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
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)] [1,2]. The product spontaneously converts to [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate.
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.
Isupov MN, Schroder E, Gibson RP, Beecher J, Donadio G, Saneei V, Dcunha SA, McGhie EJ, Sayer C, Davenport CF, Lau PC, Hasegawa Y, Iwaki H, Kadow M, Balke K, Bornscheuer UT, Bourenkov G, Littlechild JA
Title
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.
