Question suggestions by Department of Biochemistry

SRIMS&SH Durgapur
Theory Chapter Enzymes
LONG QUESTIONS
1. Define enzyme and write IUBMB Enzyme classification giving two examples each.
2. Write a note on Cofactors & Coenzymes with two example each.
3. What are metalloenzymes? Explain with examples.
4. Discuss the role of substrate concentration in enzyme catalysed reaction.
5. Explain the Michaelis Menten equation and explain the role of substrate
concentration on the rate of enzyme catalysed reaction with the help of graphs.
6. Illustrate how Vmax and Km are affected by competitive and non-competitive
inhibition of enzymes.
7. Explain with the help of enzyme velocity curve how following factors regulate the
enzyme activity: Concentration of enzyme, Concentration of substrate, pH,
Temperature.
8. Differentiate between the lock and key model & induced fit model for enzyme
catalysis.
9. Describe the factors affect enzyme activity.
10. Describe different types of enzyme inhibition. Write the clinical importance of
enzyme inhibitors.
11. Explain the mechanism of Enzyme Catalysis
12. Define isoenzymes. Discuss the isoenzyme pattern of lactate dehydrogenase and
creatine kinase in relation to their role in clinical diagnosis. Explain the principles by
which these isoenzymes can be separated and identified in a laboratory. [1+4+4+3]
13. Define isoenzymes. Write the clinical significance of serum isoenzymes in cardiac
disorder. [2+5]
14. Describe in detail how covalent modification and repression/depression mechanism
can regulate the enzyme action in vivo.[7]
15. Describe the oxidoreductase group of enzymes.
16. Define International unit of enzyme activity.
17. Describe the clinical use of enzymes.
18. Describe the diagnostic and therapeutic use of enzymes.
19. Define Km. Explain the effect of substrate concentration on enzyme activity. Describe
non- competitive enzyme inhibition with diagrams and two examples. Define
International Unit of enzyme activity (U/L). (1+3+5+1)
20. Describe allosteric regulation of enzyme activity.
21. Enumerate some diagnostic enzymes in body fluids.
22. Enumerate some enzymes that can be used as tumor markers.
EXPLAIN WHY
1. The mode of action of metalloenzymes and metal activated enzymes are different
2. Coenzymes act as co-substrate in the enzyme catalysed reaction
3. The Km value for glucokinase is much higher than that for hexokinase though both
act on glucose
4. Methotrexate is used in anti-cancer therapy.
5. Statins acts as cholesterol lowering agent.
6. Allopurinol is called suicide inhibitor. / Allopurinol is used in the treatment of gout.
7. In competitive inhibition, larger amount of substrate can overcome the effect of
inhibition.
8. Disulfiram used in the treatment of alcoholism.
9. Di-isopropylphosphofluoride can inhibit an enzyme acetylcholine esterase
10. Isoenzyme assay helps in diagnosis of MI.
11. Non-functional plasma enzymes are important only for clinical purpose.
12. Isoenzymes of ALP are of diagnostic significance.
13. Coenzymes are called co-substrates.
14. Multifunctional enzyme and multienzyme complex are different.
15. Synthase and Synthetases are different.
16. Non-competitive enzyme inhibition is irreversible.
17. Ethanol is used in the treatment of methanol poisoning.
18. Aspartate transcarbamoylase is an allosteric enzyme.

