(Solved): what is b? In Class Exercise: Enzyme Regulation Glutamate dehydrogenase (GDH) is a homohexamer that ...

In Class Exercise: Enzyme Regulation Glutamate dehydrogenase (GDH) is a homohexamer that catalyzes the oxidative deamination of glutamate to generate $$?$$-ketoglutarate. As might be expected for multimeric protein at a key metabolic regulatory point, it is allosterically regulated; GTP is an allosteric inhibitor whereas ADP is an allosteric activator. a) Sketch the relationship between catalytic rate and glutamate concentration for GDH alone, GDH+GTP, \& GDH+ADP. Be certain to label each axis and the three curves. b) Surprisingly, ADP does not activate the enzyme by increasing its affinity for glutamate. Instead, it appears to decrease the enzyme's affinity for its products. How could this lead to a faster catalytic rate? b)