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
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1.14.13.22
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baeyer-villiger
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acinetobacter
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lactones
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bvmos
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ncimb
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calcoaceticus
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cyclohexanol
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synthesis
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criegee
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epsilon-caprolactone
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c4a-peroxyflavin
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biooxidation
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bicyclo3.2.0hept-2-en-6-one
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phenylacetone
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cyclopentanone
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biotechnology
- 1.14.13.22
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baeyer-villiger
- acinetobacter
- lactones
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bvmos
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ncimb
- calcoaceticus
- cyclohexanol
- synthesis
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criegee
- epsilon-caprolactone
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c4a-peroxyflavin
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biooxidation
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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
Engineering
Engineering on EC 1.14.13.22 - cyclohexanone monooxygenase
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F246Y/K326C/L426F/F432L/T433A/L435S/S438I/F505L
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substrate specificity is markedly altered from substrate cyclohexanone toward the desired bulky substrate omeprazole sulfide despite an extremely poor activity
F281H
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cultures expressing the F281H variant produce 30 to 40% methyl propanoate, while the wild-type enzyme produce 26% methyl propanoate
I491A
L143P/F246Y/K269E/K326C/L426F/F432L/T433A/L435S/S438I/F505L/N386S/I388K/M390I/E488K/S489C/W490R
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50fold higher activity with substrate substrate omeprazole than mutant F246Y/K326C/L426F/F432L/T433A/L435S/S438I/F505L
L244R
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cultures expressing the L244R variant produce 30 to 40% methyl propanoate, while the wild-type enzyme produce 26% methyl propanoate
L435N
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cultures expressing the L435N variant produce 30 to 40% methyl propanoate, while the wild-type enzyme produce 26% methyl propanoate
T56S
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mutant, which exhibits a higher conversion yield (92%) and kcat (0.5/s) than wild type AcCHMO (52% and 0.3/s, respectively). The uncoupling rate for the T56S mutant is also significantly lower than that for the wild type enzyme
T56S/I491A
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mutant with higher conversion and improved regioselectivity
T56S/L435N/I491A
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mutant produces less total product than wild-type enzyme
A255C/A293C
mutation results in an apparent Tm increase of 1.5°C
A325C/L483C
mutation results in an apparent Tm increase of 1.5°C
D57A
variant retains stereospecificity for the proR hydrogen, substitution results in slow decomposition of the C4a-peroxyflavin intermediate in the presence of cyclohexanone
L323C/A325C
mutation results in an apparent Tm increase of 6°C and a 12fold increased half-life, the stabilizing disulfide bond, L323C/A325C, spans only one residue
R327K
variant lacks stereospecificity for hydride transfer and abstracts either the proR or proS hydrogen from NADPH
T415C
most stable variant with a 30fold increased long-term stability (33% residual activity after 24 h incubation at 25°C), the melting temperature of the variant is increased by 6°C
T415C/A463C
the melting temperature of the variant is increased by 5°C with simultaneous improved long-term stability
Y411C/A463C
the most oxidatively stable variant Y411C-A463C retains nearly 60% activity after incubation with 25 mM H2O2 whereas the wild type retains only 16%
A245G/A288V
variant retains native activity, exhibited about 4.4fold improvement in residual activity after 30°C incubation, and demonstrates about 5fold higher cyclohexanone conversion at 37°C compared to the wild-type
F432I
F432Lm
mutation efficiently reverses the inherent enantiopreference of CHMO in the Baeyer-Villiger oxidation of various 4-phenylcyclohexanone derivatives and 4-alkyl-cyclohexanones, producing a series of substituted lactones with inversed configuration
F432S
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random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
F432Y/K500R
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random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
K78E/F432S
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random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
L426P/A541V
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random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
L435A
mutation efficiently reverses the inherent enantiopreference of CHMO in the Baeyer-Villiger oxidation of various 4-phenylcyclohexanone derivatives and 4-alkyl-cyclohexanones, producing a series of substituted lactones with inversed configuration
L435G
mutation efficiently reverses the inherent enantiopreference of CHMO in the Baeyer-Villiger oxidation of various 4-phenylcyclohexanone derivatives and 4-alkyl-cyclohexanones, producing a series of substituted lactones with inversed configuration
T187A
elimination of the hydrogen bond to the phosphate of the nicotinamide mononucleotide half of NADP(H), 15fold reduction in turnover of cyclohexanone. Mutation does not affect the rate of FAD reduction or the coupling efficiency
W490F
elimination of the hydrogen bond to the ribose of the nicotinamide mononucleotide half of NADP(H), 15fold reduction in turnover of cyclohexanone. Mutation does not affect the rate of FAD reduction or the coupling efficiency
F432I
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random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
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F432S
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random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
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F432Y/K500R
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random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
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L426P/A541V
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random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
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D41N/F505Y
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site-directed mutagenesis, the mutant shows altered substrate specificity and enantioselectivity compared to the wild-type enzyme
F432I
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site-directed mutagenesis, the mutant shows altered substrate specificity and enantioselectivity compared to the wild-type enzyme
F432S
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site-directed mutagenesis, the mutant shows increased substrate specificity and enantioselectivity compared to the wild-type enzyme
L143F
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site-directed mutagenesis, the mutant shows altered substrate specificity and enantioselectivity compared to the wild-type enzyme
E91Q/A115V/R280Y/N431Y/Q439P/A455V/S534R
most stable mutant found, increase in unfolding temperature of 13 K and an approximately 33fold increase in half-life at 30°C
E91Q/D95H/A115V/Q191M/R280Y/N431Y/Q439P/A455V/S534R
increase in melting temperature of 15 K, highly diminished activity
E91Q/D95H/A115V/R280Y/N431Y/Q439P/A455V/S534R
increase in melting temperature of 13 K, highly active
Q409P/N431Y/A115V/A455V
increase in melting temperature of 6.3 K
W492A
14% activity with cyclohexanone compared to wild type enzyme
additional information
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cultures expressing the I491A variant produce 30 to 40% methyl propanoate, while the wild-type enzyme produce 26% methyl propanoate
I491A
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mutant exhibits a significant improvement over the wild type enzyme in the desired regioselectivity using 2-butanone as a substrate (40% vs 26% methyl propanoate, respectively)
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random mutagenesis, the mutant shows altered substrate specificity and increased enantioselectivity compared to the wild-type enzyme
F432I
mutation efficiently reverses the inherent enantiopreference of CHMO in the Baeyer-Villiger oxidation of various 4-phenylcyclohexanone derivatives and 4-alkyl-cyclohexanones, producing a series of substituted lactones with inversed configuration
His-tagged recombinant enzyme expressed in Escherichia coli is, despite the tag, similar to the wild-type enzyme, whereas the recombinant His-tagged enzyme expressed in yeast is posttranslationally modified, Escherichia coli is the preferred expression system
additional information
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screening of random mutants of the enzyme against a library of structurally diverse ketones for modifications in the substrate acceptance profile and stereopreference of the enzymatic Baeyer-Villiger biooxidation, improved and/or divergent stereoselectivities are observed for several substrates, overview
additional information
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screening of random mutants of the enzyme against a library of structurally diverse ketones for modifications in the substrate acceptance profile and stereopreference of the enzymatic Baeyer-Villiger biooxidation, improved and/or divergent stereoselectivities are observed for several substrates, overview
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