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

John A. Gerlt, Patricia C. Babbitt, Ivan Rayment

Research output: Contribution to journalArticlepeer-review

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 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.

Original languageEnglish (US)
Pages (from-to)59-70
Number of pages12
JournalArchives of Biochemistry and Biophysics
Volume433
Issue number1
DOIs
StatePublished - Jan 1 2005

Keywords

  • Divergent evolution
  • Enolase superfamily

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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