BIO Unit # 3, Enzymes, F. Sc Part-1

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ENZYMES
1.   Enzymes are the most important group of proteins which are biologically
      a. Active                b. Inactive                    c. Dynamic                  d. Energetic
2.   The catalytic activity of enzymes is restricted to a small portion of the enzyme known as
      a. Binding site;                   b. Active site                c. Catalytic site            d. Non-binding site
3.   The reactant called — is attached to the active site of enzyme.
      a. Food particle                  b. Substance                c. Subtrate                    d. Product
4.   If the non-protein part is covalently bonded to enzyme, it is known as a: (GB-2007)
      a. Coenzyme                      b. Co-factor                 c. Holoenzyme                        d. Prosthetic group.
5.   An activated enzyme consisting of polypeptide chain and a cofactor is known as
      a. Holoenzyme                  b. Apoenzyme             c. Coenzyme                d. Zymogen
6.   Enzymes are very------------- in their action
      a. General                          b. Specific                   c. Precise                     d. Exact
7.   An enzyme is a three dimensional -----— protein.
      a. Fibrous                           b. Straight                    c. Globular                   d. Branche
8.   An enzyme and its substrate react with each other through definite charge bearing sites called sites.
      a. Catalytic                         b. Passive                     c. Bidding                    d. Active
9.   Lock and Key model was proposed by:
      a. Koshland                                   b. Emil Fischer             c. Fiemming                 d. Watson
10. An ------ is a chemical substance which can react (in place of substrate) with the enzyme but is not transformed into product(s) and thus blocks the active site
      a. Inhibitor                         b. Accelerator              c. Retarder                   d. Reducer
11. For enzymes of human body —-— °C is the optimum temperature
      a. 27                                  b. 17                            c. 37                            d. 47
12. — inhibitors occupy the active sites by forming covalent bonds or they may physically block the active sites.
      a. Reversible                      b. Irreparable               c. Reparable                 d. Irreversible
13. The cofactor usually acts as "bridge" between the
      a. Enzyme & substrate       b. Coenzyme & substrate   c. enzyme & product            d. Cofactor& substrate
14. If non-protein part is loosely attached to the protein part it is known as: (LB-2005, SB-05)
      a. Co-factor                                   b. Enzyme                   c. Holoenzyme             d. Prosthetic group
15. The enzymes are
      a. Fibrous proteins             b. Globular proteins     c. Angular proteins      d. Spherical proteins
16. Any enzyme reacts only with its specific
      a. Surface                          b. Product                    c. Substrate                  d. Reactant
17. The active site of the enzyme is made up of two definite regions i.e., the binding site and the:
      a. Non-binding site                        b. Non-catalytic site     c. Inactive site              d. Catalytic site
18. On this basis of new evidences Induce Fit model was proposed by
      a. Koshland                                   b. Emil Fischer             c. Robert Koch d. Louis Pasteur
19. If the amount of enzyme is increased by two fold the reaction rate is:
      a. Same                              b. Doubled                   c. Fourfold                   d. Threefold
20. All enzymes can work at their; maximum rate at a specific temperature called:
      a. Minimum temperature    b. Maximum temperature         c. Optimum temperature                      d. Best temperature
21. Every enzyme functions most effectively over a narrow range of ph known as:
      a. Best Ph                           b. Mininum PH                        c. Maximum Ph                       d. Optimum Ph
22. Because of the structural similarity with the substrate, competitive inhibitors may be selected by the binding sites, but are not able activate the
      a. Catalytic sites                 b. Accelerating sites     c. Inactive sites                        d. Active sites
23. Some enzymes also have a non-protein part known as a cofactor which is essential for the proper functioning of the
      a. Substrate                                    b. Enzymes                  c. Reactant                   d. Product
24. Any factor that can alter the chemistry and shape of an enzyme affect its rate of:
      a. Reaction                         b. Activation                c. Catalysis                  d. both b & c  
25. At low concentration of substrate the reaction rate is directly proportional to the available:
      a. Enzyme                          b. Reactant                   c. Product                    d. Substrate
26. Extreme changes in pH cause the bonds in the enzyme to break resulting in the enzyme
      a. Denaturation                  b. Deceleration            c. Deconformation       d. Deconfiguration
27. Reversible Inhibitors form weak linkages with the:
      a. Enzyme                          b. Reactant                   c. Product                    d. Substrate

28. Non-competitive Inhibitors form enzyme inhibitor complex at a point other than the:
      a. Catalytic site                  b. Active site                c. Binding site              d. Both a & b
29. Some enzymes use metal-ions as co-factors like:
      a. Mg2+                             b. Fe2+            c. Cu2+                        d. All a, b, c
30. The detachable co-factor is knowri as an activator if it is
      a. Organic ion                    b. Non-ionic    c. Inorganic ion                        d. Both a & c
31. An enzyme with its coenzyme, or prosthetic group, removed is designated as:
      a. Apoenzyme                   b. Holoenzyme                        c. Hypoenzyme                       d. Prosoe'nzyme
32. The chemical reaction can oe accelerated by an enzyme even in
      a. Small amounts               b. Moderate amounts   c. Large amounts         d. All a, b, c
33. Even for a minor change in pH, temperature and substrate concentration, enzymes are:
      a. Aware                            b. Sensitive                  c. Susceptible               d. Receptive
34. The activation energy of the reactions is lowered by:
      a. Coenzymes                    b. Substrate                  c. Enzymes                  d. Product
35. The binding site helps the enzyme in the recognition and binding of a proper substrate to produce an:
      a. BS complex                   b. PS complex              c. RS complex             d. ES complex
36. According to Lock and Key Model the active site is:
      a. Rigid structure                b. Soft structure                       c. Terrible structure      d. Attractive structure
37. By increasing the enzyme molecules, there is an increase in the number of:
      a. Binding sites                  b. Active sites              c. Catalytic sites           d. None
38. Heat provides activation energy and therefore, chemical reactions are accelerated at:
      a. Low temperatures          b. Moderate temperatures        c. High temperatures    d. None
39. The ionization of the amino acids at the active site can be changed by a slight change in:
      a. Temperature                   b. Substrate concentration        c. Enzyme concentration         d. pH
40. The optimum pH of Pepsin is:
      a. 2.00                               b. 4.00             c. 6.00             d. 8.00
41. The optimum pH of Sucrase is:
      a. 2.50                               b. 4.50             c. 6.50             d. 8.50
42. The optimum pH of Enterokinase is: (LB-2Q07)
      a. 1.50                               b. 3.50             c. 5.50             d. 7.50
43. The optimum pH of Salivary amylase is: (LB-2006)
      a. 2.80                               b. 4.8.0.                       c. 6.80             d. 8.80
44. The optimum pH of Catalase is
      a. 2.50                               b. 4.60             c. 5.70             d. 7.60
45. The optimum pH of Chymotrypsin is:
      a. 7.00 - 8.00                     b. 6.00 - 7.00   c. 5.00 - 6.00               d. 4.00 - 5.00
46. The optimum pH of Pancreatic lipase is:
      a. 7.00                               b. 9.00             c. 5.00             d. 3.00
47. The optimum pH of Arginase is:
      a. 7.70                               b. 9.70             c. 5.60             d. 4.25
48. Poisons, like cyanide, antibodies, antimetabolites and some are examples of:

      a. Enzymes                                    b. Coenzymes              c. Inhibitors                 d. Holoenzymes

I am Mechatronics and Control Engineer from UET, Lahore. Helping Engineering students gives me pleasure.

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