Regulation of Carbohydrate Metabolism Flashcards
When blood sugar increases:
Insulin is ____
released
Insulin is released, which leads to the
dephosphorylation of:
- PFK-2
- Pyruvate kinase
- Pyruvate dehydrogenase
- Glycogen synthase
- Glycogen phosphorylase
When blood sugar decreases: ____ is released
Glucagon
glucagon release leads to the ______
•PFK-2 (phosphatase active, ↓ F2,6BP)
Pyruvate kinase (inactive)
•Pyruvate dehydrogenase (E1 inactive)
Glycogen synthase (inactive) •Glycogen phosphorylase (active)
phosphorylation
Insulin is released, which leads to the
dephosphorylation of:
PFK-2, Pyruvate kinase, Pyruvate dehydrogenase, Glycogen synthase, Glycogen phosphorylase
leads to active
- Glycolysis
- CAC
- Glycogen synthesis (Glycogenesis)
When blood sugar decreases: Glucagon is released, which leads to the phosphorylation of:PFK-2, Pyruvate kinase, Pyruvate dehydrogenase, Glycogen synthase, Glycogen phosphorylase
this leads to active
Gluconeogenesis
Glycogen breakdown (Glycogenolysis)
enzymes that operate ____equilibrium may be so efficient that a reduction in their activity will have little or no effect on the overall flux.
near
when a reaction is rate limiting
[S] ____ [S]eq
[S] > [S]eq
when rxn is rate limiting
[P] ___ [P]eq
[P] < [P]eq
when rxn is rate limiting
∴ΔG = ___
negative
___ (3) catalyze glycolytic steps that are rate limiting
Hexokinase, Phosphofructokinase, and Pyruvate Kinase
When an enzyme catalyzes a reaction that is near equilibrium, it means that its rate of catalysis is
much faster than net flux through that step
When an enzyme catalyzes a reaction that is ____, it means that its rate of catalysis limits flux through that step in a pathway
highly exergonic
what steps need to be bypassed (bc they are highly exergonic) in glucogenogensis?
the same ones that are rate limiting in glycolysis
Hexokinase, Phosphofructokinase, and Pyruvate Kinase
which point is not the optimal point to regualte glycolysis? why?
Bypass III is not the optimal point to regulate Glycolysis because G6P is required for other pathways
which point IS a good point to regulate glycolysis?
PFK
or pyvutate kinase
why does pyruvate kinase need to be turned off during glucogenogenssi?
the concentration of its substrate, PEP, will be elevated
PFK is allosterically inhibited by
ATP as a feedback inhibitor
___ effectively competes with ATP for binding at the allosteric site
- AMP
- F2,6BP
what speeds up glyciolysis? why?
AMP effectively competes with ATP for binding at the allosteric site signaling
Glycolysis to speed up to replenish the ATP supply
When an allosteric activator binds, PFK assumes a conformation that places a ___ near a ____
stabilizing positive charge (R162) near the negatively charged substrate
when an allosteric inhibitor binds to PFK, the conformation assumed places a
destabilizing negative charge (E161) near the negatively charged substrate
F2,6BP prevents ____ because it competes with ATP for binding on PFK
feedback inhbiition of glyolysis
, F2,6BP and AMP bind to an allosteric site on ____and inhibit, thereby slowing Gluconeogenesis
FBPase
effect of F2,6BP and AMP on gluyconeogensis?
slow gluconeogensis
difference between FBP and F2,6BP structurally?
The second phosphoryl on F2,6BP is on the C2 hydroxyl instead of on the C1 hydroxyl as is the case for FBP
In the dephosphorylated state, the catalytic site in the ____ domain ss active
kinase domain, called PFK-2
what is PFK-2?
catalytic site in the kinase domain