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 language | English (US) |
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Pages (from-to) | 59-70 |
Number of pages | 12 |
Journal | Archives of Biochemistry and Biophysics |
Volume | 433 |
Issue number | 1 |
DOIs | |
State | Published - Jan 1 2005 |
Keywords
- Divergent evolution
- Enolase superfamily
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology