1. increasing the amount of substrate
2. adding more water
3. increasing the temperature
4. decreasing enzyme concentration
What level of protein organization structure explains the 3-D shape of an enzyme?
1. primary structure
2. tertiary structure
3. secondary structure
4. quaternary structure
Given below is a schematic metabolic pathway. In an experiment, the concentration of enzyme 1 was increased but the concentration of enzymes 2 and 3 were kept constant What would happen to the rate of production of D?
(1) it would go down
(2) it would go up
(3) it would stay the same
(4) it would stop
The graph shown below shows the effect of a certain factor on the rate of a reaction catalyzed by an enzyme. The X-axis would show the said factor and that will be:
(1) substrate concentration
(3) enzyme concentration
In the following graph, the X-axis will show:
(1) substrate concentration
(2) enzyme concentration
(4) enzyme concentration or substrate concentration
The rate of enzyme action decreases at higher temperature [after a certain value] because the increased heat
(1) changes the pH of the system
(2) alters the active site of the enzyme
(3) neutralizes the acids and bases in the system
(4) increases the concentration of the enzyme
The "lock and key hypothesis", given by Emil Fischer, attempts to explain the mechanism of:
(1) denaturation of enzyme proteins
(2) the formation of peptide binds
(3) sharing of electrons
(4) enzyme specificity
At about 00 C, most enzymes are
If an active-site directed inhibitor is present in the medium, the curve that will represent the progress of the chemical reaction will be shown by the letter:
If a non active-site directed inhibitor is present in the medium, the curve that will represent the progress of the chemical reaction will be shown by the letter:
Which of the following will fit in the description of a competitive enzyme inhibitor?
(1) a highly reactive compound.
(2) a metal ion such as Hg2+ or Pb2+
(3) structurally similar to the substrate.
(4) water insoluble.
A non-competitive inhibitor of an enzyme catalyzed reaction
(1) binds to the Michaelis complex (ES)
(2) increases Vmax
(3) is without effect at saturating substrate concentrations
(4) can actually increase reaction velocity in rare cases
The measurement of which of the following would be indicator of the degree of inhibition by a competitive enzyme inhibitor?
(2) The y-intercept on a Limeweaver-Burke Plot
(4) ¼ Vmax
An allosteric inhibitor of an enzyme usually
(1) binds to the active site.
(2) participates in feedback regulation.
(3) denatures the enzyme.
(4) causes the enzyme to work faster.
A change in an amino acid located distantly from the active site of an enzyme can affect the specificity of the enzyme towards its substrate by:
(1) making the enzyme unstable
(2) cause a relocation of the enzyme within a cell
(3) changing the shape of the protein
(4) changing the optimum pH and temperature values for the enzyme