Glycogen metabolism in muscle and liver Flashcards

1
Q

What are the linkages in glycogen

A

alpha-1,4 and alpha-1,6.

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2
Q

Outline the steps of glycogen breakdown in the muscle

A

Glycogen—->G1P–r–>G6P which can enters glycolysis and becomes pyruvate. G1P—>G6P is reversible and catalysed by phosphoglucomutase.

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3
Q

Outline the steps of glycogen breakdown in the liver

A

Glycogen—–>G1P–r–>G6P——>glucose

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4
Q

What enzyme catalysis G6P to glucose in the liver

A

glucose-6-phosphatase

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5
Q

What enzyme breaks the alpha 1-4 linkages in glycogen

A

Glycogen phosphorylase to form G1P And a the glycogen molecule.

It can only break bonds up to 4 glucose residues from a branching point.

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6
Q

outline the debranching of glycogen

A

Transferase activity removes 3 residues from the branch and transfers them to the end of another chain in an alpha 1,4 linkage. The free glucose left at the end of the chain is removed via alpha 1,6-glucosidase

the chain can be broken down by phosphorylase until it meets the next branch point.

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7
Q

Glycogen synthesis

A

Glucose——->G6P
G6P—R—>G1P (phosphoglucomutase)
G1P + UTP—–>UDP-glucose
UDP-glucose +glycogen—–> Glycogen(n+1) +UDP (glycogen synthase)

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8
Q

describe the action of branching enzyme

A

transfers a block of 7 residues from a growing chain to create a new branch with an alpha-1,6 linkage

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9
Q

Why is glycogen a good energy store

A

It can be mobilised very rapidly
enzymes phosphorylase and glycogen synthase are very sensitive to regulation by hormones, stress and muscle contraction
the branched structure provides a large number of ends which the polymer can be added to or broken down

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10
Q

Allosteric regulation of phosphorylase

A

subject to allosteric regulation by AMP, ATP and G6P

When AMP is hight ATP is low so phosphorylase is activated.

ATP and G6P compete with AMP binding which inhibits phosphorylase.

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11
Q

Allosteric regulation of Glycogen synthase

A

Glycogen synthase is allosterically activated by G6P, glycogen synthesis is activated when G6P is plentiful.

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