ENZYMES

THE CATALYSTS OF LIFE

Introduction to Enzymology
“Every heartbeat, every thought, every muscle contraction, and every breath depends upon
enzymes.”

Life is essentially a series of chemical reactions occurring in an astonishingly coordinated manner.

Food must be broken down, DNA replicated, hormones synthesized, toxins detoxified, and energy
extracted from nutrients. Under ordinary conditions, many of these reactions would occur so
slowly that life could not be sustained.
Nature solved this problem through the evolution of enzymes.
Enzymes are the biological catalysts that make life possible. They accelerate biochemical reactions
by factors ranging from thousands to millions of times, enabling cells to perform complex tasks
efficiently and under the mild conditions of body temperature and physiological pH.
The branch of science devoted to the study of enzymes is called enzymology.

Learning Objectives
After studying this chapter, you should be able to:
• Define enzymes and related terminology.
• Explain why enzymes are necessary for life.
• Describe the structure of enzymes.
• Distinguish between apoenzymes, cofactors, coenzymes, and prosthetic groups.
• Explain enzyme specificity and catalytic mechanisms.
• Classify enzymes according to the reactions they catalyze.
• Understand enzyme kinetics and inhibition.
• Discuss the clinical importance of enzymes and isoenzymes.
• Apply enzymology principles to patient care.

What Are Enzymes?

Definition
Enzymes are biological catalysts that accelerate the rate of chemical reactions without themselves
being consumed or permanently altered.
Most enzymes are proteins possessing highly specialized three-dimensional structures. A few
enzymes are RNA molecules called ribozymes, which possess catalytic activity despite lacking
protein structure.

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Enzymes have several distinguishing characteristics:
• They markedly increase reaction rates.
• They are not consumed during reactions.
• They operate under physiological conditions.
• They are highly specific.
• Their activities are tightly regulated.

Why Are Enzymes Necessary?

Imagine attempting to digest your breakfast without enzymes.
The hydrolysis of proteins, carbohydrates, and fats would occur so slowly that the nutrients might
not become available before death from starvation.
Likewise:
• DNA replication would take years.
• ATP production would be insufficient.
• Neurotransmitter synthesis would be severely impaired.
Thus, enzymes permit life to proceed at a speed compatible with survival.

The Importance of Enzymes in Cellular Life

Enzymes participate in virtually every cellular process, including:
Metabolism: Breaking down nutrients and generating ATP.
Protein Synthesis: Formation of peptide bonds during translation.
DNA Replication and Repair: Ensuring genetic continuity.
Cell Cycle Regulation: Coordinating cell growth and division.
Hormone Production: Synthesis and release of endocrine signals.
Muscle Contraction: Generating movement.
Signal Transduction: Converting extracellular signals into intracellular responses.
Cellular Homeostasis: Maintaining the internal environment necessary for life.

Activation Energy: The Barrier to Chemical Reactions

Every chemical reaction requires an initial input of energy known as the activation energy.
Activation energy represents the energy required to convert reactants into an unstable transition
state before products can form.
Diagram in Words
Imagine a ball resting in a valley.

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To reach another valley, the ball must first roll over a hill.
• The hill represents activation energy.
• The ball represents reactants.
• The second valley represents products.
Enzymes lower the height of this hill, allowing reactions to proceed rapidly.
Importantly, enzymes:
• Lower activation energy.
• Do not alter the equilibrium position.
• Do not change the free energy (ΔG) of the reaction.

Structure of Enzymes
Most enzymes possess complex tertiary and quaternary structures essential for catalytic activity.
Enzymes may exist in two forms:
Simple Enzymes
These consist entirely of protein.
Example: Pancreatic ribonuclease.
Holoenzymes
These consist of:
Apoenzyme — The protein portion.
Cofactor — The non-protein component required for activity.
Holoenzyme = Apoenzyme + Cofactor
Without its cofactor, the apoenzyme is often catalytically inactive.

Cofactors
Cofactors are non-protein substances required for enzyme activity.
They may be:
Inorganic Metal Ions
Examples include:
• Magnesium (Mg²⁺)
• Zinc (Zn²⁺)
• Iron (Fe²⁺)
• Copper (Cu²⁺)
• Manganese (Mn²⁺)
• Calcium (Ca²⁺)
• Cobalt (Co²⁺)
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These metal ions may:
• Stabilize enzyme structure.
• Facilitate substrate binding.
• Participate in electron transfer.
• Distort substrates to facilitate catalysis.

