphite + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-dithiane sulfoxide + NADPH + O2
?
show the reaction diagram
-
recombinant enzyme in E. coli or Saccharomyces cerevisiae
-
-
?
1-oxa-2-oxocycloheptane + NADPH + O2
?
show the reaction diagram
-
oxidation
-
-
?
4-hydroxy-cyclohexanone + NADPH + O2
4-hydroxy-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
bicyclo[3.2.0]hept-2-en-6-one + NADPH + O2
?
show the reaction diagram
cyclohexan-1,2-dione + NADPH + O2
1-oxa-2,3-dioxo-cycloheptane + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
cyclohexan-1,4-dione + NADPH + O2
1-oxa-2,5-dioxo-cycloheptane + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
cyclohexanone + NADPH + H+ + O2
epsilon-caprolactone + NADP+ + H2O
show the reaction diagram
cyclohexanone + NADPH + H+ + O2
hexano-6-lactone + NADP+ + H2O
show the reaction diagram
cyclohexanone + NADPH + O2
1-oxa-2-oxocycloheptane + NADP+ + H2O
show the reaction diagram
cyclohexanone + NADPH + O2
epsilon-caprolactone + NADP+ + H2O
show the reaction diagram
cyclohexanone + NADPH + O2
hexano-6-lactone + NADP+ + H2O
show the reaction diagram
dithiane + NADPH + H+ + O2
(R)-dithiane sulfoxide + NADP+ + H2O
show the reaction diagram
-
recombinant enzyme in E. coli or Saccharomyces cerevisiae
-
?
methyl phenyl sulfide + NADPH + H+ + O2
(R)-methyl phenyl sulfoxide + NADP+ + H2O
show the reaction diagram
n-butyl methyl sulfide + NADPH + O2
?
show the reaction diagram
-
recombinant enzyme in E. coli or Saccharomyces cerevisiae
-
-
?
tert-butyl methyl sulfide + NADPH + O2
?
show the reaction diagram
-
recombinant enzyme in E. coli or Saccharomyces cerevisiae
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deaza-FAD
-
reactivates apoenzyme
6-Methyl-FAD
-
reactivates apoenzyme
9-Aza-FAD
-
reactivates apoenzyme
flavin
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
-
iron-hem dependent enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-dithiane
-
substrate inhibition
2-Thiacyclohexanone
-
substrate inactivates enzyme after a few turnovers
2-Thiocyclohexanone
-
-
5,5'-dithiobis(2-nitrobenzoate)
5-deaza-FAD
-
competitive
arsenate
-
-
Bathocuproine
Cu2+
-
completely
cyclohexanone
-
substrate inhibition
delta-thiovalerolactone
-
substrate inactivates enzyme after a few turnovers
diethyl dicarbonate
-
complete inhibition
ethylene monothiocarbonate
-
substrate inactivates enzyme after a few turnovers
iodoacetamide
NADP+
p-hydroxymercuribenzoate
Quinacrine
-
-
S-gamma-Thiobutyrolactone
-
substrate inactivates enzyme after a few turnovers
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7-Chloro-8-demethyl-FAD
-
reactivates apoenzyme
additional information
-
the enzyme is inducible by cyclohexanone
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
(+)-Camphor
-
-
0.045
1,3-dithiane
-
pH 8.6, 25°C
0.33
1-Phenyl-2-propanone
-
-
0.12
2-hydroxycyclobutanone
pH 8.0, 25°C
0.0093 - 0.0112
2-Hydroxycyclohexanone
0.012
2-methylcyclohexanone
-
-
0.07
2-methylcyclohexyl boronic acid
-
-
0.35
2-Phenyl-1-ethanal
-
-
0.33
2-phenylcyclohexanone
pH 8.0, 25°C
0.01
3-thiacyclohexanone
-
substrate inactivates enzyme after a few turnovers
0.39
4-Hydroxycyclohexanone
-
-
0.009 - 0.016
4-methylcyclohexanone
0.021
4-thiacyclohexanone
-
-
0.0014
Bicyclo[3.2.0]hept-2-en-6-one
-
pH 8.6, 25°C, recombinant and native enzyme
0.025
Butanal
-
-
0.0096
cis-hex-2-enyl phenyl selenide
-
-
0.0035
Cuprizone
-
-
0.007
Cyclobutanone
pH 8.0, 25°C
0.2 - 0.88
Cycloheptanone
0.143 - 0.17
Cyclohexan-1,2-dione
0.19
Cyclohexan-1,4-dione
-
-
0.00048 - 0.04
cyclohexanone
1.03 - 1.8
Cyclooctanone
3.6 - 4.66
Cyclopentanone
0.64
dihydrocarvone
-
-
0.22
ethyl p-tolyl sulfide
-
-
2.5
Iodide
-
-
0.009
n-Butylboronic acid
-
-
0.0025
n-Octylboronic acid
-
-
0.006 - 0.02
NADPH
0.14
Norcamphor
-
-
0.1
O2
-
below
0.03
Phenyl allyl selenide
-
-
0.11
Phenyl allyl sulfide
-
-
0.044
Phenyl methyl selenide
-
-
0.128
phenyl propargyl selenide
-
-
0.043
phenylboronic acid
-
-
0.024
Thiane
0.178
Thiane sulfoxide
-
-
0.0068
trans-hex-2-enyl phenyl selenide
-
-
0.36
triethyl phosphite
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.5
2-hydroxycyclobutanone
Ilyonectria destructans
G8H1L8
pH 8.0, 25°C
8.4
2-methylcyclohexyl boronic acid
Acinetobacter sp.
