Structural and mechanistic studies of enolase.
The high-resolution structure of yeast enolase cocrystallized with its equilibrium mixture of substrate and product reveals the stereochemistry of substrate/product binding and therefore the groups responsible for acid/base catalysis and stabilization of the enolate intermediate. Expression and characterization of site-specific mutant forms of the enzyme have confirmed the roles of amino acid side chains in the catalysis of the first and second steps of the reaction. Coordination of both required magnesium ions to the carboxylate of the substrate/product indicates a role for these cations in stabilization of the intermediate.
Reed
G H
GH
Institute for Enzyme Research, Graduate School, University of Wisconsin-Madison 53705, USA.
Poyner
R R
RR
Larsen
T M
TM
Wedekind
J E
JE
Rayment
I
I
D001665:Binding Sites / Q000502:physiology; D055598:Chemical Phenomena; D002621:Chemistry; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005988:Glyceric Acids / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D010751:Phosphopyruvate Hydratase / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation
D004791:Enzyme Inhibitors; D005988:Glyceric Acids; C008885:2-phosphoglycerate; D010751:Phosphopyruvate Hydratase