S135: Functional annotation for members of the amidohydrolase superfamily

A critical assessment of the functional annotations for the twelve million genes that have been sequenced thus far suggests that more than one third of the encoded proteins have an uncertain, unknown, or incorrect functional assignment.  This observation suggests that a significant fraction of the metabolic diversity in many bacterial organisms remains to be properly characterized and that an assignment of function based on amino acid sequence alone is a difficult endeavour.  Our approach to this problem has been to concentrate on the large number of enzymes of unknown function within the amidohydrolase superfamily (AHS) through a collaborative integration of three-dimensional structure determination, computational docking, genomic context, and library screening.  These methods have been employed in the discovery of new enzymes that catalyze the deamination of 8-oxoguanine, isoguanine, N6-methyl adenine, 5’-deoxy-adenosine, zeatin, thiomethyl-adenosine, and isoxanthopterin.