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    Arch Biochem Biophys. 2005 Jan 1;433(1):59-70.

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

    Gerlt JA, Babbitt PC, Rayment I.

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    Departments of Biochemistry and Chemistry, University of Illinois, Urbana, IL 61801, USA. j-gerlt@uiuc.edu

    Abstract

    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 alpha-proton of the carboxylate substrate to generate an enolate anion intermediate that is stabilized by coordination to the essential Mg(2+) 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.

    PMID:
    15581566
    [PubMed - indexed for MEDLINE]

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