KEGG   ENZYME: 1.14.14.108
Entry
EC 1.14.14.108              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 reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
(+)-bornane-2,5-dione,FMNH2:oxygen oxidoreductase (1,2-lactonizing)
Reaction(IUBMB)
(+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O [RN:R04102]
Reaction(KEGG)
R04102
Substrate
(+)-bornane-2,5-dione [CPD:C03037];
FMNH2 [CPD:C01847];
O2 [CPD:C00007]
Product
(+)-5-oxo-1,2-campholide [CPD:C02952];
FMN [CPD:C00061];
H2O [CPD:C00001]
Comment
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 1.14.14.108 created 1972 as EC 1.14.15.2, transferred 2012 to EC 1.14.13.162, transferred 2018 to EC 1.14.14.108
Orthology
K21731  2,5-diketocamphane 1,2-monooxygenase
Genes
PSET: THL1_4143
NAR: Saro_1468
SGI: SGRAN_3282(camP2)
RHA: RHA1_ro05405
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 240:495-503 (1965)
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 244:6149-52 (1969)
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 165:489-97 (1986)
DOI:10.1128/JB.165.2.489-497.1986
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 186:1429-36 (1992)
DOI:10.1016/S0006-291X(05)81566-9
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 139:797-805 (1993)
DOI:10.1099/00221287-139-4-797
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 1:13 (2011)
DOI:10.1186/2191-0855-1-13
  Sequence
Reference
7  [PMID:23524667]
  Authors
Iwaki H, Grosse S, Bergeron H, Leisch H, Morley K, Hasegawa Y, Lau PC
  Title
Camphor pathway redux: functional recombinant expression of 2,5- and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions.
  Journal
Appl Environ Microbiol 79:3282-93 (2013)
DOI:10.1128/AEM.03958-12
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.108
IUBMB Enzyme Nomenclature: 1.14.14.108
ExPASy - ENZYME nomenclature database: 1.14.14.108
BRENDA, the Enzyme Database: 1.14.14.108

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