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cyclopentanone + NADPH + H+ + O2 = 5-valerolactone + NADP+ + H2O
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
the reaction mechanism of BVMO with native substrate phenylacetone proceeds via the formation of a Criegee intermediate with anionic character, which is subsequently rearranged via the migration of alkyl group to yield the product ester, reaction mechanism, overview
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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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(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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?
2-methylcyclohexanone + NADPH + O2
1-oxa-2-oxo-3-methylcycloheptane + NADP+ + H2O
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?
2-octanone + NADPH + H+ + O2
heptylacetate + NADP+ + H2O
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?
2-phenylcyclohexanone + NADPH + H+ + O2
? + NADP+ + H2O
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high activity with PAMO enzyme mutant P253F/G254A/R258M/L443F, almost no activity with wild-type PAMO (EC 1.14.13.92)
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-
?
4-acetoxy-cyclohexanone + NADPH + O2
4-acetoxy-hexano-6-lactone + NADP+ + H2O
4-acetoxycyclohexanone + NADPH + H+ + O2
5-acetoxyoxepan-2-one + NADP+ + H2O
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-
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?
4-allyl-cyclohexanone + NADPH + O2
4-allyl-hexano-6-lactone + NADP+ + H2O
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-chlorocyclohexanone + NADPH + H+ + O2
5-chlorooxepan-2-one + NADP+ + H2O
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-
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?
4-ethoxy-cyclohexanone + NADPH + O2
4-ethoxy-hexano-6-lactone + NADP+ + H2O
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?
4-ethoxycyclohexanone + NADPH + H+ + O2
5-ethoxyoxepane-2-one + NADP+ + H2O
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?
4-ethyl-cyclohexanone + NADPH + O2
4-ethyl-hexano-6-lactone + NADP+ + H2O
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?
4-hydroxy-4-allyl-cyclohexanone + NADPH + O2
?
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?
4-hydroxy-4-ethyl-cyclohexanone + NADPH + O2
?
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?
4-hydroxy-4-methyl-cyclohexanone + NADPH + O2
?
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?
4-hydroxy-cyclohexanone + NADPH + O2
4-hydroxy-hexano-6-lactone + NADP+ + H2O
4-methoxy-cyclohexanone + NADPH + O2
4-methoxy-hexano-6-lactone + NADP+ + H2O
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?
4-methyl-cyclohexanone + NADPH + O2
4-methyl-hexano-6-lactone + NADP+ + H2O
4-n-propyl-cyclohexanone + NADPH + O2
4-n-propyl-hexano-6-lactone + NADP+ + H2O
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?
butan-2-one + NADPH + O2
?
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?
cyclobutanone + NADPH + O2
butyrolactone + 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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?
cyclopentanone + NADPH + H+ + O2
5-valerolactone + NADP+ + H2O
cyclopentanone + NADPH + O2
5-valerolactone + NADP+ + H2O
norbornanone + NADPH + O2
?
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?
additional information
?
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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-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-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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?
cyclopentanone + NADPH + H+ + O2

5-valerolactone + NADP+ + H2O
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?
cyclopentanone + NADPH + H+ + O2
5-valerolactone + NADP+ + H2O
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?
cyclopentanone + NADPH + H+ + O2
5-valerolactone + NADP+ + H2O
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high activity with PAMO enzyme mutant P253F/G254A/R258M/L443F, almost no activity with wild-type PAMO (EC 1.14.13.92)
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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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?
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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?
additional information
?
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the engineered phenylacetone monooxygenase (EC 1.14.13.92) enzyme mutant P253F/G254A/R258M/L443F has almost lost its activity with phenylacetone, but shows higher activity with cyclopentanone instead. Substrate binding analysis, overview
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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

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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
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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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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
-
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
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additional information
-
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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Griffin, M.; Trudgill, P.W.
The metabolism of cyclopentanol by Pseudomonas N.C.I.B. 9872
Biochem. J.
129
595-603
1972
Pseudomonas sp.
brenda
Griffin, M.; Trudgill, P.W.
Purification and properties of cyclopentanone oxygenase of Pseudomonas NCIB 9872
Eur. J. Biochem.
63
199-209
1976
Pseudomonas sp.
brenda
Griffin, M.; Trudgill, P.W.
The purification of cyclopentanone oxygenase from Pseudomonas N.C.I.B.9872
Biochem. Soc. Trans.
1
1255-1258
1973
Pseudomonas sp.
-
brenda
Trudgill, P.W.
Cyclopentanone 1,2-monooxygenase from Pseudomonas N.C.I.B. 9872
Methods Enzymol.
188
77-81
1990
Pseudomonas sp.
brenda
Bes, M.T.; Roberts, S.M.; Wan, P.W.H.
Oxidative biotransformations by microorganisms: production of chiral synthons by cyclopentanone monooxygenase from Pseudomonas N.C.I.B. 9872
J. Mol. Catal. , B Enzym.
1
127-134
1996
Pseudomonas sp.
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brenda
Iwaki, H.; Hasegawa, Y.; Wang, S.; Kayser, M.M.; Lau, P.C.K.
Cloning and characterization of a gene cluster involved in cyclopentanol metabolism in Comamonas sp. strain N.C.I.M.B. 9872 and biotransformations effected by Eschericha coli-expressed cyclopentanone 1,2-monooxygenase
Appl. Environ. Microbiol.
68
5671-5684
2002
Comamonas sp.
brenda
Wang, S.; Kayser, M.M.; Iwaki, H.; Lau, P.C.K.
Monooxygenase-catalyzed Baeyer-Villiger oxidations: CHMO versus CPMO
J. Mol. Catal. B
22
211-218
2003
Comamonas sp.
-
brenda
Mihovilovic, M.D.; Bianchi, D.A.; Rudroff, F.
Accessing tetrahydrofuran-based natural products by microbial Baeyer-Villiger biooxidation
Chem. Commun. (Camb. )
1
3214-3216
2006
Comamonas sp.
brenda
Clouthier, C.M.; Kayser, M.M.; Reetz, M.T.
Designing new Baeyer-Villiger monooxygenases using restricted CASTing
J. Org. Chem.
71
8431-8437
2006
Acinetobacter sp., Acinetobacter sp. NCIB 9871
brenda
Clouthier, C.M.; Kayser, M.M.
Increasing the enantioselectivity of cyclopentanone monooxygenase (CPMO): profile of new CPMO mutants
Tetrahedron Asymmetry
17
2649-2653
2006
Acinetobacter sp., Acinetobacter sp. NCIB 9871
-
brenda
Clouthier, C.M.; Kayser, M.M.
Biotransformations with engineered E. coli cells expressing wild-type and mutant Baeyer-Villiger monooxygenases under non-growing conditions
J. Mol. Catal. B
46
32-36
2007
Comamonas sp.
-
brenda
Schenkmayerova, A.; Bucko, M.; Gemeiner, P.; Katrlik, J.
Microbial monooxygenase amperometric biosensor for monitoring of Baeyer-Villiger biotransformation
Biosens. Bioelectron.
50
235-238
2013
Comamonas sp. (Q8GAW0)
brenda
Rebros, M.; Liptak, L.; Rosenberg, M.; Bucko, M.; Gemeiner, P.
Biocatalysis with Escherichia coli-overexpressing cyclopentanone monooxygenase immobilized in polyvinyl alcohol gel
Lett. Appl. Microbiol.
58
556-563
20