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The NAD(P)H:flavin oxidoreductase from Escherichia coli, named Fre, is amonomer of 26.2 kDa that catalyzes the reduction of free flavins using NADPH orNADH as electron donor. The enzyme does not contain any prosthetic group butaccommodates both the reduced pyridine nucleotide and the flavin in a ternarycomplex prior to oxidoreduction. The specificity of the flavin reductase forthe pyridine nucleotide was studied by steady-state kinetics using a variety ofNADP analogs. Both the nicotinamide ring and the adenosine part of thesubstrate molecule have been found to be important for binding to thepolypeptide chain. However, in the case of NADPH, the 2'-phosphate groupdestabilized almost completely the interaction with the adenosine moiety.Moreover, NADPH and NMNH are very good substrates for the flavin reductase, andwe have shown that both these molecules bind to the enzyme almost exclusivelyby the nicotinamide ring. This provides evidence that the flavin reductaseexhibits a unique mode for recognition of the reduced pyridine nucleotide. Inaddition, we have shown that the flavin reductase selectively transfers thepro-R hydrogen from the C-4 position of the nicotinamide ring and is thereforeclassified as an A-side-specific enzyme.

The NAD(P)H:flavin oxidoreductase from Escherichia coli. Evidence for a new mode of binding for reduced pyridine nucleotides