-
-
0.73
2-phenylcyclohexanone
Ilyonectria destructans
G8H1L8
pH 8.0, 25°C
0.683
cis-hex-2-enyl phenyl selenide
Acinetobacter sp.
-
-
6.8
Cyclobutanone
Ilyonectria destructans
G8H1L8
pH 8.0, 25°C
4.3
Cycloheptanone
Ilyonectria destructans
G8H1L8
pH 8.0, 25°C
9.8 - 30.3
cyclohexanone
0.68
Cyclooctanone
Ilyonectria destructans
G8H1L8
pH 8.0, 25°C
5.9
Cyclopentanone
Ilyonectria destructans
G8H1L8
pH 8.0, 25°C
0.24
delta-thiovalerolactone
Acinetobacter sp.
-
substrate inactivates enzyme after a few turnovers
0.227
epsilon-thiocaprolactone
Acinetobacter sp.
-
substrate inactivates enzyme after a few turnovers
2.38
ethylene monothiocarbonate
Acinetobacter sp.
-
substrate inactivates enzyme after a few turnovers
0.683
gamma-thiobutyrolactone
Acinetobacter sp.
-
substrate inactivates enzyme after a few turnovers
9.75
phenyl propargyl selenide
Acinetobacter sp.
-
-
0.917
trans-hex-2-enyl phenyl selenide
Acinetobacter sp.
-
-
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
38
2-hydroxycyclobutanone
Ilyonectria destructans
G8H1L8
pH 8.0, 25°C
42695
2.3
2-phenylcyclohexanone
Ilyonectria destructans
G8H1L8
pH 8.0, 25°C
4760
920
Cyclobutanone
Ilyonectria destructans
G8H1L8
pH 8.0, 25°C
8076
4.9
Cycloheptanone
Ilyonectria destructans
G8H1L8
pH 8.0, 25°C
5956
238
cyclohexanone
Ilyonectria destructans
G8H1L8
pH 8.0, 25°C
1299
0.7
Cyclooctanone
Ilyonectria destructans
G8H1L8
pH 8.0, 25°C
6503
1.3
Cyclopentanone
Ilyonectria destructans
G8H1L8
pH 8.0, 25°C
2478
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15
1,3-dithiane
-
pH 8.6, 25°C
2
2-Thiocyclohexanone
-
-
0.062
5-deaza-FAD
-
-
2.9
delta-thiovalerolactone
-
-
2
ethylene monothiocarbonate
-
-
0.038 - 0.39
NADP+
2
S-gamma-Thiobutyrolactone
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.4
substrate cyclohexanone, induced (1.0 mM isopropylthiogalactoside) cell culture extracts, modified Riesenberg medium, 30°C
0.5
substrate cyclohexanone, induced (1.0 mM isopropylthiogalactoside) cell culture extracts, BHI medium, 30°C
0.85
mutant W492A, cyclohexanone, 50 mM Tris-HCl buffer (pH 9.0), 0.1 mM NADPH, 25°C
1.4
-
H163Q mutant enzyme
3.57
with cyclohexanone as substrate, pH 7.5
3.68
-
with cyclohexanone as substrate, pH 7.5
3.75
with cyclohexanone as substrate, pH 7.5
5.4
-
H96Q mutant enzyme
6
wild type enzyme, cyclohexanone, 50 mM Tris-HCl buffer (pH 9.0), 0.1 mM NADPH, 25°C
6.8
substrate cyclohexanone, pH 8.0, 25°C
8 - 10
-
partially purified enzyme, substrate 4-methylcyclohexanone
9.1
-
purified recombinant enzyme, substrate bicyclo[3.2.0]hept-2-en-6-one
9.2
-
purified native enzyme, substrate bicyclo[3.2.0]hept-2-en-6-one
9.9
-
purified enzyme
14
-
purified recombinant His-tagged enzyme expressed in yeast
15
-
purified native enzyme
15.9
-
wild type enzyme
19.9
-
purified recombinant His-tagged enzyme expressed in E. coli
21
-
purified enzyme
24.75
purified His-tagged recombinant enzyme
678
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 10.1
-
broad, isozyme type 2
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10.5
-
no activity below pH 5.5 and above pH 10.5 at 30°C
6 - 10.5
-
pH 6.0: about 40% of activity maximum with isozymes type 1 and type 2, pH 10.5: about 10% of activity maximum with isozyme type 1, about 60% of activity maximum with isozyme type 2
6 - 11
-
at pH 6.0 and 11.0: about 10% of activity maximum
7 - 8.5
70% of maximal activity at pH 7.0 within this range, His-tagged recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
gel filtration
53000
-
low speed sedimentation without reaching equilibrium
56000
-
native PAGE
59000
-
low speed sedimentation without reaching equilibrium
60800
-
wild-type, electrospray mass spectrometry
61600
-
mass spectrometry
61620
-
recombinant His-tagged enzyme expressed in E. coli
61670
-
recombinant His-tagged enzyme expressed in yeast
74000
-
gel filtration
