*OBJ - Enzyme Regulation Flashcards
Define allosteric regulation of enzymes, and explain the T and R states of an allosteric enzyme
a
Distinguish between homotropic and heterotropic allosteric regulation
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Describe cooperativity in substrate binding to multisubunit protein with reference to hemoglobin
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Distinguish the action of allosteric activators and inhibitors by inspection of a V0/ Vmax versus [S] plot
a
Describe the role of conformational changes in functional regulation of metabolic enzymes with special reference to covalent modifications (such as phosphorylation and proteolytic cleavage) and protein-protein interaction (as in case of calmodulin)
a
Distinguish the basic structural plan of myoglobin from that of hemoglobin, and explain how their respective structures correlate to their specific physiological functions.
a
Interpret the saturation curve of oxygen binding by hemoglobin and myoglobin at increasing partial pressure of O2, and explain the physiological significance of cooperativity in O2 binding to hemoglobin
a
Describe the role of heme in oxygen binding by hemoglobin and illustrate why free heme cannot substitute for hemoglobin in transporting oxygen
a
Explain the molecular basis of sickle cell anemia, and the mechanistic basis of the existing modalities of treatment
a
Explain why enzyme catalyzed reactions are pH- and temperature-sensitive
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