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Investigating The Allosteric Behavior Of Malate Dehydrogenase From Escherichia Coli, Eman M. Ghanem
Investigating The Allosteric Behavior Of Malate Dehydrogenase From Escherichia Coli, Eman M. Ghanem
Masters Theses
Regulatory mechanisms of malate dehydrogenase from E.coli (eMDH) involving NADH as an allosteric effector were investigated. The reaction was studied in both directions: malate oxidation and oxaloacetate reduction. When malate was the variable substrate, a plot of rate against substrate concentration was sigmoidal in the presence of 0.065 mM NADH, which indicates the presence of an allosteric site for NADH on the enzyme. Binding of NADH at the allosteric site causes conformational changes in the active site and, thereby, changes the catalytic activity of the enzyme. An increase in Km value, from 1.3 to 3.9 mM malate was observed, …