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Literature summary for 1.14.13.22 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
Search for more literature for 1.14.13.22

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
D41N/F505Y site-directed mutagenesis, the mutant shows altered substrate specificity and enantioselectivity compared to the wild-type enzyme Escherichia coli
F432I site-directed mutagenesis, the mutant shows altered substrate specificity and enantioselectivity compared to the wild-type enzyme Escherichia coli
F432S site-directed mutagenesis, the mutant shows increased substrate specificity and enantioselectivity compared to the wild-type enzyme Escherichia coli
L143F site-directed mutagenesis, the mutant shows altered substrate specificity and enantioselectivity compared to the wild-type enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cyclohexanone + NADPH + O2 Escherichia coli
-
 hexano-6-lactone + NADP+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-allyl-cyclohexanone + NADPH + O2
-
 Escherichia coli 4-allyl-hexano-6-lactone + NADP+ + H2O
-
 ?
4-bromocyclohexanone + NADPH + O2
-
 Escherichia coli 4-bromo-hexano-6-lactone + NADP+ + H2O
-
 ?
4-chlorocyclohexanone + NADPH + O2
-
 Escherichia coli 4-chloro-hexano-6-lactone + NADP+ + H2O
-
 ?
4-ethoxy-cyclohexanone + NADPH + O2
-
 Escherichia coli 4-ethoxy-hexano-6-lactone + NADP+ + H2O
-
 ?
4-ethyl-cyclohexanone + NADPH + O2
-
 Escherichia coli 4-ethyl-hexano-6-lactone + NADP+ + H2O
-
 ?
4-hydroxy-cyclohexanone + NADPH + O2 low enantioselectivity Escherichia coli 4-hydroxy-hexano-6-lactone + NADP+ + H2O
-
 ?
4-iodocyclohexanone + NADPH + O2
-
 Escherichia coli 4-iodo-hexano-6-lactone + NADP+ + H2O
-
 ?
4-methoxy-cyclohexanone + NADPH + O2
-
 Escherichia coli 4-methoxy-hexano-6-lactone + NADP+ + H2O
-
 ?
4-methyl-cyclohexanone + NADPH + O2
-
 Escherichia coli 4-methyl-hexano-6-lactone + NADP+ + H2O
-
 ?
4-n-propyl-cyclohexanone + NADPH + O2
-
 Escherichia coli 4-n-propyl-hexano-6-lactone + NADP+ + H2O
-
 ?
cyclohexanone + NADPH + O2
-
 Escherichia coli hexano-6-lactone + NADP+ + H2O
-
 ?
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

Subunits Comment Organism
More sequence alignment, and structure modelling and comparison to cyclopentanone monooxygenase, EC 1.14.13.16, structure-function analysis Escherichia coli

Synonyms

Synonyms Comment Organism
CHMO
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Escherichia coli