Type II Baeyer Villiger Monooxygenases

Type II BVMOs [8] are typically composed of two different subunits in which a reductase subunit utilizes NADH to reduce FMN while the other subunit utilizes this reduced flavin to perform a Baeyer-Villiger reaction. While type I BVMO genes have been frequently reported, cloning of a type II BVMO gene has not been described in the literature. For a long time only several sequenced N-termini were known [8] which prohibited classification of these monooxygenases in the flavoprotein suprafamily. Recently, however, a sequence of a "limone monooxy-

genase" (GI12054950) has been deposited in the sequence database which shares homology with the known type II BVMO N-termini. This bacterial monooxygen-ase gene, which is part of a gene cluster involved in limonene degradation, probably represents the oxygenase component of a type II BVMO that is involved in the conversion of 1-hydroxy-2-oxolimonene or a related terpene [22].

Based on the inspection of the published N-terminal sequences and database searches using the fully sequenced putative type II BVMO, it can be concluded that type II BVMOs are rather rare enzymes. Only 10 sequence homologs can be identified, which is in sharp contrast with more than 400 type I BVMO genes that can be found by in silico inspection of sequenced genomes. In addition to the corresponding oxygenase subunit genes, a reductase component is also necessary to obtain a functional type II BVMO system. This clearly complicates the cloning and expression of type II BVMOs and might partly explain the lack of type II BVMOs in a recombinant form.

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