KEGG   ENZYME: 1.14.13.162Help
Entry
EC 1.14.13.162              Enzyme                                 

Name
2,5-diketocamphane 1,2-monooxygenase;
2,5-diketocamphane lactonizing enzyme;
ketolactonase I (ambiguous);
2,5-diketocamphane 1,2-monooxygenase oxygenating component;
2,5-DKCMO;
camP (gene name);
camphor 1,2-monooxygenase;
camphor ketolactonase I
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
(+)-bornane-2,5-dione,NADH:oxygen oxidoreductase (1,2-lactonizing)
Reaction(IUBMB)
(+)-bornane-2,5-dione + O2 + NADH + H+ = (+)-5-oxo-1,2-campholide + NAD+ + H2O [RN:R04102]
Reaction(KEGG)
Substrate
(+)-bornane-2,5-dione [CPD:C03037];
O2 [CPD:C00007];
NADH [CPD:C00004];
H+ [CPD:C00080]
Product
(+)-5-oxo-1,2-campholide [CPD:C02952];
NAD+ [CPD:C00003];
H2O [CPD:C00001]
Comment
A flavoprotein (FMN) which requires Fe2+. A Baeyer-Villiger monooxygenase isolated from camphor-grown strains of Pseudomonas putida and encoded on the cam plasmid. Involved in the degradation of (+)-camphor. Requires a dedicated NADH-FMN reductase [cf. EC 1.5.1.42, FMN reductase (NADH)] [1-3]. Can accept several bicyclic ketones including (+)- and (-)-camphor [6] and adamantanone [4].
The product spontaneously converts to [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate.
History
EC 1.14.13.162 created 1972 as EC 1.14.15.2, transferred 2012 to EC 1.14.13.162
Reference
1  [PMID:14253460]
  Authors
CONRAD HE, DUBUS R, NAMTVEDT MJ, GUNSALUS IC.
  Title
MIXED FUNCTION OXIDATION. II. SEPARATION AND PROPERTIES OF THE ENZYMES CATALYZING CAMPHOR LACTONIZATION.
  Journal
J. Biol. Chem. 240 (1965) 495-503.
Reference
2  [PMID:4310834]
  Authors
Yu CA, Gunsalus IC.
  Title
Monoxygenases. VII. Camphor ketolactonase I and the role of three protein components.
  Journal
J. Biol. Chem. 244 (1969) 6149-52.
Reference
3  [PMID:3944058]
  Authors
Taylor DG, Trudgill PW
  Title
Camphor revisited: studies of 2,5-diketocamphane 1,2-monooxygenase from Pseudomonas putida ATCC 17453.
  Journal
J. Bacteriol. 165 (1986) 489-97.
Reference
4  [PMID:1510672]
  Authors
Selifonov SA
  Title
Microbial oxidation of adamantanone by Pseudomonas putida carrying the camphor catabolic plasmid.
  Journal
Biochem. Biophys. Res. Commun. 186 (1992) 1429-36.
Reference
5  [PMID:8515237]
  Authors
Jones KH, Smith RT, Trudgill PW
  Title
Diketocamphane enantiomer-specific 'Baeyer-Villiger' monooxygenases from camphor-grown Pseudomonas putida ATCC 17453.
  Journal
J. Gen. Microbiol. 139 (1993) 797-805.
Reference
6  [PMID:21906366]
  Authors
Kadow M, Sass S, Schmidt M, Bornscheuer UT
  Title
Recombinant expression and purification of the 2,5-diketocamphane 1,2-monooxygenase from the camphor metabolizing Pseudomonas putida strain NCIMB 10007.
  Journal
AMB. Express. 1 (2011) 13.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 

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