ENZYMES
Q:1: The catalytic activity of an enzyme is (A) 37°C
restricted to its small portion called (B) 40°C
(C) 25°C
(D) 30°C
(A) Active site
(B) Passive site Q:7: Optimum pH value for pepsin is
(C) Allosteric site
(D) All Choices are correct
(A) 5.5
Q:2: An activated enzyme made of polypeptide (B) 7.4
chain and a co-factor is (C) 4.1
(D) 1.4
(A) Coenzyme
(B) Substrate Q:8: Competitive inhibitors stop an enzyme from
(C) Apoenzyme working by
(D) Holoenzyme
(A) Changing the shape of the enzyme
Q:3: Koshland in 1959 proposed (B) merging with the substrate instead
(C) blocking the active site of the enzyme
(A) Fluid mosaic model (D) combining with the product of the reaction
(B) Induce fit model
(C) Lock and key model Q:9: The enzymes are sensitive to
(D) Reflective index model
(A) Changes in pH
Q:4: Enzymes are largely __________ in their (B) Changes in temperature
chemical nature. (C) Both A and B
(D) None of these
(A) Lipids
(B) Steroids Q:10: Enzyme B requires Zn2+ in order to
(C) Proteinaceous catalyze the conversion of substrate X. The zinc is
(D) All A, B and C best identified as a(n):
Q:5: Who proposed “lock and key” model to (A) Coenzyme
study enzyme – substrate interaction? (B) Activator
(C) Substrate
(A) Koshland (1959) (D) Product
(B) Wilhelm Kuhne (1878)
(C) Fischer (1898) Q:11: The enzyme minus its coenzyme is referred
(D) None of these to as the
Q:6: In human body the optimum temperature (A) Iso-enzyme
for enzymatic activities is (B) Metalloenzyme
(C) Apoenzyme
(D) All of these
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ENZYMES
Q:12: The “lock and key” model of enzyme action (A) Enzyme in the breakdown of hydrogen
illustrates that a particular enzyme molecule peroxide
(B) Enzyme in the synthesis of hydrogen peroxide
(A) forms a permanent enzyme-substrate complex (C) Emulsifier in the digestion of hydrogen
(B) may be destroyed and resynthesized several peroxide
times (D) Indicator in the detection of hydrogen
(C) interacts with a specific type of substrate peroxide
molecule
(D) reacts at identical rates under all conditions
Q:17: An enzyme is generally named by adding
Q:13: Consider this reaction. A + B --> C + D + ________ to the end of the name of the
energy. ____________.
(A) This reaction is exergonic (A) "-ase". coenzyme
(B) An enzyme could still speed the reaction (B) "-ase". cell in which it is found
(C) A and B are reactants; C and D are products (C) "-ose". substrate .
(D) All of these are correct (D) "-ase". substrate
Q:14: An inhibitor that changes the overall shape Q:18: The minimum amount of energy needed
and chemistry of an enzyme is known as a(n) for a process to occur is called the
(A) Auto-steric inhibitor (A) Minimal energy theory
(B) Competitive inhibitor (B) Process energy
(C) Kinetic energy
(C) Steric inhibitor
(D) Noncompetitive inhibitor (D) Activation energy
Q:15: Non-protein components of enzymes are Q:19: A student conducts an experiment to test
known as the efficiency of a certain enzyme. Which would
probably not result in a change in the enzyme's
(A) Coenzymes efficiency?