Organic Cofactors (Coenzymes)

Coenzymes are organic molecules, frequently derived from vitamins.
Examples include:
• Vitamin B1 → Thiamine pyrophosphate (TPP)
• Vitamin B2 → FAD, FMN
• Vitamin B3 → NAD⁺, NADP⁺
• Vitamin B5 → Coenzyme A
• Vitamin B6 → Pyridoxal phosphate
• Vitamin B7 → Biotin
• Vitamin B9 → Tetrahydrofolate
• Vitamin B12 → Cobalamin

Clinical Correlation: Vitamin Deficiency

The dependence of enzymes on vitamins explains why vitamin deficiencies produce disease.
For example:
Vitamin B6 Deficiency
Impaired transamination reactions.
Clinical manifestations include:
• Peripheral neuropathy
• Seizures
• Microcytic anemia
Vitamin B12 Deficiency
Defective DNA synthesis.
Clinical manifestations include:
• Megaloblastic anemia
• Glossitis
• Neurological deficits

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The Active Site: The Catalytic Heart of the Enzyme
The active site is a specialized three-dimensional pocket where catalysis occurs.
It is formed by amino acid residues brought together through protein folding.
Functions include:
1. Recognition of substrate.
2. Formation of the enzyme-substrate complex.
3. Catalysis.
4. Release of products.
Diagram in Words
Picture a glove molded precisely for a hand.
• The glove represents the enzyme.
• The hand represents the substrate.
Only the correctly shaped substrate fits.

Enzyme Specificity
Enzymes exhibit remarkable specificity.
This ensures precision within metabolic pathways.
Absolute Specificity
One enzyme acts on one substrate.
Example: Urease acts only on urea.
Stereospecificity
The enzyme recognizes only one stereoisomer.
Example: Arginase acts on L-arginine but not D-arginine.
Bond Specificity
The enzyme recognizes specific chemical bonds.
Examples:
• Esterases → ester bonds
• Peptidases → peptide bonds
• Glycosidases → glycosidic bonds

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Mechanism of Enzyme Action
Two major theories explain enzyme-substrate interaction.
The Lock-and-Key Model
Proposed by Emil Fischer.
The active site possesses a rigid shape complementary to the substrate.
Only the correct substrate fits.
Diagram in Words: A key fits only its matching lock.
The Induced-Fit Model
Proposed by Daniel Koshland.
The active site is flexible rather than rigid.
Substrate binding induces conformational changes that optimize catalysis.
Diagram in Words: A hand slips into a glove, causing the glove to mold perfectly around it.
This model better explains enzyme behavior.

Enzyme Regulation
Cells must regulate enzyme activity to meet changing demands.
Regulation occurs through several mechanisms.
Regulation by Enzyme Quantity
Activity depends partly upon the amount of enzyme present.
Enzyme concentration is controlled by:
• Synthesis
• Degradation
Covalent Modification
Phosphorylation and dephosphorylation alter activity.
Examples include enzymes involved in glycogen metabolism.
Allosteric Regulation
Allosteric enzymes possess regulatory sites separate from active sites.
Binding of effectors alters catalytic activity.
Positive Effectors — Increase activity.
Negative Effectors — Decrease activity.

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Feedback Inhibition
Feedback inhibition is a form of allosteric regulation in which the end product of a metabolic
pathway inhibits an earlier enzyme.
Why Is This Important?
It prevents wasteful overproduction.
Diagram in Words: A factory producing shoes — once the warehouse is full, a signal stops further
production.

Proenzymes (Zymogens)
Certain enzymes are synthesized as inactive precursors.
Activation occurs by proteolytic cleavage.
Examples include:
• Pepsinogen → Pepsin
• Trypsinogen → Trypsin
• Plasminogen → Plasmin
Clinical Significance
Premature activation of pancreatic zymogens leads to autodigestion.
Acute Pancreatitis
Features include:
• Severe epigastric pain
• Nausea and vomiting
• Elevated serum amylase and lipase

Classification of Enzymes
The International Union of Biochemistry classifies enzymes into six major classes.
Mnemonic: Old Teachers Hate Learning Interesting Lessons

1. Oxidoreductases
Catalyze oxidation-reduction reactions.
Example: Lactate dehydrogenase.
2. Transferases
Transfer functional groups.
Example: AST and ALT.
3. Hydrolases
Catalyze hydrolysis reactions.

