Refer the graph of two enzymatic reactions and answer the following questions :
(a) What is denoted by plot A?
(b) What is denoted by plot B?
(c) What is C? What is the difference between C of A & B.
(d) What is allosteric modulation?

Explanation

Plot A denote the enzyme substrate reaction which is high after reaching its maximum velocity due to high affinity between them . The rate of reaction is at a rapid state as compared to B .
(b) In plot B , the rate of reaction is slow as compared to plot A due to less affinity of enzyme for the substrate , but the increase in enzyme concentration increases the rate of reaction by producing more active sites to the substrates .
(c) C is the Michaelis constant (Km) Km is the concentration of a substrate required in order for an enzyme to act at half of its maximum velocity `(V_("max"))` . The Michaelis constant is the measure of the affinity of an enzyme for a substrate . In A there is a high affinity for substrate than the affinity of enzyme in B .
(d) Allosteric modulation is the regulation of an enzyme or protein by binding an effector molecule at the protein.s activity are referred to as allosteric activators , whereas those that decrase the protein.s activation are called allosteric inhibitors . The term allostery comes from Greek allos "other" and stereos , "shape" , referring to the regulatory site of an allosteric protein.s being separate from its actives site . Allosteric regulation is a natural examples of feedback control .