Exam 24: Glycogen Degradation

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Why does the liver possess a specific enzyme that can cleave glucose 6-phosphate to form glucose and orthophosphate?

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The liver controls the blood glucose concentration. Thus, it must be able to remove the phosphate so the glucose can be released from liver cells.

Muscle phosphorylase is mostly inactive when:

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D

Which molecule(s) must be excluded from the active site of glycogen phosphorylase?

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C

The transferase enzyme shifts a block of ______________ glycosyl units.

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In skeletal muscle, the binding of ______________ stabilizes phosphorylation b into the active form.

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Phosphorylase a and b both exist in equilibrium between R and T states. Which are the most active and least active combinations?

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Which GTP binding protein is activated by epinephrine binding to the adrenergic 7TM receptor?

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Why must glycogen control be manifested differently in muscle and liver?

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How does epinephrine stimulate glycogen breakdown in muscle? (Describe the series of events.)

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What are some of the advantages of having glycogen as a readily available glucose source?

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The key enzyme in glycogen degradation is:

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Conversion of glucose 1-phosphate to glucose 6-phosphate is carried out by the enzyme:

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Phosphoglucomutase requires the intermediate ______________ for the interconversion of glucose 1-phosphate and glucose 6-phosphate.

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What is required to remove branches in glycogen?

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How is phosphorylase b converted into phosphorylase a?

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What are the three steps in glycogen degradation?

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In the liver, glycogen synthesis and degradation are regulated to maintain levels of ______________ in the blood.

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Two critical hormones that signal for glycogen breakdown are:

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____________ is the end of glycogen where interconversion between the open and closed conformation of the anomeric carbon is possible

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The ____________ enzyme serves as the glucose "sensor" enzyme in liver cells.

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