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Literature summary extracted from

  • Sheng, D.; Ballou, D.P.; Massey, V.
    Mechanistic studies of cyclohexanone monooxygenase: chemical properties of intermediates involved in catalysis (2001), Biochemistry, 40, 11156-11167.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.22 expression in Escherichia coli Acinetobacter sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.13.22 NADP+ competitive against NADPH Acinetobacter sp.

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.22 Acinetobacter sp.
-
NCIB 9871
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.22 recombinant from Escherichia coli Acinetobacter sp.

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.22 cyclohexanone + NADPH + H+ + O2 = hexano-6-lactone + NADP+ + H2O reaction mechanism Acinetobacter sp.
1.14.13.22 cyclohexanone + NADPH + H+ + O2 = hexano-6-lactone + NADP+ + H2O kinetic studies Acinetobacter sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.22 cyclohexanone + NADPH + O2 activity limited to cyclic ketones Acinetobacter sp. 6-hexanolide + NADP+ + H2O product: epsilon-caprolactone i.e. 1-oxa-2-oxocycloheptane ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.22 CHMO
-
Acinetobacter sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.22 25
-
assay at Acinetobacter sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.22 FAD
-
Acinetobacter sp.
1.14.13.22 NADPH
-
Acinetobacter sp.

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.14.13.22 0.038
-
NADP+ pH 9.0, 25°C Acinetobacter sp.