Question 1 Control points for glycolysis The enzyme phosphofructokinase is allosterically inhibited by and The enzyme phosphofructokinase is activated by an excess of 2 pts
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(2 points) Phosphofructokinase (PFK) is the main regulatory enzyme in glycolysis; it can be positively regulated. What molecule binds to the allosteric site to activate this enzyme?
Sri K.
For each of the following molecules, state whether you expect each to be an activator or inhibitor of pyruvate kinase, the 10th enzyme of glycolysis. Then give a type of regulation (competitive, allosteric, covalent, genetic) and a regulatory theme (feedforward, feedback, cell status, organism status) for each one. (3 points each) ATP- ADP- Fructose-1,6-diphosphate- D. Acetyl-CoA- E. Protein kinase A (enzyme which is activated by glucagon)
Adi S.
Regulation of Enzyme Activity Fructose-2,6-bisphosphate (F-2,6-BP) is a metabolic intermediate that functions as an allosteric activator of the glycolytic enzyme phosphofructokinase-1 (PFK-1). A bifunctional enzyme that can be called either phosphofructokinase-2 (PFK-2) or fructose bisphosphatase-2 (FBPase-2) catalyzes the following reactions: F-6-P + ATP --> F-2,6-BP + ADP F-2,6-BP + H2O --> F-6-P + Pi Fill in the blanks to make this statement TRUE: _____ levels of AMP will _____ PFK-2, and _____ FBPase-2. Low; activate; inhibit High; activate; inhibit Low; inhibit; activate High; inhibit; activate
Suman K.
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