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Enzyme Nomenclature
Information on EC 1.14.13.16 - cyclopentanone monooxygenase
Word Map on EC 1.14.13.16
- 1.14.13.16
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baeyer-villiger
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lactone
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biooxidation
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enantioselective
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polyelectrolyte
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syntheses
- cyclohexanone
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whole-cell
- synthesis
- acetyl-coa
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encapsulated
- alginate
- flavin
- ketone
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regio
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regioisomeric
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polyvinyl
- capsules
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biotransformation
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immobilised
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chirality
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ncimb
- cellulose
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biocatalysis
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.16
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RECOMMENDED NAME
GeneOntology No.
cyclopentanone monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cyclopentanone + NADPH + H+ + O2 = 5-valerolactone + NADP+ + H2O
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cyclopentanone + NADPH + H+ + O2 = 5-valerolactone + NADP+ + H2O
reaction mechanism via key intermediate flavin C4a-peroxide, involving the four-electron reduction of O2 at the expense of a two-electron oxidation of NADPH and a two-electron oxidation of cyclohexanone to epsilon-caprolactone, overview
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cyclopentanone + NADPH + H+ + O2 = 5-valerolactone + NADP+ + H2O
residues Phe450 and Phe156 are important for reaction stereospecificity
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cyclopentanone + NADPH + H+ + O2 = 5-valerolactone + NADP+ + H2O
reaction mechanism via key intermediate flavin C4a-peroxide, involving the four-electron reduction of O2 at the expense of a two-electron oxidation of NADPH and a two-electron oxidation of cyclohexanone to epsilon-caprolactone, overview; residues Phe450 and Phe156 are important for reaction stereospecificity
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
37364-15-1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
(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
2-methylcyclohexanone + NADPH + O2
1-oxa-2-oxo-3-methylcycloheptane + NADP+ + H2O
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?
4-ethoxy-cyclohexanone + NADPH + O2
4-ethoxy-hexano-6-lactone + NADP+ + H2O
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-
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?
4-ethyl-cyclohexanone + NADPH + O2
4-ethyl-hexano-6-lactone + NADP+ + H2O
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?
4-methoxy-cyclohexanone + NADPH + O2
4-methoxy-hexano-6-lactone + NADP+ + H2O
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?
4-n-propyl-cyclohexanone + NADPH + O2
4-n-propyl-hexano-6-lactone + NADP+ + H2O
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?
cycloheptanone + NADPH + O2
1-oxa-2-oxocyclooctane + NADP+ + H2O
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poor substrate
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-
?
cyclohexanone + NADPH + O2
1-oxa-2-oxocycloheptane + NADP+ + H2O
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?
cyclooctanone + NADPH + O2
1-oxa-2-oxocyclononane + NADP+ + H2O
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poor substrate
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-
?
(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
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stereospecific (1S,6S)-product formation
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?
(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
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stereospecific (1S,6S)-product formation
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?
4-acetoxy-cyclohexanone + NADPH + O2
4-acetoxy-hexano-6-lactone + NADP+ + H2O
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?
4-acetoxy-cyclohexanone + NADPH + O2
4-acetoxy-hexano-6-lactone + NADP+ + H2O
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low enantioselectivity
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?
4-acetoxy-cyclohexanone + NADPH + O2
4-acetoxy-hexano-6-lactone + NADP+ + H2O
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low enantioselectivity
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?
4-acetoxy-cyclohexanone + NADPH + O2
4-acetoxy-hexano-6-lactone + NADP+ + H2O
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?
4-acetoxycyclohexanone + NADPH + H+ + O2
5-acetoxyoxepan-2-one + NADP+ + H2O
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?
4-acetoxycyclohexanone + NADPH + H+ + O2
5-acetoxyoxepan-2-one + NADP+ + H2O
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?
4-allyl-cyclohexanone + NADPH + O2
4-allyl-hexano-6-lactone + NADP+ + H2O
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?
4-allyl-cyclohexanone + NADPH + O2
4-allyl-hexano-6-lactone + NADP+ + H2O
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?
4-allyloxycyclohexanone + NADPH + H+ + O2
5-allyloxyoxepan-2-one + NADP+ + H2O
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?