(B) Activators
(C) Cofactors (A) Adding an acidic solution to the setup
(D) All A, B, and C (B) Adding more substrate but not enzyme
(C) Increasing temperature of solution
Q:16: The reaction below occurs within the cells (D)All a, b, & c change enzyme's efficiency
to prevent the accumulation of hydrogen
Q:20: Enzymes function as
peroxide. In this reaction, catalase functions as
an
(A) Organic catalysts
(B) Inorganic catalysts
(C) Inhibitors
(D) All of these
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ENZYMES
Q:21: A catalyst is a chemical involved in, but not (A) Enzyme-product complex
____________ by, a chemical reaction. (B) Enzyme-intermediate complex
(C) Enzyme-substrate complex
(A) Supported (D) None of these
(B) Changed
(C) Controlled Q:27: The function of competitive inhibitors is
(D) All of these defined by their ability to interact or bind to
Q:22: Many enzymes function by (A) The active site of an enzyme
__________________ the activation energy of (B) Regulatory sub-units of an enzyme
reactions. (C) Non-competitive inhibitor
(D) Enzyme cofactors
(A) Increasing
(B) Promoting Q:28: If an enzyme solution is saturated with
(C) Lowering substrate, the most effective way to obtain an
(D) Both A and B even faster yield of products would be
Q:23: An uncatalysed reaction requires a (A) Add more of the enzymes
(B) Add more substrate
(A) Higher activation energy (C) Add an allosteric inhibitor
(B) Lower activation energy (D) Add a non-competitive inhibitor
(C) Balanced activation energy
(D) All of these Q:29: During _____________ the final product of
a metabolic pathway turn off the first step of
Q:24: It suggests that the binding of the metabolic pathway.
substrate to the enzyme alters the structure of
the enzyme, placing some strain on the substrate (A) Positive feed back
and further facilitating the reaction. (B) Negative feed back
(C) Competitive feed back
(A) Lock and Key hypothesis (D) Both A and C
(B) Induced fit hypothesis
(C) Fischer’s hypothesis Q:30: _____________ occurs when the inhibitory
(D) D.D. Wood’s hypothesis chemical, which does not have to resemble the
substrate, binds to the enzyme other than at the
Q:25: They are non-protein organic molecules active site.
bound to enzymes near the active site.
(A) Noncompetitive Inhibition
(A) Activators (B) Competitive Inhibition
(B) Coenzymes (C) Uncatalysed reaction
(C) Holoenzymes (D) All A, B and C
(D) All of these
Q:31: Which one is not attribute of enzyme
Q:26: The first step in any reaction catalysed by
an enzyme is the formation of a specific
association between the molecules called an
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ENZYMES
(A) Specific in nature Q:37: Proteinaceous part of holoenzyme is
(B) Protein in chemistry
(C) Consumed in reaction
(D) Increases rate of reaction (A) Prosthetic group
(B) Apoenzyme
Q:32: Which one inactivates an enzyme by (C) Lecithin
indirectly changing the shape of the active site of (D) None of these
an enzyme
Q:38: The "lock and key hypothesis" attempts to
(A) Non-competitive inhibitor explain the mechanism of
(B) Competitive inhibitor
(C) Coenzyme (A) vacuole formation
(D) Activator (B) pinocytosis
(C) sharing of electrons
Q:33: The enzymes are classified into (D) enzyme specificity
(A) Five groups Q:39: An enzyme that hydrolyzes protein will not
act upon starch. This fact is an indication that
(B) Three groups
(C) Six groups enzymes are
(D) Four groups
(A) hydrolytic
Q:34: Non-proteinaceous part of holoenzyme is (B) specific
(C) catalytic
(A) Prosthetic group (D) synthetic
(B) Apoenzyme
(C) Tubulin Q:40: The site where enzyme catalyzed reaction
(D) None of these takes place is called?
Q:35: Enymes are highly specific for a given (A) Active site
substrate which is due to the shape of their (B) Allosteric site
(C) Denatures site
(A) Active site (D) Dead Site
(B) Allosteric site
(C) Non-competitive site Q:41: What is a cofactor?
