Flavin monooxygenases (FMO)

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Not all P450-dependent reactions are monooxygenations, and not all monooxygenases are P450 enzymes (Mansuy and Renaud, 1995).

In particular, flavin monooxygenases or FMOs are NADPH-dependent enzymes that catalyze some reactions similar or identical to those catalyzed by P450 enzymes.

In mammalian species, FMOs are microsomal enzymes best known for their N- and S-oxidation activities (Ziegler, 2002).

Little is known about FMOs in insects. In the cinnabar moth Tyria jacobaea, a soluble FMO specifically N-oxidizes pyrolizidine alkaloids such as senecionine, seneciphylline, monocrotaline and axillarine (Lindigkeit et al., 1997, Naumann et al., 2002). Only two FMO genes have been recognized in the Drosophila genome, and recombinant DmFMO-2 produced in E. coli is active in methimazole sulfoxidation assay (Scharf et al., 2004). The Bombyx mori genome has three FMO genes (Sehlmeyer et al., 2010).

Spodoptera exigua Tian et al., 2018

A flavin-dependent monooxgenase confers resistance to chlorantraniliprole in the diamondback moth, Plutella xylostella (Mallott et al., 2019)