76000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 61586.04, recombinant enzyme, mass spectrometry, x * 61583.54, native enzyme, mass spectrometry
monomer
additional information
-
sequence alignment, and structure modelling and comparison to cyclopentanone monooxygenase, EC 1.14.13.16, structure-function analysis
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
microdialysis method, saturated ammonium sulfate solution
-
enzyme in complex with FAD and NADP+ in 2 distinct states, hanging drop or sitting drop vapor diffusion methods, crystal form I with 0.2 M sodium acetate trihydrate, 0.1 M sodium cacodylate pH 6.5, and 30% PEG 8000, for crystal form II with 0.2 M magnesium acetate tetrahydrate, 0.1 M sodium cacodylate pH 6.5, and 20% PEG 8000
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
48 h, purified recombinant enzyme: loss of 12% activity, native enzyme: loss of 24% activity
675461
6 - 8
purified recombinant enzyme, 70% remaining activity after 24 h at 4°C
685723
7 - 8
-
stable
438993
8.6
-
48 h, purified recombinant enzyme: loss of 15% activity, native enzyme: loss of 24% activity
675461
10
-
48 h, purified recombinant enzyme: loss of 45% activity, native enzyme: loss of 82% activity
675461
additional information
-
comparison of pH stability of crude, partially purified, and purified native and recombinant enzymes, overview
675461
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
2 min, 40% loss of activity for isozyme type 1, 7% loss of activity for isozyme type 2
45
-
1 min, 40% loss of activity for isozyme type 1, 18% loss of activity for isozyme type 2
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilization stabilizes
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is reduced by visible light in presence of EDTA under anaerobic conditions
-
438984
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, crude homogenates, negligible loss of activity, 2 months
-
-20°C, more than 1 year
-
-20°C, stable
-
-25°C, pH 7.1
25°C, 1 M sodium sulfate, half-life 1 week
-
25°C, half-life 1 day
-
4°C, in presence of cyclohexane or 0.1 mM NADPH
-
apoenzyme and enzyme complexed with 8-hydroxy-5-deazaflavin is stable on ice for several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cells centrifuged, washed with reaction buffer (0.1 M glycine/NaOH buffer, pH 9.0), disruption by ultrasonic processor, centrifugation, supernatants used as crude enzyme extracts
crude extract of Rhodococcus cells is partially purified using ammonium sulfate fractionation (50-70%), chromatography on Butyl-Toyopearl 650S with a linear gradient of 30%-0% (NH4)2SO4, and gel filtration on a Sephadex G-150 column. Purification of the recombinant enzyme: cells centrifuged and lysed with a French press, crude extract centrifuged, supernatant loaded on a DEAE-Sepharose FF column equilibrated with 50 mM sodium phosphate buffer (pH 7.0), elution with 0-0.2 M NaCl gradient, ammonium sulfate added to active fractions (30%), loaded onto a Butyl-S-Sepharose 6 FF column equilibrated with 30% ammonium sulfate in 50 mM sodium phosphate buffer (pH 7.0), elution with 30-0% ammonium sulfate gradient, active fractions pooled, concentrated, applied to two combined Superose 6 HR (10/300)/Superose 12 HR (10/300) gel filtration columns equilibrated with 50 mM sodium phosphate buffer (pH 7.0) containing 150 mM NaCl, elution with same buffer, pooled, concentrated with YM 10 membrane
industrial scale production
-
native enzyme and recombinant His-tagged enzyme from Escherichia coli and Saccharomyces cerevisiae
-
partial purification of recombinant enzyme
-
partially, recombinant from Escherichia coli
-
recombinant enzyme 21fold from Escherichia coli and native enzyme to homogeneity by ion exchange and affinity chromatography
-
recombinant enzyme using His-tag
recombinant from bacterial expression system
-
recombinant from Escherichia coli