4-allyloxycyclohexanone + NADPH + H+ + O2
5-allyloxyoxepan-2-one + NADP+ + H2O
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?
4-benzyloxycyclohexanone + NADPH + H+ + O2
5-benzyloxyoxepan-2-one + NADP+ + H2O
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?
4-benzyloxycyclohexanone + NADPH + H+ + O2
5-benzyloxyoxepan-2-one + NADP+ + H2O
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?
4-chlorocyclohexanone + NADPH + H+ + O2
5-chlorooxepan-2-one + NADP+ + H2O
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?
4-chlorocyclohexanone + NADPH + H+ + O2
5-chlorooxepan-2-one + NADP+ + H2O
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?
4-ethoxycyclohexanone + NADPH + H+ + O2
5-ethoxyoxepane-2-one + NADP+ + H2O
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?
4-ethoxycyclohexanone + NADPH + H+ + O2
5-ethoxyoxepane-2-one + NADP+ + H2O
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?
4-hydroxy-cyclohexanone + NADPH + O2
4-hydroxy-hexano-6-lactone + NADP+ + H2O
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?
4-hydroxy-cyclohexanone + NADPH + O2
4-hydroxy-hexano-6-lactone + NADP+ + H2O
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high enantioselectivity with 85% formation of the S-isomer, Ser450 is responsible for the high stereoselectivity
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?
4-hydroxy-cyclohexanone + NADPH + O2
4-hydroxy-hexano-6-lactone + NADP+ + H2O
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high enantioselectivity with 85% formation of the S-isomer, Ser450 is responsible for the high stereoselectivity
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?
4-hydroxy-cyclohexanone + NADPH + O2
4-hydroxy-hexano-6-lactone + NADP+ + H2O
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?
4-methyl-cyclohexanone + NADPH + O2
4-methyl-hexano-6-lactone + NADP+ + H2O
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?
4-methyl-cyclohexanone + NADPH + O2
4-methyl-hexano-6-lactone + NADP+ + H2O
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low enantioselectivity
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?
4-methyl-cyclohexanone + NADPH + O2
4-methyl-hexano-6-lactone + NADP+ + H2O
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low enantioselectivity
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?
4-methyl-cyclohexanone + NADPH + O2
4-methyl-hexano-6-lactone + NADP+ + H2O
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?
4-methyl-cyclohexanone + NADPH + O2
4-methyl-hexano-6-lactone + NADP+ + H2O
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?
cyclopentanone + NADPH + O2
5-valerolactone + NADP+ + H2O
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?
cyclopentanone + NADPH + O2
5-valerolactone + NADP+ + H2O
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?
cyclopentanone + NADPH + O2
5-valerolactone + NADP+ + H2O
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?
additional information
?
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the enzyme acts as Baeyer-Villiger monooxygenase, substrate specificity and enantioselectivity of wild-type and mutant enzymes, structure-function analysis and comparison to cyclohexanone monooxygenase, EC 1.14.13.22, residues Phe450 and Phe156 are important, overview
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additional information
?
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the enzyme acts as Baeyer-Villiger monooxygenase, substrate specificity and enantioselectivity, overview, 4-tert-butylcyclohexanone is a no substrate
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additional information
?
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the enzyme acts as Baeyer-Villiger monooxygenase, substrate specificity and enantioselectivity, overview, 4-tert-butylcyclohexanone is a no substrate
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additional information
?
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the enzyme acts as Baeyer-Villiger monooxygenase, substrate specificity and enantioselectivity of wild-type and mutant enzymes, structure-function analysis and comparison to cyclohexanone monooxygenase, EC 1.14.13.22, residues Phe450 and Phe156 are important, overview
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
cyclopentanone + NADPH + O2
5-valerolactone + NADP+ + H2O
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?
cyclopentanone + NADPH + O2
5-valerolactone + NADP+ + H2O
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?
