In recent years, two-component flavin-dependent monooxygenases have emerged as an important group of enzymes involved in various metabolic and biosynthetic processes in microorganisms. Efforts to elucidate the details governing the catalytic mechanisms of these systems continue to be an area of active investigation. The two-component alkanesulfonate monooxygenase reaction found in various microorganisms is being studied as a model for this group. The system is composed of a NAD(P)H-dependent FMN reductase and a FMNH2-dependent monooxygenase that alleviate periods of sulfur limitation by converting environmental alkanesulfonates into aldehydes and sulfites. An active site base has been proposed to play a direct role in catalysis at specific steps in the reaction pathway. Sequence and structural analyses were used to identify several putative amino acids in the monoooxygenase. Variants of these residues wereconstructed and evaluated to assess the role of each in catalysis. These results illuminate critical catalytic features of this complex system.

Elucidating the catalytic mechanism of a two-component flavin-dependent monooxygenase

239th National Meeting (2010)

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