Information on EC 1.14.13.16 - cyclopentanone monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.16
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RECOMMENDED NAME
GeneOntology No.
cyclopentanone monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cyclopentanone + NADPH + H+ + O2 = 5-valerolactone + NADP+ + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
cyclopentanone,NADPH:oxygen oxidoreductase (5-hydroxylating, lactonizing)
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CAS REGISTRY NUMBER
COMMENTARY hide
37364-15-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1R,5S)-8-oxabicyclo[3.2.1]oct-6-en-3-one + NADPH + O2
(1S,6S)-3,9-dioxabicyclo[4.2.1]non-7-en-4-one + NADP+ + H2O
show the reaction diagram
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stereospecific (1S,6S)-product formation
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?
2-methylcyclohexanone + NADPH + O2
1-oxa-2-oxo-3-methylcycloheptane + NADP+ + H2O
show the reaction diagram
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-
-
-
?
4-acetoxy-cyclohexanone + NADPH + O2
4-acetoxy-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
4-acetoxycyclohexanone + NADPH + H+ + O2
5-acetoxyoxepan-2-one + NADP+ + H2O
show the reaction diagram
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-
-
-
?
4-allyl-cyclohexanone + NADPH + O2
4-allyl-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
4-allyloxycyclohexanone + NADPH + H+ + O2
5-allyloxyoxepan-2-one + NADP+ + H2O
show the reaction diagram
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-
-
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?
4-benzyloxycyclohexanone + NADPH + H+ + O2
5-benzyloxyoxepan-2-one + NADP+ + H2O
show the reaction diagram
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-
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?
4-chlorocyclohexanone + NADPH + H+ + O2
5-chlorooxepan-2-one + NADP+ + H2O
show the reaction diagram
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-
-
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?
4-ethoxy-cyclohexanone + NADPH + O2
4-ethoxy-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
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-
-
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?
4-ethoxycyclohexanone + NADPH + H+ + O2
5-ethoxyoxepane-2-one + NADP+ + H2O
show the reaction diagram
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-
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?
4-ethyl-cyclohexanone + NADPH + O2
4-ethyl-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
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?
4-hydroxy-4-allyl-cyclohexanone + NADPH + O2
?
show the reaction diagram
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?
4-hydroxy-4-ethyl-cyclohexanone + NADPH + O2
?
show the reaction diagram
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?
4-hydroxy-4-methyl-cyclohexanone + NADPH + O2
?
show the reaction diagram
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-
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?
4-hydroxy-cyclohexanone + NADPH + O2
4-hydroxy-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
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?
4-methyl-cyclohexanone + NADPH + O2
4-methyl-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
4-n-propyl-cyclohexanone + NADPH + O2
4-n-propyl-hexano-6-lactone + NADP+ + H2O
show the reaction diagram
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?
butan-2-one + NADPH + O2
?
show the reaction diagram
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?
cyclobutanone + NADPH + O2
butyrolactone + NADP+ + H2O
show the reaction diagram
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?
cycloheptanone + NADPH + O2
1-oxa-2-oxocyclooctane + NADP+ + H2O
show the reaction diagram
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poor substrate
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?
cyclohexanone + NADPH + O2
1-oxa-2-oxocycloheptane + NADP+ + H2O
show the reaction diagram
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?
cyclooctanone + NADPH + O2
1-oxa-2-oxocyclononane + NADP+ + H2O
show the reaction diagram
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poor substrate
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?
cyclopentanone + NADPH + H+ + O2
5-valerolactone + NADP+ + H2O
show the reaction diagram
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?
cyclopentanone + NADPH + O2
5-valerolactone + NADP+ + H2O
show the reaction diagram
norbornanone + NADPH + O2
?
show the reaction diagram
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?
additional information
?
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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
cyclopentanone + NADPH + O2
5-valerolactone + NADP+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
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arsenite
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Bathocuproine
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bathophenanthroline
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diethyldithiocarbamate
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iodoacetamide
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p-hydroxymercuribenzoate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
Cyclopentanone
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0.001
O2
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
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alpha4, 4 * 50000, SDS-Page
194000
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ultracentrifugation
200000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
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alpha4, 4 * 50000, SDS-Page
trimer or tetramer
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3 or 4 * 54000-58000, SDS-PAGE
additional information
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
reduction of enzyme by visible light in presence of EDTA
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439017
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expression in Escherichia coli
overexpression in Escherichia coli
overexpression of wild-type and mutant enzymes in Escherichia coli
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overexpression of wild-type and mutants in strains BL121(DE3) and JM109
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F156H/G157L
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
F156L/G157F
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site-directed mutagenesis, the mutations improve the hydrophobic active site pocket increasing enzyme selectivity and stereospecificity
F156N/G157Y
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
F450C
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
F450I
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
G119S/F450Y
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
F156N/G157Y
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
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F450C
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
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F450I
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
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G119S/F450Y
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site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
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additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
immobilization in polyvinylalcohol gel particles is desirable technique with presumptive impact on industrial applications of recombinant whole-cell Baeyer–Villiger monooxygenases as biocatalysts for production of bioactive compounds and precursors of potentially new drugs. An immobilization of Escherichia coli cells with overproduced Baeyer-Villiger monooxygenase improves their stability in repetitive batch biooxidations as compared to free cells. Detected autoinduction of recombinant enzyme in pET22b+ plays a significant role in application of immobilized cells as it may increase specific activity of cells in repetitive use under growing reaction conditions. Original technique for qualitative analysis of enzyme expression within immobilized cells is developed
synthesis