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Literature summary extracted from

  • Isupov, M.N.; Schroeder, E.; Gibson, R.P.; Beecher, J.; Donadio, G.; Saneei, V.; Dcunha, S.A.; McGhie, E.J.; Sayer, C.; Davenport, C.F.; Lau, P.C.; Hasegawa, Y.; Iwaki, H.; Kadow, M.; Balke, K.; Bornscheuer, U.T.; Bourenkov, G.; Littlechild, J.A.
    The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida the first crystal structure of a type II Baeyer-Villiger monooxygenase (2015), Acta Crystallogr. Sect. D, 71, 2344-2353 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.155 the enzyme is encoded on the large CAM plasmid of Pseudomonas putida, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) Pseudomonas putida

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.14.155 purified recombinant N-terminally His6-tagged enzyme, by Microbatch crystallization, mixing of 7 mg/ml protein in 20 mM FMN, 5 mM NADH and 5 mM (-)-camphor in a 1:1 ration, purified native enzyme, by vapour-diffusion technique, 10 mg/ml protein solution are mixed in equal volumes with 50 mM PIPES pH 6.5, 50% ammonium sulfate, room temperature, best from 100 mM HEPES pH 7.0, 20% PEG 3350 in the presence of 20 mM FMN, 5 mM NADH and 5 mM (-)-camphor, at 18°C, X-ray diffraction structure determination and analysis at 1.9-2.7 A resolution, the enzyme's crystal structure is solved by a combination of multiple anomalous dispersion from a bromine crystal soak and molecular replacement using a bacterial luciferase model Pseudomonas putida
1.14.14.155 vapour-diffusion technique, three-dimensional structures of the native enzyme and the FMN complex of the overexpressed form of the oxygenating component of the type II Baeyer-Villiger 3,6-diketocamphane monooxygenase have been determined to 1.9 A resolution Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.155 Pseudomonas putida D7UER1
-
-
1.14.14.155 Pseudomonas putida NCIMB 10007 D7UER1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.14.155
-
 Pseudomonas putida
1.14.14.155 recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Pseudomonas putida

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.14.155 culture condition:camphor-grown cell
-
 Pseudomonas putida
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.155 additional information mechanism of enantioselectivity for the hydroxyl-peroxide rearrangement taking place in the BVMO active site Pseudomonas putida ?
-
 ?
1.14.14.155 additional information mechanism of enantioselectivity for the hydroxyl-peroxide rearrangement taking place in the BVMO active site Pseudomonas putida NCIMB 10007 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.14.155 dimer
-
 Pseudomonas putida
1.14.14.155 dimer three-dimensional structure analysis, overview Pseudomonas putida

Synonyms

EC Number Synonyms Comment Organism
1.14.14.155 3,6-diketocamphane monooxygenase
-
 Pseudomonas putida
1.14.14.155 3,6-DKMO
-
 Pseudomonas putida
1.14.14.155 type II Baeyer-Villiger 3,6-diketocamphane monooxygenase
-
 Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.155 FMN dependent on, FMN cofactor modelling. Type II Baeyer-Villiger monooxygenases are attributed to the R group in relation to the re-face attachment of the hydroperoxide to the flavin coenzyme. The FMN cofactor binds in the cleft formed at the C-terminal side of the TIM barrel, with the phosphate group involved in hydrogen bonding at the edge of the cleft and the isoalloxazine ring located deep inside of the cleft Pseudomonas putida
1.14.14.155 FMN FMN-dependent enzyme Pseudomonas putida

General Information

EC Number General Information Comment Organism
1.14.14.155 evolution the orientation of the isoalloxazine ring of the FMN cofactor in the active site of the TIM-barrel fold enzyme differs significantly from that previously observed in enzymes of the bacterial luciferase-like superfamily. The Ala77 residue is in a cis conformation and forms a beta-bulge at the C-terminus of beta-strand 3, which is a feature observed in many proteins of this superfamily. Both the 2,5-DKMO and 3,6-DKMO oxygenating components have sequence similarity to bacterial luciferases and bear little similarity to type I Baeyer-Villiger monooxygenase, type I BVMOs Pseudomonas putida
1.14.14.155 metabolism the enzyme is involved in the camphor-degradation pathway, overview Pseudomonas putida
1.14.14.155 additional information the enzyme is a type II Baeyer-Villiger monooxygenase, enzyme structure modeling, active site structure, overview Pseudomonas putida