-
recombinant from Escherichia coli and Saccharomyces cerevisiae
-
recombinant His6-tagged enzyme 8.3fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant protein
-
recombinant protein from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as His-tag fusion protein in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli TOP10
-
expression in bacterial expression system, DNA and amino acid sequence analysis
-
expression in Escherichia coli
expression in Escherichia coli under control of a strong L-arabinose inducible promoter
-
expression in Escherichia coli, amino acid and DNA sequence analysis, identification of potential flavin- and nicotinamide-binding sites; overexpression in Escherichia coli, amino acid sequence determination
-
expression in Escherichia coli, optimization of CHMO expression conditions, high concentrations of cyclohexanone cause the formation of CHMO as inclusion bodies during the reaction period, co-expression with the NADPH-regenerating enzyme glucose 6-phosphate dehydrogenase, overview
-
expression of His-tagged enzyme in Escherichia coli and Saccharomyces cerevisiae
-
gene amplification, cloning in pUC19 vector, transformation in Escherichia coli DH5 of plasmid pCMR100 containing the complete gene chnB1 (1620 bp), amplification of fragment carrying chnB1, cloning into plasmid pSD80 to result in pSDRmchnB1, overexpressed in Escherichia coli BL21 (DE3)
gene chnB, genomic library screening, DNA and amino acid sequence determination and analysis, sequence comparisons, functional expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
overexpression in Escherichia coli
-
overexpression in Escherichia coli and Saccharomyces cerevisiae
-
overexpression of wild-type and mutants in Escherichia coli
-
overexpression of wild-type and mutants in strains BL121(DE3) and JM109
-
PCR-amplification of chnB gene with template vector pMM4, cloning into pEKEx2 shuttle vector, expression in Corynebacterium glutamicum (ATCC13032)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F432I
-
random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
F432S
-
random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
F432Y/K500R
-
random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
H113Q
-
only minor effects on activity
H162Q
-
only minor effects on activity
H163Q
-
10fold lower turnover, doubling of Km
H200Q
-
only minor effects on activity
H522Q
-
only minor effects on activity
H59Q
-
not expressed at significant levels
H96Q
-
greatly reduced FAD content, reduced activity
K78E/F432S
-
random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
L426P/A541V
-
random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
F432I
Acinetobacter sp. NCIMB 9871
-
random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
-
F432S
Acinetobacter sp. NCIMB 9871
-
random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
-
F432Y/K500R
Acinetobacter sp. NCIMB 9871
-
random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
-
L426P/A541V
Acinetobacter sp. NCIMB 9871
-
random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
-
D41N/F505Y
-
site-directed mutagenesis, the mutant shows altered substrate specificity and enantioselectivity compared to the wild-type enzyme
F432I
-
site-directed mutagenesis, the mutant shows altered substrate specificity and enantioselectivity compared to the wild-type enzyme
F432S
-
site-directed mutagenesis, the mutant shows increased substrate specificity and enantioselectivity compared to the wild-type enzyme
L143F
-
site-directed mutagenesis, the mutant shows altered substrate specificity and enantioselectivity compared to the wild-type enzyme
W492A
14% activity with cyclohexanone compared to wild type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
synthesis
Show AA Sequence (344 entries)
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