Lecture 3: Key Summary Points Flashcards

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1
Q

Allosteric Regulation of PFK1: Activate? Inhibit? or No Change?

A

Activate: F26BP, ADP or AMP
Inhibit: High ATP, citrate, H+
No Change: Enolase & aldolase

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2
Q

Where is the allosteric site?

A

In the middle of the ring

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3
Q

Which state is inactivated or activated?

A

Inactivated: T state
Active: R state

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4
Q

Allosteric Regulation of pyruvate kinase (PK): Inhibit, Activate, or no change?

A

Inhibit: Alanine, ATP
Activate: F1,6 bisP

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5
Q

Why regulated at multiple enzymes?

A

Because glycolysis is both a catabolic and an anabolic pathway

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6
Q

Which enzyme breaks down glycogen?

A

Glycogen phosphorylase

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7
Q

What are the products of glycogen phosphorylase?

A

G1P

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8
Q

What is the enzyme involved that turns G1P to G6P?

A

PGMutase

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9
Q

What are the 3 layers of control in glycogen metabolism?

A

1: P-glycogen phosphorylase (active); P-glycogen synthase (inactive)
2: Kinase (Glucagon); Phosphatase (Insulin)
3: Glucagon; Insulin

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10
Q

If liver is hit with insulin, which process would decrease, increase, or no change?

A

Increase: active transport, glycolysis, glycogen synthesis, lipid synthesis, and protein synthesis
Decrease: lipid breakdown and gluconeogenesis

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11
Q

Glycolysis vs. gluconeogenesis: GLYCOLYSIS PFK1 (Activate & Inhibit)

A

Activate: AMP, F2,6 BP
Inhibit: Citrate

F1,6 BPase is the opposite of these for gluconeogenesis

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12
Q

Glycolysis vs. gluconeogenesis: GLYCOLYSIS PK (Activate & inhibit)

A

Activate: F1,6 BP
Inhibit: ATP

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13
Q

Glycolysis vs. gluconeogenesis: GLUCONEOGENESIS PC (activate & inhibit)

A

Activate: Acetyl CoA (fuel rich)
Inhibit: ADP (energy charge)

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14
Q

Which enzyme will increase the size of glycogen?

A

Glycogen synthase

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15
Q

In order to activate glucose for glycogen synthesis, glucose is turned into what?

A

UDP-glucose

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