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Enzyme Kinetics

Previous kinetic studies demonstrated that NADH inhibits the AMP activation of glycogen phosphorylase b. Crystallographic binding studies at 3.5 Å resolution show that NADH binds to the same sites on the enzyme as AMP. This site is close to the subunit-subunit interface which is 12 Å from the catalytic site. The nucleoside inhibitor site is also 12 Å from the catalytic site. The two sites bind both NADH but nucleoside inhibitor binds the adenosine from NADH and AMP site binds only the nicotine head group. The conformations of the two sites are different but both bind NADH. When AMP binds to its effector site it allosterically activates glycogen phosphorylase b. .
             In this experiment the ability of 1-methylnicotinamide, a structural analogue of the nicotinamide in NAD+, to bind to the AMP site and inactivate glycogen phosphorylase b is tested. If 1-methylnicotinamide can bind to the AMP site it would be unlikely to activate glycogen phosphorylase b. With glycogen phosphorylase b locked in the inactive state more glucose would be stored as glycogen. In the case of diabetes this could prove beneficial to lock glycogen phosphorylase b in the inactive form. Diabetics lose the ability to control glucose levels in their blood specifically the ability to lower blood glucose levels. Since NADH is proven to bind to the AMP effector site this experiment will be testing the ability of the nicotinamide functional group of NADH to bind to the AMP site and inhibit glycogen phosphorylase b. Since the adenosine part of NADH also binds to glycogen phosphorylase b the test will determine if nicotinamide itself is enough to inhibit Glycogen phosphorylase b. .
             Glycogen phosphorylase b's ability to facilitate glucose-1-p hydrolyzation in the presence of 1-methylnicotinamide will be determined with increasing levels of substrate and AMP. If 1-methylnicotinamide inhibits the reaction in a glucose-1-p dependence test then it could be concluded that any inhibition would be the result of competition for the catalytic site and would not be evidence that 1-methylnicotinamide is an allosteric inhibitor.


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