1.14.13.22: cyclohexanone monooxygenase
This is an abbreviated version!
For detailed information about cyclohexanone monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.22
-
1.14.13.22
-
baeyer-villiger
-
acinetobacter
-
lactones
-
bvmos
-
ncimb
-
calcoaceticus
-
cyclohexanol
-
synthesis
-
criegee
-
epsilon-caprolactone
-
c4a-peroxyflavin
-
biooxidation
-
bicyclo3.2.0hept-2-en-6-one
-
phenylacetone
-
cyclopentanone
-
biotechnology
- 1.14.13.22
-
baeyer-villiger
- acinetobacter
- lactones
-
bvmos
-
ncimb
- calcoaceticus
- cyclohexanol
- synthesis
-
criegee
- epsilon-caprolactone
-
c4a-peroxyflavin
-
biooxidation
-
bicyclo3.2.0hept-2-en-6-one
- phenylacetone
- cyclopentanone
- biotechnology
Reaction
Synonyms
Bpro_556, CAMO, CHMO, ChnB, chnB protein, chnB1 protein, CHXON, CMO, cycloalkaone monooxygenase, cyclohexanone 1, 2-mono-oxygenase, cyclohexanone mono-oxygenase, cyclohexanone monooxygenase, cyclohexanone oxygenase, cyclohexanone:NADPH:oxygen oxidoreductase (lactone-forming), oxygenase, cyclohexanone mono-
ECTree
Advanced search results
Application
Application on EC 1.14.13.22 - cyclohexanone monooxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
analysis
biotechnology
synthesis
application of an aerobic, high-throughput growth selection platform in Escherichia coli for the discovery of thermostability enhancing mutations for CHMO. The selection employs growth for the easy readout of CHMO activity in vivo, by requiring nicotinamide adenine dinucleotide phosphate (NADPH)-consuming enzymes to restore cellular redox balance
analysis
-
effective halo-based selection method for mutant proteins using the solubility difference between the substrate (omeprazole sulfide) and product (esomeprazole)
analysis
protocol for linker design for beneficial effects on expression levels, enzyme stability and/or enzyme performance. Analysis of the effect of the length of a glycine-rich linker for the epsilon-caprolactone synthesis through an alcohol dehydrogenase-cyclohexanone monooxygenase fusion system
analysis
-
protocol for linker design for beneficial effects on expression levels, enzyme stability and/or enzyme performance. Analysis of the effect of the length of a glycine-rich linker for the epsilon-caprolactone synthesis through an alcohol dehydrogenase-cyclohexanone monooxygenase fusion system
-
-
biocatalysis system for Baeyer-Villiger oxidations, the average specific oxidation rate and product molar yield based on reaction substrate reaches 0.15 g/g dry cells/h (21.9 micromol/min/g of dry cells), at high cell densities (20 g dry cells/l) the specific product formation rate is lower with 0.12 g/g dry cells/h and 17.5 micromol/min/g of dry cells (probably due to low availability of the energy source glucose), though absolute yield is 2fold higher
biotechnology
-
biocatalysis system for Baeyer-Villiger oxidations, the average specific oxidation rate and product molar yield based on reaction substrate reaches 0.15 g/g dry cells/h (21.9 micromol/min/g of dry cells), at high cell densities (20 g dry cells/l) the specific product formation rate is lower with 0.12 g/g dry cells/h and 17.5 micromol/min/g of dry cells (probably due to low availability of the energy source glucose), though absolute yield is 2fold higher
-
-
production of optically pure sulfoxides by biotransformation in whole cell systems of several sulfides, dithianes and dithiolanes
synthesis
-
chiral catalysis for the laboratory-scale transformation of racemic and prochiral ketones to chiral lactones and organic sulfur compounds to optically active sulfoxides, as a whole cell preparation and as an isolated immobilized enzyme
synthesis
-
the enzyme in crude extract can be used for synthesis of enantiopure lactones, development of a simple and easy to handle method including a coupled NADPG regeneration system
synthesis
-
model enantioselective Baeyer-Villiger biooxidations of rac-bicyclo[3.2.0]hept-2-en-6-one to corresponding lactones (1R,5S)-3-oxabicyclo-[3.3.0]oct-6-en-3-one and (1S,5R)-2-oxabicyclo-[3.3.0]oct-6-en-3-one as important chiral synthons for the synthesis of bioactive compounds. Reactions are performed in the minireactor equipped with a column packed with encapsulated recombinant cells Escherichia coli overexpressing cyclohexanone monooxygenase. The cells are encapsulated in polyelectrolyte complex capsules formed by reaction of oppositely charged polymers. Encapsulated cells tested in inireactor exhibit high operational stability with 4 complete substrate conversions to products and 6 conversions above 80% within 14 repeated consecutive biooxidation tests. Encapsulated cells show high enzyme stability during 91 days of storage with substrate conversions above 80% up to 60 days of storage
synthesis
a fusion protein that can convert cyclohexanol to epsilon-caprolactone in vitro is created. The alcohol dehydrogenase(Mesotoga infera)/cyclohexanone monooxygenase(Thermocrispum municipale) fusion construct is expressed in Escherichia coli cells. By circumventing substrate and product inhibition, a more than 99% conversion of 200 mM cyclohexanol can be achieved in 24 h, with more than 13000 turnovers per fusion enzyme molecule
synthesis
