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
-
bvmos
-
ncimb
- calcoaceticus
- cyclohexanol
- synthesis
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criegee
- epsilon-caprolactone
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c4a-peroxyflavin
-
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
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Cloned
Cloned on EC 1.14.13.22 - cyclohexanone monooxygenase
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alcohol dehydrogenase(Mesotoga infera)/cyclohexanone monooxygenase(Thermocrispum municipale) fusion construct expressed in Escherichia coli cells
dual expression of alcohol dehydrogenase (from Lactobacillus kefir) and cyclohexanone monooxygenase is achieved in Escherichia coli. Investigation of an approach for optimization of a whole-cell multi-enzyme cascade reaction by applying co-expression of the required cascade enzymes. Using the co-expression strategy, higher conversion values are obtained in whole-cell biocatalysis compared to expression of the cyclohexanone monooxygenase and alcohol dehydrogenase in individual Escherichia coli cells
expressed as His-tag fusion protein in Escherichia coli
expressed in Escherichia coli
expression in bacterial expression system, DNA and amino acid sequence analysis
expression in Escherichia coli
expression in Escherichia coli under control of a strong L-arabinose inducible promoter
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expression in Escherichia coli, amino acid and DNA sequence analysis, identification of potential flavin- and nicotinamide-binding sites
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expression in Escherichia coli, optimization of CHMO expression conditions, high concentrations of cyclohexanone cause the formation of CHMO as inclusion bodies during the reaction period, co-expression with the NADPH-regenerating enzyme glucose 6-phosphate dehydrogenase, overview
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expression in Escherichia coli. A protocol is developed for an optimal and reproducible protein expression in microtiter plates showcased for the expression of the cyclohexanone monooxygenase (CMO) from Acinetobacter sp. NCIMB 9871. By emerging this protocol, several parameters concerning the expression medium, the cultivation temperatures, shaking conditions as well as time and induction periods for CHMO are investigated. A microtiter plate shaker with humidity and temperature control (Cytomat) (integrated in a robotic platform) is employed to obtain an even growth and expression over the plates. An optimized protocol provides a comprehensive overview of the key factors influencing a reproducible protein expression
expression in Escherichia coli. The host organism is found capable of maintaining the NADPH requirements of the enzyme, providing a stable environment with sufficiently high levels of precursors for the protein itself, as well as for essential cofactors. However, due to the low concentration of FAD, it fails to fully saturate cyclohexanone monooxygenase in overexpression
expression of His-tagged enzyme in Escherichia coli and Saccharomyces cerevisiae
gene amplification, cloning in pUC19 vector, transformation in Escherichia coli DH5 of plasmid pCMR100 containing the complete gene chnB1 (1620 bp), amplification of fragment carrying chnB1, cloning into plasmid pSD80 to result in pSDRmchnB1, overexpressed in Escherichia coli BL21 (DE3)
gene chnB, genomic library screening, DNA and amino acid sequence determination and analysis, sequence comparisons, functional expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
PCR-amplification of chnB gene with template vector pMM4, cloning into pEKEx2 shuttle vector, expression in Corynebacterium glutamicum (ATCC13032)
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