SHORT NOTES
1. Km of enzyme
2. Lineweaver-Burk Equation
3. Competitive inhibition
4. Non-competitive inhibition
5. Clinical Application of Enzyme Inhibitor
6. Group Specific Irreversible Inhibition
7. Substrate Analogue Irreversible Inhibition
8. Ribozyme
9. Non-functional enzyme
10. Michalis-Menten equation
11. Isoenzyme
12. Active site of the enzyme
13. Effect of pH on Enzyme activity
14. IUBMB Classification of Enzymes
15. Coenzymes
16. Effect of Temperature on Enzyme activity
17. Non-competitive enzyme inhibition
18. Michaelis Menten constant (Km)
19. Allosteric inhibition
 20. Allosteric enzymes
Clinical Case based Question
A 60-year-old male was brought to the emergency department with complaints of chest
pain, radiating to the left arm for the last 1 hour. He was sweating profusely and on
examination, he had tachycardia and mild hypotension. He has a history of diabetes mellitus
and hypertension for last 15 years and is on medication. He is a chronic smoker for last 20
years. The ECG showed ST-segment elevation. The blood report showed an elevated CK-MB
level of 360 IU/L.
i. What is your most probable diagnosis?
ii. Describe the enzymatic and nonenzymatic markers to diagnose and monitor the
above condition.
iii. Illustrate the occurrence of cardiac biomarkers in the above case with a labelled
diagram.
iv. Enumerate the markers that can predict the risk for the above diagnosis.
v. Enumerate the markers of myocardial stress/congestive cardiac failure.
MCQs
1. Transfer of an amino group from an amino acid to an alpha keto acid is done by:
A. Transaminase
B. Oxidase
C. Transketolase
D. Deaminase
2. All of the following enzymes are regulated by calcium or calmodulin EXCEPT:
A. Adenylate cyclase
B. Glycogen Synthase
C. Guanylate cyclase
D. Hexokinase
3. Hexokinase is a
A. Transferase
B. Reductase
C. Oxidoreductase
D. Oxidase
4. Form of coenzymes are correctly matched EXCEPT:
A. Biotin – carboxylated
 B. Vitamin B12 – ATP
C. Niacin – NAD+, NADP+
D. Vitamin B2 – FAD+, FMN+
5. Zinc is a cofactor for
A. Pyruvate dehydrogenase
B. Pyruvate decarboxylase
C. α – Keto glutarate dehydrogenase
D. Alcohol dehydrogenase
6. All the following enzymes are involved in oxidation – reduction reaction EXCEPT:
A. Dehydrogenase
B. Peroxidase
C. Hydrolase
D. Oxygenase
7. Which of the following enzyme is stable at acidic pH?
A. Pepsin
B. Trypsin
C. Chymotrypsin
D. Carboxypeptidase
8. The Km value of an enzyme is:
A. The substrate concentration at half maximal velocity
B. Half the substrate concentration at maximal velocity
C. Dissociation constant of enzyme concentration
D. The total enzyme concentration
9. Lineweaver-Burk (double reciprocal) graph is ploted by:
A. Substrate concentration against Vmax
B. Reciprocal of substrate concentration against reciprocal of velocity
C. Reciprocal of initial velocity against substrate concentration
D. Km against initial velocity
10. Which one of following functional enzyme is present in plasma?
 A. Amylase
B. Lipase
C. Alkaline phosphatase
D. Plasminogen
11. Creatine kinase level in serum is increased in:
A. Myocardial infraction
B. Infective hepatitis
C. Prostate cancer
D. carcinoma of lung
12. Enzyme elevated in alcoholic liver disease is:
A. Alanine transaminase (ALT)
B. Alkaline phosphatase (ALP)
C. Nucleotide phosphatase (5’NT)
D. Gamma glutamyl-Transopeptidase (GGT)
13. Which isoenzyme of lactate dehydrogenase (LDH) are raised in myocardial infraction?
A. LDH 1 & 2
B. LDH 2 & 3
C. LDH 3 & 4
D. LDH 4 & 5
14. Which technique is used for separating isoenzymes?
A. Centrifugation
B. Electrophoresis
C. Colorimetry
D. Spectrophotometry
15. Which of the following enzyme has therapeutic application?
A. Creatinine kinase
B. Hexokinase
C. Streptokinase
D. Glucokinase
16. Which one of the following Enzyme is elevated in bone disease?
A. Lipase
B. Amylase
C. Alkaline phosphatase
D. Acid phosphatase
17. Digestive enzymes belong to the class of
A. Transferases
B. Lyases
C. Hydrolases
D. Ligases
18. Co-enzymes are:
A. Dialyzable, non-protein molecules
B. Colloidal protein molecules
C. Structural analogs of enzymes
D. Different forms of the same enzyme
19. The kinetic effect of purely competitive inhibitor of an enzyme
A. Increases Km without affecting Vmax
B. Decreases Km without affecting Vmax
C. Increases Vmax without affecting Km
D. Decreases Vmax without affecting Km
20. Fischer’s ‘lock and key’ model of the enzyme action implies that
A. The active site is complementary in shape to that of substance only after
interaction.
B. The active site is complementary in shape to that of substance
C. Substrates change conformation prior to active site interaction
D. The active site is flexible and adjusts to substrate
21. Enzymes, which are produced in inactive form in the living cells are called
A. Papain
B. Lysozymes
C. Apoenzymes
D. Proenzymes
22. Allosteric enzymes show all the following characteristics EXCEPT:
A. Cooperative binding of the substrate
B. Sigmoid kinetics
C. Binding between substrate and regulatory sites
D. Substrate binding site and regulatory site are different
23. All the following are metallo-enzymes EXCEPT:
A. Xanthine oxidase
 B. Hexokinase
C. Carbonic anhydrase
D. Lactate dehydrogenase
24. The antimetabolite methotrexate acts by:
A. Non- competitive inhibition
B. Formation of a covalent bond between enzyme and inhibitor
C. Increasing the Vmax of the reaction
D. Competitive inhibition
25. An allosteric enzyme:
A. Is generally present at the end of a pathway
B. Generally, catalyzes a reversible reaction
C. Generally, catalyzes the committed step unique to a pathway
D. Possesses only substrate site
26. Regan isoenzyme is increased in
A. Carcinoma of the lung
B. Paget’s disease
C. Osteoporosis
D. Cholestasis
27. Creatine kinase is found in all of the following tissues EXCEPT:
A. Myocardium
B. Brain
C. Muscles
D. Liver
28. Increased levels of lactate dehydrogenase (LDH) can be observed in all of following
disorders EXCEPT:
A. Myocardial infraction
B. Hemolytic anemia
C. Leukemia
D. Glomerulonephritis
29. In competitive inhibition of enzymes
A. Km increase whereas Vmax decrease
B. Km increase whereas Vmax remain unchanged
C. Vmax decrease while Km decrease
D. Vmax decrease while Km remains unchanged
30. In non-competitive enzyme action:
a. Vmax is increased
b. Apparent Km is increased
c. Apparent Km is decreased
d. Concentration of active enzyme molecule is reduced
31. A competitive inhibitor of an enzyme has which of the
following properties?
a. It is frequently a feedback inhibitor
b. It becomes covalently attached to an enzyme
c. It decreases the Vmax
d. It interferes with substrate binding to the enzyme

