I. Segment representing the energy of activation.

   II. Segment representing the amount of free energy released by the reaction.

   III. Transition state

   IV. Segment would be the same regardless of whether the reaction were uncatalysed or catalysed

Which one is correct?

	I	II	III	IV
(a)	1	3	2	4
(b)	1	2	3	2
(c)	1	3	2	4
(d)	1	2	4	3

Which one of the graphs shows the effect of pH on the velocity of a typical enzymatic reaction (V)?

1.     2.     3.      4.

Which one of the graphs show the effect of temperature on the velocity of a typical enzymatic reaction?

Which one of the following graphs show the relationship between the rate of an enzymatic activity and substrate conc.(S):

Choose the correct statement(s):
(1) Km (Michaelis - Menten) constant is the substrate concentration at which the enzymatic reaction attains half of its maximum velocity (1/2 Vmax)

(2) At lower Km, higher the substrate affinity for enzyme

(3) Vmax is reached when all the active sites of an enzyme are saturated with substrate

(4) All are correct

In competitive inhibition:

(1) Inhibitor resembles the substrate in molecular structure

(2) Competition between substrates and inhibitors to occupy active sites

(3) Binding the inhibitors to activities sites declines the enzyme action

(4) All are correct

Amylase is an example of:

(1) Oxidoreductase                                     

(2) Transferase

(3) Hydrolase                                             

(4) Ligase

The figure given below shows the conversion of a substrate into product by an enzyme. In which one of the four options (a-d) the components of reaction labelled as A, B, C and D are identified correctly?

The adjoining graph shows change in conc. of substrate on enzyme activity. Identify A, B and C:

Go through the figures and select the correct option:

(1) I - In non-competitive type of enzymatic inhibition the V max decreases and K_m remain unchanged

     II - In competitive type of enzymatic inhibition the V_max decreases and K_m remain unchanged

(2) II - In non-competitive type of enzymatic inhibition the V_max decreases and K_m remain unchanged

      I - In competitive type of enzymatic inhibition the V_max remain same and K_m is changed

(3)  I - In non-competitive type of enzymatic inhibition the V_max increases and K_m remain unchanged

      II - In competitive type of enzymatic inhibition the V_max changes and K_m decreases

(4)  I - In non-competitive type of enzymatic inhibition the V_max increases and K_m remain unchanged

      II - In competitive type of enzymatic inhibition the V_max increases and K_m increases