1.14.13.22: cyclohexanone monooxygenase

This is an abbreviated version!
For detailed information about cyclohexanone monooxygenase, go to the full flat file.

Word Map on EC 1.14.13.22

Reaction

cyclohexanone
+
NADPH
+
H+
+
O2
=
hexano-6-lactone
+
NADP+
+
H2O

Synonyms

Bpro_556, CAMO, CHMO, ChnB, chnB protein, chnB1 protein, CHXON, CMO, cycloalkaone monooxygenase, cyclohexanone 1, 2-mono-oxygenase, cyclohexanone mono-oxygenase, cyclohexanone monooxygenase, cyclohexanone oxygenase, cyclohexanone:NADPH:oxygen oxidoreductase (lactone-forming), oxygenase, cyclohexanone mono-

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.22 cyclohexanone monooxygenase

Crystallization

Crystallization on EC 1.14.13.22 - cyclohexanone monooxygenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
microdialysis method, saturated ammonium sulfate solution
-
enzyme in complex with FAD and NADP+ in 2 distinct states, hanging drop or sitting drop vapor diffusion methods, crystal form I with 0.2 M sodium acetate trihydrate, 0.1 M sodium cacodylate pH 6.5, and 30% PEG 8000, for crystal form II with 0.2 M magnesium acetate tetrahydrate, 0.1 M sodium cacodylate pH 6.5, and 20% PEG 8000
sitting drop vapor diffusion method. Two crystal structures of cyclohexanone monooxygenase with its product, epsilon-caprolactone, bound: the CHMO(Tight) and CHMO(Loose) structures. The CHMO(Tight) structure represents the enzyme state in which substrate acceptance and stereospecificity is determined, providing a foundation for engineering BVMOs with altered substrate spectra and/or stereospecificity. The CHMO(Loose) structure is the first structure where the product is solvent accessible. This structure represents the enzyme state upon binding and release of the substrate and product