32. When (S) is equal to Km, which of the following conditions exist?
a. Half the enzyme molecules are bound to substrate
b. The velocity of the reaction is equal to Vmax
c. The velocity of the reaction is independent of substrate concentration
d. Enzyme is completely saturated with substrate

34. Which of the following statements about an enzyme

exhibiting allosteric kinetics with cooperative interaction
is false?
a. A plot of V-Vs (S) has a sigmoidal shape
b. An inhibitor may increase the apparent Km
c. Lineweaver-Burk plot is useful for determining Km and Vmax
d. Removal of allosteric inhibitor may result in hyperbolic V-Vs (S) plot

35. Lock-and-key” model of enzyme action proposed by Fisher implies that:

a. The active site is flexible and adjust to substrate
b. The active site requires removal of PO4 group
c. The active site is complementary in shape to that of the substrate
d. Substrates change conformation prior to active site interaction

36. In competitive inhibition which of the following kinetic effect is true.

a. Decreases both Km and Vmax
b. Increases both Km and Vmax
c. Decreases Km without affecting Vmax
d. Increases Km without affecting Vmax

37. In competitive inhibition of enzymes action

a. The apparent Km is decreased
b. The apparent Km is increased
c. Vmax is decreased
d. Apparent concentration of enzyme molecules decreased

38. Enzymes increase the rates of reaction by

a. Increasing the free energy of activation
b. Decreasing the energy of activation
c. Changing the equilibrium constant of the reaction
d. Increasing the free energy change of the reaction.

39. Enzymes synthesized in inactive form are called –

 A. Coenzymes
B. Apoenzymes
C. Lysozymes
D. Proenzymes
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PRACTICAL Topic – Analysis of normal Urine

Viva questions
1. What is the volume of normal urine output per day? Describe the term polyurea,
oliguria and anuria.
2. What are the common causes of turbidity in a fresh urine sample?
3. What is the pigment responsible for the normal colour of urine?
4. How is the specific gravity of urine measured? Name one condition where the
specific gravity of urine is high.
5. What is temperature correction while reading the urinometer?
6. Despite polyuria, specific gravity is high in diabetes mellites. why?
7. Name the condition in which large amounts of calcium are excreted in urine.
8. Name the NPN substance excreted in urine.
9. Is urobilinogen normally present in urine? Name one condition where excretion of
urobilinogen is increased.name the test to identify urobilinogen.
10. Name the conditions in which excretion of urea in urine is increased.
11. When is the excretion of creatinine increased?