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 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.
Gerlt
John A
JA
Departments of Biochemistry and Chemistry, University of Illinois, Urbana, IL 61801, USA. j-gerlt@uiuc.edu
Babbitt
Patricia C
PC
Rayment
Ivan
I
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001665:Binding Sites / Q000235:genetics; D002264:Carboxylic Acids / Q000737:chemistry; D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D019143:Evolution, Molecular; D005544:Forecasting; D016680:Genome, Bacterial; D008024:Ligands; D008274:Magnesium / Q000737:chemistry; D008956:Models, Chemical; D008958:Models, Molecular; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D010751:Phosphopyruvate Hydratase / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D017433:Protein Structure, Secondary; D011522:Protons; D012680:Sensitivity and Specificity; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D002264:Carboxylic Acids; D008024:Ligands; D011522:Protons; D010751:Phosphopyruvate Hydratase; D008274:Magnesium