cyclopentanone + NADPH + O2
5-valerolactone + NADP+ + H2O
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
200000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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sequence alignment, and structure modelling and comparison to cyclophexanone monooxygenase, EC 1.14.13.22, structure-function analysis
additional information
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sequence alignment, and structure modelling and comparison to cyclophexanone monooxygenase, EC 1.14.13.22, structure-function analysis
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
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
additional information
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mutations in the active site residues responsible for stereoselectivity is a shortcut to an improvement in enantioselectivity in the often unselective CPMO, the combination of rational design and random mutagenesis at the predefined positions gives rise to focused libraries for improvement of the catalytic performance of enzymes, including enhanced enantioselectivity, using Complete Active Site Saturation Test, CAST, overview
additional information
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active site mutations to improve enantioselectivity of the enzyme towards 4-substituted cyclohexanone substrates, method evaluation, overview, the effect of mutation of residues 449 and 450 does not have a full impact on the improvement of the hydrophobic pocket
additional information
-
active site mutations to improve enantioselectivity of the enzyme towards 4-substituted cyclohexanone substrates, method evaluation, overview, the effect of mutation of residues 449 and 450 does not have a full impact on the improvement of the hydrophobic pocket; mutations in the active site residues responsible for stereoselectivity is a shortcut to an improvement in enantioselectivity in the often unselective CPMO, the combination of rational design and random mutagenesis at the predefined positions gives rise to focused libraries for improvement of the catalytic performance of enzymes, including enhanced enantioselectivity, using Complete Active Site Saturation Test, CAST, overview
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additional information
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completion of the formal total synthesis of (+)-showdomycin and establishing of the absolute configuration of biooxidation product as (1S,6S)-3,9-dioxabicyclo[4.2.1]non-7-en-4-one, overview
additional information
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completion of the formal total synthesis of (+)-showdomycin and establishing of the absolute configuration of biooxidation product as (1S,6S)-3,9-dioxabicyclo[4.2.1]non-7-en-4-one, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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the enzyme can be used for accessing tetrahydrofuran-based natural products by stereoselective Baeyer-Villiger biooxidation, in particular for the formation of chiral lactones, natural compound synthesis, completion of the formal total synthesis of (+)-showdomycin and establishing of the absolute configuration of biooxidation product as (1S,6S)-3,9-dioxabicyclo[4.2.1]non-7-en-4-one, overview
synthesis
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the Escherichia coli overexpression systems of Baeyer–Villiger monooxygenases, cyclohexanone monooxygenase and cyclopentanone monooxygenase and their mutants derived from directed evolution are used as catalysts in oxidations of six 4-substituted cyclohexanones. Several substrates that give negative results with growing cells, afford excellent conversions in the transformations under non-growing conditions
synthesis
Baeyer-Villiger biooxidation of 4-methylcyclohexanone to 5-methyloxepane-2-one catalysed by recombinant Escherichia coli overexpressing cyclopentanone monooxygenase encapsulated in polyelectrolyte complex capsules. Viability of encapsulated cells decreases with increasing substrate concentration from 99 to 83%, while substrate conversions decrease from 100 to 6%. Storage stabilization of encapsulated cells is observed by increased substrate conversion form 68 to 96%
synthesis
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Baeyer-Villiger biooxidation of 4-methylcyclohexanone to 5-methyloxepane-2-one catalysed by recombinant Escherichia coli overexpressing cyclopentanone monooxygenase encapsulated in polyelectrolyte complex capsules. Viability of encapsulated cells decreases with increasing substrate concentration from 99 to 83%, while substrate conversions decrease from 100 to 6%. Storage stabilization of encapsulated cells is observed by increased substrate conversion form 68 to 96%; the enzyme can be used for accessing tetrahydrofuran-based natural products by stereoselective Baeyer-Villiger biooxidation, in particular for the formation of chiral lactones, natural compound synthesis, completion of the formal total synthesis of (+)-showdomycin and establishing of the absolute configuration of biooxidation product as (1S,6S)-3,9-dioxabicyclo[4.2.1]non-7-en-4-one, overview; the Escherichia coli overexpression systems of Baeyer–Villiger monooxygenases, cyclohexanone monooxygenase and cyclopentanone monooxygenase and their mutants derived from directed evolution are used as catalysts in oxidations of six 4-substituted cyclohexanones. Several substrates that give negative results with growing cells, afford excellent conversions in the transformations under non-growing conditions
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.16)
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