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Information on EC 1.14.13.16 - cyclopentanone monooxygenase
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EC Tree
1.14.13.16 cyclopentanone monooxygenaseSpecify your search results
Word Map
- 1.14.13.16
-
baeyer-villiger
-
biooxidation
- lactones
-
polyelectrolyte
-
encapsulated
-
enantioselective
- capsules
- flavin
- cyclohexanone
- cellulose
- synthesis
- alginate
-
enantiomeric
-
regioisomeric
-
conversions
- propidium
-
immobilised
-
polyvinyl
-
autofluorescence
-
biocatalysis
- ketone
-
ncimb
- iodide
-
regio
-
halved
- drug development
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
cyclopentanone monooxygenase, cyclopentanone oxygenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CPMO
cyclopentanone oxygenase
-
-
-
-
additional information
additional information
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cf. EC 1.14.13.22, the enzyme belongs to a class of bacterial flavoprotein monooxygenases
additional information
-
cf. EC 1.14.13.22, the enzyme belongs to a class of bacterial flavoprotein monooxygenases
-
additional information
-
the enzyme belongs to the flavin-containing BaeyerVilliger monooxygenases, BVMOs
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cyclopentanone + NADPH + H+ + O2 = 5-valerolactone + NADP+ + H2O
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-
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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
-
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
-
-
cyclopentanone + NADPH + H+ + O2 = 5-valerolactone + NADP+ + H2O
residues Phe450 and Phe156 are important for reaction stereospecificity
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-
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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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-
-
-
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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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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
-
-
stereospecific (1S,6S)-product formation
-
?
2-methylcyclohexanone + NADPH + O2
1-oxa-2-oxo-3-methylcycloheptane + NADP+ + H2O
-
-
-
-
?
2-phenylcyclohexanone + NADPH + H+ + O2
? + NADP+ + H2O
-
high activity with PAMO enzyme mutant P253F/G254A/R258M/L443F, almost no activity with wild-type PAMO (EC 1.14.13.92)
-
-
?
4-acetoxycyclohexanone + NADPH + H+ + O2
5-acetoxyoxepan-2-one + NADP+ + H2O
-
-
-
-
?
4-allyloxycyclohexanone + NADPH + H+ + O2
5-allyloxyoxepan-2-one + NADP+ + H2O
-
-
-
-
?
4-benzyloxycyclohexanone + NADPH + H+ + O2
5-benzyloxyoxepan-2-one + NADP+ + H2O
-
-
-
-
?
4-chlorocyclohexanone + NADPH + H+ + O2
5-chlorooxepan-2-one + NADP+ + H2O
-
-
-
-
?
4-ethoxy-cyclohexanone + NADPH + O2
4-ethoxy-hexano-6-lactone + NADP+ + H2O
-
-
-
-
?
4-ethoxycyclohexanone + NADPH + H+ + O2
5-ethoxyoxepane-2-one + NADP+ + H2O
-
-
-
-
?
4-ethyl-cyclohexanone + NADPH + O2
4-ethyl-hexano-6-lactone + NADP+ + H2O
-
-
-
-
?
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
-
-
?
cyclohexanone + NADPH + O2
1-oxa-2-oxocycloheptane + NADP+ + H2O
-
-
-
-
?
cyclooctanone + NADPH + O2
1-oxa-2-oxocyclononane + NADP+ + H2O
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poor substrate
-
-
?
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
-
-
?
4-acetoxy-cyclohexanone + NADPH + O2
4-acetoxy-hexano-6-lactone + NADP+ + H2O
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low enantioselectivity
-
-
?
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
-
-
-
-
?
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
-
high enantioselectivity with 85% formation of the S-isomer, Ser450 is responsible for the high stereoselectivity
-
-
?
4-hydroxy-cyclohexanone + NADPH + O2
4-hydroxy-hexano-6-lactone + NADP+ + H2O
-
high enantioselectivity with 85% formation of the S-isomer, Ser450 is responsible for the high stereoselectivity
-
-
?
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
-
-
-
-
?
4-methyl-cyclohexanone + NADPH + O2
4-methyl-hexano-6-lactone + NADP+ + H2O
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low enantioselectivity
-
-
?
4-methyl-cyclohexanone + NADPH + O2
4-methyl-hexano-6-lactone + NADP+ + H2O
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low enantioselectivity
-
-
?
4-methyl-cyclohexanone + NADPH + O2
4-methyl-hexano-6-lactone + NADP+ + H2O
-
-
-
?
cyclopentanone + NADPH + H+ + O2
5-valerolactone + NADP+ + H2O
-
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
-
-
-
-
?
cyclopentanone + NADPH + O2
5-valerolactone + NADP+ + H2O
-
-
-
-
?
additional information
?
-
-
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
?
-
-
the enzyme acts as Baeyer-Villiger monooxygenase, substrate specificity and enantioselectivity, overview, 4-tert-butylcyclohexanone is a no substrate
-
-
?
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
-
-
?
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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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
cyclopentanone + NADPH + O2
5-valerolactone + NADP+ + H2O
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-
-
-
?
cyclopentanone + NADPH + O2
5-valerolactone + NADP+ + H2O
-
-
-
-
?
cyclopentanone + NADPH + O2
5-valerolactone + NADP+ + H2O
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.25
2-Octanone
-
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
0.8
2-phenylcyclohexanone
-
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
additional information
additional information
-
steady-state kinetic analysis of the mutant enzyme
-
1000
Cyclopentanone
-
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
2-phenylcyclohexanone
-
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
1.6
Cyclopentanone
-
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.375
2-phenylcyclohexanone
-
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
0.0016
Cyclopentanone
-
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
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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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
phenylacetone monooxygenase enzyme mutant P253F/G254A/R258M/L443F
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzyme belongs to the group I of Baeyer-Villiger monooxygenases (BMVOs)
additional information
-
enzyme molecular docking and molecular dynamics, computational modeling, overview
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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). F4D237_PSEUX
Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 / CB1190)
546
0
61283
TrEMBL
-
A0A084G2B9_PSEDA
528
0
60047
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
200000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
sequence alignment, and structure modelling and comparison to cyclophexanone monooxygenase, EC 1.14.13.22, structure-function analysis
additional information
-
sequence alignment, and structure modelling and comparison to cyclophexanone monooxygenase, EC 1.14.13.22, structure-function analysis
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F156H/G157L
-
site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
F156L/G157F
-
site-directed mutagenesis, the mutations improve the hydrophobic active site pocket increasing enzyme selectivity and stereospecificity
F156N/G157Y
-
site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
F450C
-
site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
F450I
-
site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
G119S/F450Y
-
site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
F156N/G157Y
-
site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
-
F450C
-
site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
-
F450I
-
site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
-
G119S/F450Y
-
site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme
-
additional information
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
additional information
-
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
-
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
-
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
-
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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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
immobilization in polyvinylalcohol gel particles is desirable technique with presumptive impact on industrial applications of recombinant whole-cell BaeyerVilliger 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
synthesis
-
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
-
the Escherichia coli overexpression systems of BaeyerVilliger 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%
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
-
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