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Example: Lipases and proteases.
4. Lyases
Break bonds without hydrolysis. Often form double bonds.
5. Isomerases
Catalyze rearrangement reactions.
Example: Phosphoglucose isomerase.
6. Ligases
Join molecules using ATP.
Example: DNA ligase.

Enzyme Kinetics
Enzyme kinetics examines the factors influencing reaction rates.
These include:
• Substrate concentration
• Enzyme concentration
• Temperature
• pH
• Inhibitors
Michaelis–Menten Kinetics
As substrate concentration increases, reaction velocity initially rises rapidly.
Eventually, all active sites become occupied.
The reaction reaches maximum velocity (Vmax).
Michaelis Constant (Km)
Km is the substrate concentration required to achieve one-half of Vmax.
Low Km: High affinity.
High Km: Low affinity.
Diagram in Words
Imagine seats in a lecture hall. At first, many seats are empty and students find places easily. As
the hall fills, finding empty seats becomes difficult. Eventually, every seat is occupied — this
represents Vmax.

Enzyme Inhibition
Enzyme inhibitors reduce catalytic activity.
Many important drugs function through enzyme inhibition.
Competitive Inhibition
The inhibitor resembles the substrate. Both compete for the active site.

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Effects:
• Increased Km.
• Vmax unchanged.
Clinical Examples:
• Sulfonamides
• Methotrexate
• Ethanol treatment of methanol poisoning
Noncompetitive Inhibition
The inhibitor binds elsewhere on the enzyme. Catalytic efficiency decreases.
Effects:
• Vmax decreases.
• Km remains unchanged.
Clinical Examples:
• Lead poisoning
• Mercury toxicity
Irreversible Inhibition
Permanent enzyme inactivation. Examples include:
• Aspirin
• Organophosphates
• Penicillin

Isoenzymes
Isoenzymes are different molecular forms of an enzyme that catalyze the same reaction.
They differ in:
• Amino acid composition
• Physical properties
• Tissue distribution
Their measurement assists in identifying the site of tissue injury.
Creatine Kinase Isoenzymes
CK-BB → Brain
CK-MB → Myocardium
CK-MM → Skeletal muscle
CK-MB historically served as a marker of myocardial infarction.
Lactate Dehydrogenase Isoenzymes
LDH exists as five isoenzymes.
LDH1 predominates in:
• Myocardium

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 • Red blood cells
LDH5 predominates in:
• Liver
• Skeletal muscle
Patterns of LDH elevation may indicate tissue injury.

Clinical Enzymology
Many intracellular enzymes enter the bloodstream when cells are damaged.
Measurement of these enzymes provides valuable diagnostic information.
Commonly Measured Serum Enzymes
• ALT: Hepatocellular injury
• AST: Liver and cardiac injury
• ALP: Cholestasis and bone disease
• ACP: Prostate disease
• GGT: Alcoholic liver disease
• CK: Muscle injury
• LDH: Tissue damage
• Amylase: Acute pancreatitis

Clinical Case: Acute Hepatitis

A 36-year-old man presents with:
• Nausea
• Vomiting
• Malaise
• Dark urine
• Jaundice
Laboratory findings reveal:
• ALT: 1500 IU/L
• AST: 400 IU/L
• Elevated bilirubin
These findings strongly suggest hepatocellular injury consistent with hepatitis.
ALT elevation reflects damage to hepatocytes, permitting leakage of intracellular enzymes into
plasma.

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Chapter Summary
Enzymes are the indispensable catalysts of life.
Their structure determines their function.
Their regulation ensures metabolic balance.
Their inhibition forms the basis of numerous therapeutic interventions.
Their appearance in plasma provides powerful diagnostic clues.
To understand enzymes is to understand the language through which cells communicate, survive,
adapt, and sometimes fail. For the future physician, enzymology is not merely biochemistry—it is
the foundation of clinical medicine.

