The removal of the N-terminal methionine from proteins and peptides is dependent upon a
novel class of proteases typified by the dinuclear metalloenzyme methionine
aminopeptidase from Escherichia coli (eMetAP). Substantial progress has recently been
made in determining the structures of several members of this family. The identification of
human MetAP as the target of putative anti-cancer drugs reiterates the importance of this
family of enzymes. Determination of the modes of binding to E. coli MetAP of a substrate-like …