(D) None of these
(A) Inorganic ions
Q:36: The name enzyme was suggested in 1878 (B) Organic molecules
by the German physiologist (C) Both a and b
(D) None of the above
(A) Wilhelm Kuhne
(B) Koshland Q:42: Mg+2 is an inorganic activator for the
(C) Fischer enzyme
(D) Paul Filder
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ENZYMES
(A) Phosophatase Q:48: In the Lock and Key model of enzyme
(B) Carbonic anhydrase action, the part of the enzyme that recognizes
(C) Enterokinase the substrate is known as the
(D) Amylase
(A) Enzyme-substrate complex
Q:43: Zn+2 is an inorganic activator for enzyme. (B) Product
(C) Enzyme-product complex
(A) Carbonic anhydrase (D) Active site
(B) Phosophatase
(C) Chymotrypsin Q:49: Which model of enzyme action is
(D) Maltase represented in this diagram.
Q:44: Which antibiotic blocks the active site of
an enzyme that many bacteria used to make cell-
walls.
(A) Amphotericin
(B) Gentamicin
(C) Penicillin
(D) Cephalosporin (A) Fluid mosaic model
(B) Induce fit model
Q:45: DDT and Parathion are inhibitors of key (C) Lock and key model
enzymes in (D) Reflective index model
(A) Nervous system Q:50: A certain enzyme will hydrolyze egg white
(B) Respiratory system but not starch. Which statement best explains
(C) Digestive system this observation?
(D) Circulatory system
(A) Starch molecules are too large to be
Q:46: At high temperature the rate of enzyme hydrolyzed
action decreases because the increased heat (B) Enzyme molecules are specific in their actions
(C) Egg white acts as a coenzyme for hydrolysis
(A) Changes the pH of the system (D) Starch is composed of amino acids.
(B) Alters the active site of the enzyme
(C) Neutralize acids and bases in the system Q:51: At about 0 C, most enzymes are
(D) Increases the concentration of enzymes
(A) Inactive
Q:47: Which of the following enzymes would (B) Active
digest a fat? (C) Destroyed
(D) Replicated
(A) sucrase
(B) protease Q: 52: Vitamins are essential to the survival of
(C) Ligase organisms because vitamins usually function as
(D) lipase
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ENZYMES
(A) Substrates
(B) Nucleic acids
(C) Co-enzymes
(A) Competitive
(D) Nucleosides
(B) Non-competitive
(C) Allosteric
Q:53:When a molecule binds to an area of an
(D) Both B and C
enzyme that is not the active site, and changes
the shape of the enzyme so that it no longer can
Q:57: Which enzyme represents an enzyme
work, this is called
functioning in this reaction?
(A) denaturation
(B) competitive inhibition
(C) noncompetitive inhibition
(D) substrate delocation
Q:54: What is a coenzyme?
(A) Inorganic ion
(B) Organic molecule
(C) Both A and B
(D) None of these
(A) E
(B) C
Q:55: Which statement best expresses the
(C) B
information represented in the graph shown?
(D) A
Q:58: Enzyme which converts Starch into
Maltose:
(A) Zymase
(B)Lipase
(C)Maltase
(A) The action of enzymes varies with pH
(B) A pH of 7 provides the optimum environment (D)Sucrose
for digestive enzymes Q:59: Correct statement for enzyme’s activity at
(C) Gastric juice is active at a pH extending from 0 100°C is:
to 12
(D) Acids have a pH greater than 7 (A) Activity is reduced to minimum
Q:56: Which type of inhibitor is shown in this (B) Activity is accelerated
diagram? (C) Enzymes are destroyed
(D) Enzymes shape becomes changed
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ENZYMES
Q:60: Name of enzyme found in liver:
(A) Cellulase
(B) Astrase
(C) Zymase
(D) Catalase
Answer Key
18.D
1.A
19.D
2.D
20.A
3.B
21.B
4.C
22.C
5.C
23.A
6.A
24.B
7.D
25.B
8.C
26.C
9.C
27.A
10.B
28.A
11.C
29.B
12.C
30.A
13.D
31.C
14.D
32.A
15.D
33.C
16.A
34.A
17.D
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ENZYMES
35.A
36.A
37.B
38.D
39.B
40.A
41.C
42.A
43.A
44.C
45.A
46.B
47.D
48.D
49.C
50.B
51.A
52.C
53.C
54.B
55.A
65.D
57.C
59.C
60.D
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