cyclohexanone monooxygenase (CHMO) from Acinetobacter sp. NCIMB 9871 is a prototype Baeyer-Villiger monooxygenases (BVMO). The enzyme shows an impressive substrate scope with a high chemo-, regio- and/or enantioselectivity. BVMO reactions are often difficult, if not impossible to achieve by chemical approaches and this makes these enzymes highly desired candidates for industrial applications. The industrial use is hampered by several factors related to the lack of stability of these biocatalysts. An easy computational method is used for the prediction of stabilizing disulfide bonds in the cyclohexanone monooxygenase-scaffold. The most promising predicted disulfide pairs are created and biochemically characterized. The T415C single point variant is the most stable variant with a 30fold increased long-term stability (33% residual activity after 24 h incubation at 25°C)
synthesis
synthesis od lactones from cycloalkanes. A heterologous pathway comprising enzymes with compatible kinetics is designed in Pseudomonas taiwanensis VLB120 enabling in-vivo cascade for synthesizing lactones from cycloalkanes. The respective pathway includes cytochrome P450 monooxygenase (CHX), cyclohexanol dehydrogenase (CDH), and cyclohexanone monooxygenase (CHXON) from Acidovorax sp. CHX100. Resting cells of the recombinant host Pseudomonas taiwanensis VLB120 convert cyclohexane, cyclohexanol, and cyclohexanone to epsilon-caprolactone at 22, 80-100, and 170 U/g cell dry weight, respectively. Cyclohexane (5 mM) is completely converted with a selectivity of 65% for epsilon-caprolactone formation in 2 h without accumulation of intermediate products
synthesis
-
the enzyme catalyzes the Baeyer-Villiger oxidation of 2-butanone, yielding ethyl acetate and methyl propanoate as products. Methyl propanoate is of industrial interest as a precursor of acrylic plastic. Various residues near the substrate and NADP+ binding sites are subjected to saturation mutagenesis to enhance both the activity on 2-butanone and the regioselectivity toward methyl propanoate
synthesis
analysis of conversion kinetics for isolated enzyme, suspended whole cells, and biofilms, the latter two based on recombinant CHMO-containing P. taiwanensis VLB120. Biofilms show less favorable values for KS (9.3fold higher) and kcat (4.8fold lower) compared with corresponding KM and kcat values of isolated CHMO, but a favorable KI for cyclohexanone (5.3fold higher). Suspended cells show only 1.8fold higher KS, but 1.3- and 4.2fold higher kcat and KI values than isolated CHMO
synthesis
extracellular production of engineered CHMO by Pichia pastoris. The recombinant CHMO shows a higher flavin occupation rate than that produced by Escherichia coli, accompanied by a 3.2fold increase in catalytic efficiency. At a cell density of 150 g/l cell dry weight, a recombinant CHMO production rate of 1,700 U/l is achieved. By directly employing the pH adjusted supernatant as a biocatalyst, 10 g/l of pyrmetazole is almost completely transformed into the corresponding (S)-sulfoxide, with > 99% enantiomeric excess
synthesis
synthesis of lactones from cycloalkanes in Pseudomonas taiwanensis VLB120. The pathway includes cytochrome P450 monooxygenase, cyclohexanol dehydrogenase, and cyclohexanone monooxygenase from Acidovorax sp. CHX100. Recombinant P. taiwanensis converts cyclohexane, cyclohexanol, and cyclohexanone to epsilon-caprolactone at 22, 80-100, and 170 U/gCDW, respectively. Cyclohexane (5 mM) is completely converted with a selectivity of 65% for epsilon-caprolactone formation in 2 hr without accumulation of intermediate products. Analogous lactones can be obtained from cyclooctane and cyclodecane
synthesis
synthesis of trimethyl-epsilon-caprolactone using cyclohexanone monooxygenase immobilized on Mana-agarose and a highly active glucose dehydrogenase for cofactor regeneration. A biocatalyst yield of 37.3 g trimethyl-epsilon-caprolactone per g of CHMO and 474.2 g trimethyl-epsilon-caprolactone per g of glucose dehydrogenase are obtained
synthesis
-
synthesis of trimethyl-epsilon-caprolactone using cyclohexanone monooxygenase immobilized on Mana-agarose and a highly active glucose dehydrogenase for cofactor regeneration. A biocatalyst yield of 37.3 g trimethyl-epsilon-caprolactone per g of CHMO and 474.2 g trimethyl-epsilon-caprolactone per g of glucose dehydrogenase are obtained
-
synthesis
-
model enantioselective Baeyer-Villiger biooxidations of rac-bicyclo[3.2.0]hept-2-en-6-one to corresponding lactones (1R,5S)-3-oxabicyclo-[3.3.0]oct-6-en-3-one and (1S,5R)-2-oxabicyclo-[3.3.0]oct-6-en-3-one as important chiral synthons for the synthesis of bioactive compounds. Reactions are performed in the minireactor equipped with a column packed with encapsulated recombinant cells Escherichia coli overexpressing cyclohexanone monooxygenase. The cells are encapsulated in polyelectrolyte complex capsules formed by reaction of oppositely charged polymers. Encapsulated cells tested in inireactor exhibit high operational stability with 4 complete substrate conversions to products and 6 conversions above 80% within 14 repeated consecutive biooxidation tests. Encapsulated cells show high enzyme stability during 91 days of storage with substrate conversions above 80% up to 60 days of storage
-
synthesis
-
the enzyme in crude extract can be used for synthesis of enantiopure lactones, development of a simple and easy to handle method including a coupled NADPG regeneration system
-