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J Biol Chem, Vol. 274, Issue 26, 18252-18260, June 25, 1999

The NAD(P)H:Flavin Oxidoreductase from Escherichia coli
EVIDENCE FOR A NEW MODE OF BINDING FOR REDUCED PYRIDINE NUCLEOTIDES

Vincent Nivière, Franck Fieschi^¶, Jean-Luc Décout, and Marc Fontecave

From the  Laboratoire de Chimie et Biochimie des Centres Rédox Biologiques, DBMS-CEA/CNRS/Université J. Fourier, Batiment K, 17 Avenue des Martyrs, 38054 Grenoble, Cedex 9, France and ^¶ Institut de Biologie Structurale, CEA/CNRS/Université J. Fourier, 41 Avenue des Martyrs, 38027 Grenoble Cedex 1, France

The NAD(P)H:flavin oxidoreductase from Escherichia coli, named Fre, is a monomer of 26.2 kDa that catalyzes the reduction of free flavins using NADPH or NADH as electron donor. The enzyme does not contain any prosthetic group but accommodates both the reduced pyridine nucleotide and the flavin in a ternary complex prior to oxidoreduction. The specificity of the flavin reductase for the pyridine nucleotide was studied by steady-state kinetics using a variety of NADP analogs. Both the nicotinamide ring and the adenosine part of the substrate molecule have been found to be important for binding to the polypeptide chain. However, in the case of NADPH, the 2'-phosphate group destabilized almost completely the interaction with the adenosine moiety. Moreover, NADPH and NMNH are very good substrates for the flavin reductase, and we have shown that both these molecules bind to the enzyme almost exclusively by the nicotinamide ring. This provides evidence that the flavin reductase exhibits a unique mode for recognition of the reduced pyridine nucleotide. In addition, we have shown that the flavin reductase selectively transfers the pro-R hydrogen from the C-4 position of the nicotinamide ring and is therefore classified as an A-side-specific enzyme.

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