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.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Amino Acid Sequence
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Amino Acid Substitution
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Binding Sites / genetics
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Carboxylic Acids / chemistry
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Catalysis
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Escherichia coli / enzymology
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Escherichia coli / genetics
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Evolution, Molecular*
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Forecasting
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Genome, Bacterial
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Ligands
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Magnesium / chemistry
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Models, Chemical
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Models, Molecular
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Molecular Structure
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Mutagenesis, Site-Directed
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Phosphopyruvate Hydratase / chemistry*
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Phosphopyruvate Hydratase / genetics*
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Phosphopyruvate Hydratase / metabolism
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Protein Structure, Secondary
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Protons
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Sensitivity and Specificity
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Structure-Activity Relationship
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Substrate Specificity
Substances
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Carboxylic Acids
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Ligands
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Protons
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Phosphopyruvate Hydratase
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Magnesium