2,5-diketocamphane 1,2-monooxygenase

2,5-diketocamphane 1,2-monooxygenase (EC 1.14.14.108, 2,5-diketocamphane lactonizing enzyme, ketolactonase I, 2,5-diketocamphane 1,2-monooxygenase oxygenating component, 2,5-DKCMO, camphor 1,2-monooxygenase, camphor ketolactonase I) is an enzyme with systematic name (+)-bornane-2,5-dione,NADH:oxygen oxidoreductase (1,2-lactonizing). This enzyme catalyses the following chemical reaction

(+)-bornane-2,5-dione + O₂ + NADH + H

\rightleftharpoons

(+)-5-oxo-1,2-campholide + NAD + H₂O

2,5-diketocamphane 1,2-monooxygenase is a flavoprotein (FMN) which requires Fe.

References

Conrad HE, Dubus R, Namtvedt MJ, Gunsalus IC (January 1965). "Mixed function oxidation. II. Separation and properties of the enzymes catalyzing camphor lactonizaton". The Journal of Biological Chemistry. 240: 495–503. doi:10.1016/S0021-9258(18)97679-9. PMID 14253460.
Yu CA, Gunsalus IC (November 1969). "Monoxygenases. VII. Camphor ketolactonase I and the role of three protein components". The Journal of Biological Chemistry. 244 (22): 6149–52. doi:10.1016/S0021-9258(18)63518-5. PMID 4310834.
Taylor DG, Trudgill PW (February 1986). "Camphor revisited: studies of 2,5-diketocamphane 1,2-monooxygenase from Pseudomonas putida ATCC 17453". Journal of Bacteriology. 165 (2): 489–97. doi:10.1128/jb.165.2.489-497.1986. PMC 214445. PMID 3944058.
Selifonov SA (August 1992). "Microbial oxidation of adamantanone by Pseudomonas putida carrying the camphor catabolic plasmid". Biochemical and Biophysical Research Communications. 186 (3): 1429–36. doi:10.1016/s0006-291x(05)81566-9. PMID 1510672.
Jones KH, Smith RT, Trudgill PW (April 1993). "Diketocamphane enantiomer-specific 'Baeyer-Villiger' monooxygenases from camphor-grown Pseudomonas putida ATCC 17453". Journal of General Microbiology. 139 (4): 797–805. doi:10.1099/00221287-139-4-797. PMID 8515237.
Kadow M, Saß S, Schmidt M, Bornscheuer UT (June 2011). "Recombinant expression and purification of the 2,5-diketocamphane 1,2-monooxygenase from the camphor metabolizing Pseudomonas putida strain NCIMB 10007". AMB Express. 1 (1): 13. doi:10.1186/2191-0855-1-13. PMC 3222318. PMID 21906366.

External links

2,5-diketocamphane+1,2-monooxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate	Prolyl hydroxylase HIF prolyl-hydroxylase EGLN1 EGLN2 EGLN3 P4HTM Lysyl hydroxylase AlkB ALKBH1 FTO
1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 14α-demethylase 24-hydroxycholesterol 7α-hydroxylase
1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1
1.14.15: reduced iron–sulfur protein	11B1 11B2 11A1
1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase
1.14.17: reduced ascorbate	Dopamine beta-hydroxylase
1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1
1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2 Ecdysone 20-monooxygenase Deoxyhypusine monooxygenase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 1.14.13