Baeyer-Villiger monooxygenase BVMO

Flavin-containing Baeyer-Villiger monooxygenases (BVMOs) represent nature s equivalent of conventional peracids or de novo designed metal complexes... 

Among the most popular oxidative biotransformations, Baeyer-Villiger monooxygenases (BVMOs) belong to the main fields of research. Nowadays, manifold enzymes catalyzing the Baeyer-Villiger oxidation are expressed in common recombinant organisms, such as E. coli or S. cerevisiae. The mechanism of the enzymatic... 

Baeyer-VilUger Reactions. Baeyer-Villiger oxidation is the oxidative cleavage of a carbon-carbon bond adjacent to a carbonyl, and converts ketones to esters and cyclic ketones to lactones (Figure 1.46). The enzymes that catalyze these reactions are Baeyer-Villiger monooxygenases (BVMOs), which are NADPH-dependent flavo-... 

The first indication of the existence of so-called Baeyer-Villiger monooxygenases (BVMOs) was reported in the late 1940s [56]. It was observed that certain fungi were able to oxidize steroids via a BV reaction [56], but two decades elapsed before the first BVMOs were isolated and characterized [57, 58]. All characterized BVMOs contain a flavin cofactor that is vital for the catalytic activity of the enzyme, Furthermore, NADH or NADPH cofactors are needed as electron donors. Careful inspection of all available biochemical data on BVMOs has revealed that at least two discrete classes of BVMOs exist, types I and II [59]. 

Scheme 10.4 Comparison of the conventional regeneration of a Baeyer-Villiger monooxygenase (BVMO, e.g., PAMO) for catalysis through enzymatic regeneration of NADPH (A) and the novel simplified light-driven pathway using a flavin (B).

Scheme 2.2 NADPH-dependent Baeyer-Villiger monooxygenases (BVMO) fused to a phosphite dehydrogenase (PTDH) for self-sufficient coenzyme regeneration.

Scheme 3.2 Elegant combination of an alcohol dehydrogenase (ADH) and a Baeyer-Villiger monooxygenase (BVMO) for a redox-balanced biocatalytic system.

Baeyer-Villiger monooxygenases (BVMOs) are flavin-containing (either flavine adenine dinucleotide [FAD] or flavine mononucleotide [FMN]), NAD(P)H-dependent enzymes only found in bacteria and fungi. They catalyze... 

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