KEGG   ENZYME: 1.14.13.22Help
Entry
EC 1.14.13.22               Enzyme                                 

Name
cyclohexanone monooxygenase;
cyclohexanone 1,2-monooxygenase;
cyclohexanone oxygenase;
cyclohexanone:NADPH:oxygen oxidoreductase (6-hydroxylating, 1,2-lactonizing)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
cyclohexanone,NADPH:oxygen oxidoreductase (lactone-forming)
Reaction(IUBMB)
cyclohexanone + NADPH + H+ + O2 = hexano-6-lactone + NADP+ + H2O [RN:R02231]
Reaction(KEGG)
R02231;
(other) R06622
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Substrate
cyclohexanone [CPD:C00414];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
hexano-6-lactone [CPD:C01880];
NADP+ [CPD:C00006];
H2O [CPD:C00001]
Comment
A flavoprotein (FAD). In the catalytic mechanism of this enzyme, the nucleophilic species that attacks the carbonyl group is a peroxyflavin intermediate that is generated by reaction of the enzyme-bound flavin cofactor with NAD(P)H and oxygen [2]. This enzyme is able to catalyse a wide range of oxidative reactions, including enantioselective Baeyer-Villiger reactions [3], sulfoxidations [4], amine oxidations [5] and epoxidations [6].
History
EC 1.14.13.22 created 1984, modified 2004
Pathway
ec00930  Caprolactam degradation
ec01120  Microbial metabolism in diverse environments
Orthology
K03379  cyclohexanone monooxygenase
Genes
PIC: PICST_52278(FMO3) PICST_57936(FMO5)
MGR: MGG_06577
NHE: NECHADRAFT_48101 NECHADRAFT_54743 NECHADRAFT_82172
MAJ: MAA_06594
CMT: CCM_02795
MBE: MBM_08709
AFM: AFUA_2G09400
ANG: ANI_1_1806104(An12g05000)
AFV: AFLA_041640 AFLA_045600
ACT: ACLA_081190
LAB: LA76x_3343(chnB)
LAQ: GLA29479_2376(chnB)
PMY: Pmen_2620
PPX: T1E_5541
MAQ: Maqu_3819
POL: Bpro_5565
AJS: Ajs_2102
SCL: sce4944
NAR: Saro_0510
PUB: SAR11_0845(smo)
MBB: BCG_1454c
MAVI: RC58_01260
NDA: Ndas_5034
FAL: FRAAL3387
SEN: SACE_2596
PDX: Psed_0488
PSEA: WY02_02785
PSEH: XF36_18620
 » show all
Taxonomy
Reference
1  [PMID:1261545]
  Authors
Donoghue NA, Norris DB, Trudgill PW.
  Title
The purification and properties of cyclohexanone oxygenase from Nocardia globerula CL1 and Acinetobacter NCIB 9871.
  Journal
Eur J Biochem 63:175-92 (1976)
DOI:10.1111/j.1432-1033.1976.tb10220.x
Reference
2  [PMID:11551214]
  Authors
Sheng D, Ballou DP, Massey V.
  Title
Mechanistic studies of cyclohexanone monooxygenase: chemical properties of intermediates involved in catalysis.
  Journal
Biochemistry 40:11156-67 (2001)
DOI:10.1021/bi011153h
Reference
3
  Authors
Stewart, J.D.
  Title
Cyclohexanone monooxygenase: a useful reagent for asymmetric Baeyer-Villiger reactions.
  Journal
Curr Org Chem 2:195-216 (1998)
Reference
4
  Authors
Chen, G., Kayser, M.M., Milhovilovic, M.D., Mrstik, M.E., Martinez, C.A. and Stewart, J.D.
  Title
Asymmetric oxidations at sulfur catalyzed by engineered strains that overexpress cyclohexanone monooxygenase.
  Journal
New J Chem 23:827-832 (1999)
Reference
5
  Authors
Ottolina, G., Bianchi, S., Belloni, B., Carrea, G. and Danieli, B.
  Title
First asymmetric oxidation of tertiary amines by cyclohexanone monooxygenase.
  Journal
Tetrahedron Lett 40:8483-8486 (1999)
Reference
6
  Authors
Colonna, S., Gaggero, N., Carrea, G., Ottolina, G., Pasta, P. and Zambianchi, F.
  Title
First asymmetric epoxidation catalysed by cyclohexanone monooxygenase.
  Journal
Tetrahedron Lett 43:1797-1799 (2002)
Other DBs
ExplorEnz - The Enzyme Database: 1.14.13.22
IUBMB Enzyme Nomenclature: 1.14.13.22
ExPASy - ENZYME nomenclature database: 1.14.13.22
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.22
BRENDA, the Enzyme Database: 1.14.13.22
CAS: 52037-90-8

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