Cyclohexanone Monooxygenase from Acinetobacter sp.

Cyclohexanone monooxygenase has been used in a study that cloned and overexpressed the 2-oxo-Δ(3)-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase (OTEMO) in Escherichia coli. Cyclohexanone monooxygenase has also been used in a study that investigated the effects of structural modification of the cell wall on the biotransformation capability by recombinant Corynebacterium glutamicum cells.

Purified cyclohexanone monooxygenase has a molecular weight of 59,000 Da. It is a versatile oxygenation catalyst. The enzyme uses the bound FAD-4a-OOH oxygenating intermediate to initiate transfer of oxygen to electrophilic substrate sites. The reaction consequently yields the corresponding sulfoxide and selenoxide products. This enzyme is also capable of oxygenating at nitrogen, trivalent phosphorus, and boron sites in boronic acids. Hence, it is one of the most broad-based flavoprotein oxygenases known.

Suspension in 80% saturated ammonium sulfate, 20 mM K-Na-phosphate buffer pH 7, 3.5 mM 1,4-Dithioerythritol (DTE)

1 unit corresponds to the amount of enzyme which catalyzes the cyclohexanone-stimulated oxidation of 1 μmol of NADPH per minute at pH 9.0 and 30 °C