Monday, 23 May 2005

This presentation is part of: Biological Chemistry Posters

FAD Synthetase is slightly promiscuous

David M. Yearsley1, William S. McIntire2, and Robert J. Stanley1. (1) Temple University, Philadelphia, PA, (2) Department of Veterans Affairs Medical Center, San Francisco, CA

FAD Synthetase (FS) is a bifunctional enzyme in that it catalyzed both the phosphorylation of riboflavin to produce flavin mononucleotide (FMN) and the adenylylation of FMN to produce flavin adenine dinucleotide (FAD). In the latter reaction the adenosine moiety, along with one phosphate group, is taken from adenosine triphosphate (ATP) in a divalent cation dependent mechanism. It has been shown that FS does not except any other nucleotides - such as TTP, CTP, GTP or UTP as substrates. However, no studies have been done to determine if the nucleotide binding site of FS will accept ATP analogs with an adenine moiety modification. Our early results suggest that FS may be promiscuous enough to accept 2-Aminopurine-2'-deoxyriboside-5'-triphosphate as a substrate instead of ATP.

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