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Lecture 20

MCB 2000 Lecture 20: PFK-1

2 Pages

Molecular and Cell Biology
Course Code
MCB 2000

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Monday, March 27, 2017 MCB 2000 3/27 - 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 modification - 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 - rati
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