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Literature summary extracted from

  • Kayser, M.M.; Clouthier, C.M.
    New bioorganic reagents: evolved cyclohexanone monooxygenase - why is it more selective? (2006), J. Org. Chem., 71, 8424-8430.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.22 overexpression of wild-type and mutants in strains BL121(DE3) and JM109 Escherichia coli

Protein Variants

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

Natural Substrates/ Products (Substrates)

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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.22 Escherichia coli
-
-
-

Substrates and Products (Substrate)

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 ?
-
 ?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
1.14.13.22 CHMO
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.22 NADPH
-
 Escherichia coli