Question

Explain how you would overcome a non-competitive inhibitor in an enzymatically catalyzed reaction to increase the reaction rate, if you had plenty of materials on hand.

simple basic biology knowledge

Answer 1

Lock and Key hypothesis is the basis of enzyme substrate reaction. A competetive inhibitor is a chemical substance that binds to the non active site of the enzyme and alters the chemical structure of the enzyme. It is an allosteric regulation binding to the allosteric site of the enzyme and decreasing the efficacy of the enzyme .The change in the 3 D structure of the enzyme changes the rate of catalytic action of the enzyme . In enzyme kinetics the Maximum velocity of the reaction, Vmax decreases due to non competetive inhibitor. Sometimes the overall shape of the size of the substrate is changed and slow down the rate of enzyme reaction. Example for non competitive inhibitors include Alanine and ATP which act as non-competitive inhibitors of pyruvate kinase, the enzyme that catalyzes the final step in the glycolytic pathway.