Literature summary for 1.14.14.155 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 .

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Cloned(Commentary)

Cloned (Comment)	Organism
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)

Crystallization (Comment)	Organism
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
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

Crystallization (Comment)

Organism

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

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

Organism	UniProt	Comment	Textmining
Pseudomonas putida	D7UER1	-	-
Pseudomonas putida NCIMB 10007	D7UER1	-	-

Purification (Commentary)

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

Source Tissue

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Cofactor

Cofactor	Comment	Organism	Structure
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
FMN	FMN-dependent enzyme	Pseudomonas putida

General Information

General Information	Comment	Organism
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
metabolism	the enzyme is involved in the camphor-degradation pathway, overview	Pseudomonas putida
additional information	the enzyme is a type II Baeyer-Villiger monooxygenase, enzyme structure modeling, active site structure, overview	Pseudomonas putida