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Lecture 20

MCB 2000 Lecture Notes - Lecture 20: Acetyl-Coa, Phosphofructokinase 2, Thiamine Pyrophosphate

2 pages92 viewsSpring 2017

Molecular and Cell Biology
Course Code
MCB 2000

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Monday, March 27, 2017
MCB 2000
-exam membranes through pyruvate hydrogenase
-Regulation of PFK-1, the rate limiting enzyme and control point in glycolysis
-Activity of PFK-1 is dependent on cellular energy charge (levels of ATP and AMP)
-ATP is both a substrate and allosteric modifier
-PFK-1 primarily uses energy charge (concentrations of ATP/ADP/AMP) for allosteric
-small drop in ATP is magnified by a larger increase in either ADP/AMP or both
-absolute concentrations of ADP/AMP are less than ATP, it is the percent/fold changes
in the concentrations that make the difference
-Cell charge ~0.85-0.9
-ATP is both the substrate and a negative allosteric modifier
-when ATP is a substrate, will bind in active site of PFK-1, will happen when ATP is low
in concentration and needs to be synthesized
-affinity for ATP in PFK-1 when [ATP] has dropped is high
-PFK activity increases when energy charge is low
-PFK activity decreases when energy charge is high
-Fructose-2,6-bisphosphate as an allosteric modifier of PFK-1
-Enzyme with 2 distinct catalytic activities will respond to insulin/glucagon ratio
-ratio high: fed, kinase domain active
-ratio low: fasted, phosphatase domain active
-PFK-2 and FBPase-2
-Kinase: active when dephosphorylated, makes fructose-2,6-bisphosphate when
insulin:glucagon high
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