Stopped-flow studies of the reaction of D-tartronate semialdehyde-2-phosphate with human neuronal enolase and yeast enolase 1.
We determined the kinetics of the reaction of human neuronal enolase and yeast enolase 1 with the slowly-reacting chromophoric substrate D-tartronate semialdehyde phosphate (TSP), each in tris (tris (hydroxymethyl) aminomethane) and another buffer at several Mg2+ concentrations, 50 or 100 microM, 1 mM and 30 mM. All data were biphasic, and could be satisfactorily fit, assuming either two successive first-order reactions or two independent first-order reactions. Higher Mg2+ concentrations reduce the relative magnitude of the slower reaction. The results are interpreted in terms of a catalytically significant interaction between the two subunits of these enzymes.
Brewer
John M
JM
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, United States. brewer@bmb.uga.edu
McKinnon
Jared S
JS
Phillips
Robert S
RS
D006801:Humans; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D010751:Phosphopyruvate Hydratase / Q000378:metabolism*; D011485:Protein Binding; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D013379:Substrate Specificity; D013646:Tartronates / Q000378:metabolism*
D029701:Saccharomyces cerevisiae Proteins; D013646:Tartronates; C059689:tartronate semialdehyde phosphate; C521376:ENO1 protein, S cerevisiae; D010751:Phosphopyruvate Hydratase; D008274:Magnesium