Exam 21: Glycogen Metabolism

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Why is the T state of glycogen phosphorylase less active?

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B

Why is the formation of glucose-1-phosphate energetically favorable even though the ΔG°′ is very small?

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It is favored because the ratio of [Pi] to glucose-1-phosphate is greater than 100:1.

What physiological conditions render phosphorylase b less active?

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C

Compare the evolutionary history of the catalytic and regulatory features of glycogen phosphorylase.

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Give the reaction catalyzed by UDP-glucose pyrophosphorylase.

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What protein is the δ\delta subunit of phosphorylase kinase?

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What enzyme(s) is (are) required to cleave α\alpha -1,6-glycosidic branches in glycogen?

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What are the three steps in glycogen degradation?

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Which of the following occur after a carbohydrate-rich meal?

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Insulin stimulates glycogen synthase by inactivating ________________________.

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What is the normal glucose concentration in blood?

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In skeletal muscle, the binding of ___________ converts phosphorylase b into the active form.

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Critical hormones that signal for glycogen breakdown are

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What hormone signifies the starved state?

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Glycogen synthase catalyzes the transfer of a glucose residue from UDP-glucose to one of the _____________ ends of glycogen.

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What type of glycosidic bond is found at the branch points of glycogen?

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Which of the following serves as the glucose "sensor" enzyme in liver cells?

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Thermodynamically, the reaction glucose-1-phosphate + UTP Thermodynamically, the reaction glucose-1-phosphate + UTP   UDP-glucose + PP<sub>i</sub> is readily reversible. Explain why the formation of UDP-glucose from glucose-1-phosphate and UTP is essentially irreversible. UDP-glucose + PPi is readily reversible. Explain why the formation of UDP-glucose from glucose-1-phosphate and UTP is essentially irreversible.

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Phosphorylase kinase becomes fully active by being phosphorylated and binding ___________.

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How is phosphorylase b converted into phosphorylase a?

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