Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity

The members of the mechanistically diverse enolase superfamily catalyze different overall reactions. Each shares a partial reaction in which an active site base abstracts the α-proton of the carboxylate substrate to generate an enolate anion intermediate that is stabilized by coordination to the essential Mg2+ ion; the intermediates are then directed to different products in the different active sites. In this minireview, our current understanding of structure/function relationships in the divergent members of the superfamily is reviewed, and the use of this knowledge for our future studies is proposed.