Question

10. A good transition-state analog: A) binds covalently to the enzyme. B) binds to the enzyme more tightly than the substrate. C) binds very weakly to the enzyme. D) is too unstable to isolate. E) must be almost identical to the substrate. 11. Which factor bas NOT been shown to play a role in determining the specificity of protein kinases? A) disulfide bonds near the phosphorylation site B) primary sequence at phosphorylation site C) protein quaternary structure D) protein tertiary structure E) residues near the phosphorylation site

Answer 1

10) A good transition state analog is a compound generally used as a inhibitor in the reactions which are catalysed with the use of enzymes.Good Transition state analogs basically binds with the enzyme more tightly as compared to substrate and slows the reactions.Therefore, the correct option is (B).

11) protein kinase are basically involved in the modification of other proteins by addition phosphate to them.The primary sequence at the phosphorylation site is not primarily involved in determining the specificity of protein kinases.Rest other option are involved in determining the specificity.Therefore, the correct option is (B).

12) Activation energy is the energy that is required in the course of reaction to produce products from the reactants .The higher the activation energy, slower is the reaction and vice versa.The catalyst (enzymes) lowers the activation energy of the reaction and leads to the formation of product.Therefore, the correct option is (C).