EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.13.22 | overexpression of wild-type and mutants in strains BL121(DE3) and JM109 | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.13.22 | D41N/F505Y | site-directed mutagenesis, the mutant shows altered substrate specificity and enantioselectivity compared to the wild-type enzyme | Escherichia coli |
1.14.13.22 | F432I | site-directed mutagenesis, the mutant shows altered substrate specificity and enantioselectivity compared to the wild-type enzyme | Escherichia coli |
1.14.13.22 | F432S | site-directed mutagenesis, the mutant shows increased substrate specificity and enantioselectivity compared to the wild-type enzyme | Escherichia coli |
1.14.13.22 | L143F | site-directed mutagenesis, the mutant shows altered substrate specificity and enantioselectivity compared to the wild-type enzyme | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.22 | cyclohexanone + NADPH + O2 | Escherichia coli | - |
hexano-6-lactone + NADP+ + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.13.22 | Escherichia coli | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.22 | 4-allyl-cyclohexanone + NADPH + O2 | - |
Escherichia coli | 4-allyl-hexano-6-lactone + NADP+ + H2O | - |
? | |
1.14.13.22 | 4-bromocyclohexanone + NADPH + O2 | - |
Escherichia coli | 4-bromo-hexano-6-lactone + NADP+ + H2O | - |
? | |
1.14.13.22 | 4-chlorocyclohexanone + NADPH + O2 | - |
Escherichia coli | 4-chloro-hexano-6-lactone + NADP+ + H2O | - |
? | |
1.14.13.22 | 4-ethoxy-cyclohexanone + NADPH + O2 | - |
Escherichia coli | 4-ethoxy-hexano-6-lactone + NADP+ + H2O | - |
? | |
1.14.13.22 | 4-ethyl-cyclohexanone + NADPH + O2 | - |
Escherichia coli | 4-ethyl-hexano-6-lactone + NADP+ + H2O | - |
? | |
1.14.13.22 | 4-hydroxy-cyclohexanone + NADPH + O2 | low enantioselectivity | Escherichia coli | 4-hydroxy-hexano-6-lactone + NADP+ + H2O | - |
? | |
1.14.13.22 | 4-iodocyclohexanone + NADPH + O2 | - |
Escherichia coli | 4-iodo-hexano-6-lactone + NADP+ + H2O | - |
? | |
1.14.13.22 | 4-methoxy-cyclohexanone + NADPH + O2 | - |
Escherichia coli | 4-methoxy-hexano-6-lactone + NADP+ + H2O | - |
? | |
1.14.13.22 | 4-methyl-cyclohexanone + NADPH + O2 | - |
Escherichia coli | 4-methyl-hexano-6-lactone + NADP+ + H2O | - |
? | |
1.14.13.22 | 4-n-propyl-cyclohexanone + NADPH + O2 | - |
Escherichia coli | 4-n-propyl-hexano-6-lactone + NADP+ + H2O | - |
? | |
1.14.13.22 | cyclohexanone + NADPH + O2 | - |
Escherichia coli | hexano-6-lactone + NADP+ + H2O | - |
? | |
1.14.13.22 | additional information | substrate specificity and enantioselectivity, overview, the enzyme catalyzes the Baeyer-Villiger oxidations of prochiral 4-substituted ketones, e.g. 4,4-disubstituted cyclohexanones, to the corresponding lactones, configuration of lactone products, 4-tert-butylcyclohexanone is a poor substrate for wild-type and mutant enzymes, no activity with 4-hydroxy-4-phenylcyclohexanone of wild-type enzyme and mutant F432S, 4-tert-butylcyclohexanone is a poor substrate | Escherichia coli | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.13.22 | More | sequence alignment, and structure modelling and comparison to cyclopentanone monooxygenase, EC 1.14.13.16, structure-function analysis | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.13.22 | CHMO | - |
Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.22 | NADPH | - |
Escherichia coli |