1.14.13.22: cyclohexanone monooxygenase

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

Reaction

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

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Results	in table
3	Activating Compound
667	AA Sequence
23	Application
2	CAS Registry Number
33	Cloned(Commentary)
84	Cofactor
5	Crystallization (Commentary)
3	General Information
1	General Stability
37	Inhibitors
30	kcat/KM [mM/s]
11	Ki Value [mM]
102	KM Value [mM]
6	Localization
1	Metals/Ions
16	Molecular Weight [Da]
51	Natural Substrates/ Products (Substrates)
4	Organic Solvent Stability
171	Organism
1	Oxidation Stability
5	Pathway
14	PDB ID
15	pH Optimum
4	pH Range
6	pH Stability
59	Protein Variants
32	Purification (Commentary)
23	Reaction
11	Reaction Type
102	Reference
2	Source Tissue
28	Specific Activity [micromol/min/mg]
10	Storage Stability
491	Substrates and Products (Substrate)
16	Subunits
65	Synonyms
1	Systematic Name
11	Temperature Optimum [°C]
15	Temperature Stability [°C]
72	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.14.13.22 - cyclohexanone monooxygenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

structure of variant F246Y/K326C/L426F/F432L/T433A/L435S/S438I/F505L complexed with FAD, to 2.2 A resolution

Acinetobacter calcoaceticus

-

763826

microdialysis method, saturated ammonium sulfate solution

Nocardia globerula

-

438984

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

Rhodococcus sp. HI-31

C0STX7

698499

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

Rhodococcus sp. HI-31

C0STX7

741493

-

Thermocrispum municipale

A0A1L1QK39

741605