Exploring nicotinamide cofactor promiscuity in NAD(P)H-dependent flavin containing monooxygenases (FMOs) using natural variation within the phosphate binding loop. Structure and activity of FMOs from <i>Cellvibrio</i> sp. BR and <i>Pseudomonas stutzeri</i> NF13.

The structure of SMFMO was determined [10] , and analysis of the nicotinamide cofactor binding loop revealed differences between NADPH-dependent mFMO [12] , [13] , [14] and SMFMO that might be significant in the recognition of the NADPH 2′ ribose phosphate that distinguishes NADPH and NADH [10] .

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