Literature summary for 1.14.13.22 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.

Search for more literature for 1.14.13.22

Cloned(Commentary)

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

Inhibitors

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

Organism

Organism	UniProt	Comment	Textmining
Acinetobacter sp.	-	NCIB 9871	-

Purification (Commentary)

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

Reaction

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
CHMO	-	Acinetobacter sp.

Temperature Optimum [°C]

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

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Acinetobacter sp.
NADPH	-	Acinetobacter sp.

Ki Value [mM]

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

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Release 2023.1 (January 2023)