ENZYMES — 50 HIGH-YIELD MCQs WITH EXPLANATIONS

MBBS Year 1 Biochemistry (COMAHS Style) — Arranged from Easy to Difficult

EASY MCQs (1–20)

1. Enzymes are best defined as:
A. Hormones that regulate metabolism
B. Biological catalysts that increase reaction rates
C. Structural proteins
D. Energy-producing molecules
Answer: B
Explanation: Enzymes accelerate biochemical reactions without being consumed. Most are
proteins.
2. The study of enzymes is called:
A. Histology
B. Hematology
C. Enzymology
D. Immunology
Answer: C
Explanation: Enzymology is the branch of biochemistry concerned with enzyme structure and
function.
3. Most enzymes are:
A. Lipids
B. Carbohydrates
C. Proteins
D. DNA
Answer: C
Explanation: Almost all enzymes are proteins, except ribozymes.
4. Enzymes increase reaction rates by:
A. Increasing ΔG

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 B. Increasing equilibrium constant
C. Lowering activation energy
D. Increasing substrate concentration
Answer: C
Explanation: Enzymes reduce the activation energy barrier.
5. The region of the enzyme where substrate binds is called:
A. Cofactor
B. Active site
C. Apoenzyme
D. Prosthetic group
Answer: B
Explanation: The active site binds substrate and catalyzes reactions.
6. The protein portion of a holoenzyme is:
A. Coenzyme
B. Prosthetic group
C. Apoenzyme
D. Activator
Answer: C
7. A holoenzyme consists of:
A. Protein only
B. Cofactor only
C. Apoenzyme + Cofactor
D. Substrate + Product
Answer: C
8. Which of the following is an organic cofactor?
A. Mg²⁺
B. Zn²⁺
C. NAD⁺
D. Ca²⁺
Answer: C
9. Enzymes are usually:
A. Consumed during reactions
B. Permanently altered
C. Recycled after reactions
D. Destroyed after catalysis
Answer: C
10. Which vitamin forms NAD⁺?
A. Vitamin B1
B. Vitamin B2
C. Vitamin B3
D. Vitamin B12
Answer: C
Explanation: Niacin (Vitamin B3) forms NAD⁺ and NADP⁺.

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11. Urease acting only on urea demonstrates:
A. Bond specificity
B. Absolute specificity
C. Stereospecificity
D. Feedback inhibition
Answer: B
12. Arginase acting on L-arginine but not D-arginine demonstrates:
A. Absolute specificity
B. Bond specificity
C. Stereospecificity
D. Allosteric regulation
Answer: C
13. Esterases act on:
A. Peptide bonds
B. Glycosidic bonds
C. Ester bonds
D. Phosphodiester bonds
Answer: C
14. Which enzyme class catalyzes hydrolysis?
A. Transferases
B. Hydrolases
C. Lyases
D. Ligases
Answer: B
15. Which class transfers functional groups?
A. Oxidoreductases
B. Transferases
C. Isomerases
D. Hydrolases
Answer: B
16. DNA ligase belongs to:
A. Hydrolases
B. Ligases
C. Lyases
D. Isomerases
Answer: B
17. Which model proposes that enzymes change shape during catalysis?
A. Lock-and-key
B. Fischer model
C. Induced-fit
D. Collision theory
Answer: C
18. The lock-and-key theory was proposed by:

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 A. Michaelis
B. Koshland
C. Fischer
D. Lineweaver
Answer: C
19. Enzymes function best under:
A. Extreme temperatures
B. Physiological conditions
C. Boiling temperatures
D. Strong acids
Answer: B
20. Which statement is FALSE?
A. Enzymes lower activation energy.
B. Enzymes change equilibrium.
C. Enzymes are catalysts.
D. Enzymes are specific.
Answer: B

MODERATE MCQs (21–40)

21. Km represents:
A. Maximum velocity
B. Half-life
C. Substrate concentration at ½ Vmax
D. Enzyme concentration
Answer: C
22. A low Km indicates:
A. Low affinity
B. High affinity
C. Low Vmax
D. High inhibition
Answer: B
23. Vmax is reached when:
A. No substrate is present
B. All enzyme active sites are saturated
C. Inhibitors are added
D. pH decreases
Answer: B
24. Competitive inhibitors:
A. Decrease Vmax
B. Increase Km
C. Decrease Km
D. Increase Vmax
Answer: B

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25. In competitive inhibition:
A. Vmax decreases
B. Km decreases
C. Vmax unchanged
D. Enzyme destroyed
Answer: C
26. Noncompetitive inhibitors cause:
A. Increased Vmax
B. Decreased Km
C. Decreased Vmax
D. Increased affinity
Answer: C
27. Heavy metals usually act as:
A. Competitive inhibitors
B. Noncompetitive inhibitors
C. Activators
D. Coenzymes
Answer: B
28. Sulfonamides are examples of:
A. Irreversible inhibitors
B. Noncompetitive inhibitors
C. Competitive inhibitors
D. Activators
Answer: C
29. End-product inhibition is called:
A. Covalent modification
B. Allosteric activation
C. Feedback inhibition
D. Cooperativity
Answer: C
30. Positive effectors:
A. Inhibit catalysis
B. Increase catalytic activity
C. Destroy enzymes
D. Denature proteins
Answer: B
31. Pepsinogen is converted into:
A. Trypsin
B. Chymotrypsin
C. Pepsin
D. Plasmin
Answer: C
32. Trypsinogen is a:

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 A. Coenzyme
B. Zymogen
C. Inhibitor
D. Isoenzyme
Answer: B
33. Premature activation of pancreatic enzymes causes:
A. Hepatitis
B. Pancreatitis
C. Cirrhosis
D. Gastritis
Answer: B
34. Pyridoxal phosphate is derived from:
A. Vitamin B12
B. Vitamin B6
C. Vitamin B2
D. Vitamin C
Answer: B
35. Tetrahydrofolate is derived from:
A. Folic acid
B. Niacin
C. Riboflavin
D. Biotin
Answer: A
36. Vitamin B12 deficiency causes:
A. Hemolytic anemia
B. Megaloblastic anemia
C. Iron deficiency anemia
D. Aplastic anemia
Answer: B
37. Biotin functions mainly in:
A. Carboxylation reactions
B. Oxidation
C. Hydrolysis
D. Isomerization
Answer: A
38. Coenzyme A is derived from:
A. Vitamin B6
B. Vitamin B5
C. Vitamin B1
D. Vitamin B2
Answer: B
39. Metal ions may assist enzymes by:
A. Electron transfer

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 B. Stabilizing structure
C. Substrate binding
D. All of the above
Answer: D
40. Which enzyme class catalyzes redox reactions?
A. Transferases
B. Ligases
C. Oxidoreductases
D. Lyases
Answer: C

DIFFICULT MCQs (41–50)

41. CK-MB is elevated in:
A. Hepatitis
B. Myocardial infarction
C. Pancreatitis
D. Prostate cancer
Answer: B
42. CK-BB is predominantly found in:
A. Liver
B. Heart
C. Brain
D. Kidney
Answer: C
43. LDH1 is mainly found in:
A. Liver
B. Skeletal muscle
C. Myocardium
D. Pancreas
Answer: C
44. Elevated LDH5 suggests:
A. Acute MI
B. Liver disease
C. Brain disease
D. Leukemia
Answer: B
45. The most liver-specific enzyme is:
A. AST
B. ALT
C. CK
D. LDH
Answer: B
46. Elevated ALP is characteristic of:

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 A. Acute pancreatitis
B. Biliary obstruction
C. Myocardial infarction
D. CNS disease
Answer: B
47. GGT is particularly useful in diagnosing:
A. Bone metastases
B. Alcohol-induced liver disease
C. Acute leukemia
D. Prostate cancer
Answer: B
48. Amylase is elevated in:
A. Hepatitis
B. Pancreatitis
C. MI
D. Cirrhosis
Answer: B
49. AST catalyzes transfer of amino groups using which coenzyme?
A. FAD
B. NAD⁺
C. Pyridoxal phosphate
D. CoA
Answer: C
50. A patient with jaundice has ALT 1500 IU/L and AST 400 IU/L. The most likely diagnosis is:
A. Acute pancreatitis
B. Acute hepatitis
C. Myocardial infarction
D. Prostate carcinoma
Answer: B
Explanation: Massive ALT elevation indicates hepatocellular injury, especially viral hepatitis.

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Enzyme MCQ Score Guide
• 45–50: Distinction (Genius level)
• 40–44: Excellent MBBS standard
• 35–39: Very Good
• 30–34: Pass
• Below 30: Requires revision of enzymology fundamentals

ENZYMES — PART 2
20 Short Answer Questions (SAQs) with Model Answers
MBBS Year 1 Biochemistry (COMAHS Style) — Arranged from Easy to Difficult

Easy SAQs (1–7)

SAQ 1. Define an enzyme.
Enzymes are biological catalysts, mostly proteins, that increase the rate of biochemical
reactions without being consumed or permanently altered in the process.
SAQ 2. List four properties of enzymes.
– They are biological catalysts.
– They lower activation energy.
– They are highly specific.
– They are not consumed during reactions.
– They function under physiological conditions.
SAQ 3. Differentiate between apoenzyme and holoenzyme.
Apoenzyme — protein portion only, inactive alone, requires cofactor vs. Holoenzyme:
complete active enzyme, catalytically active, = apoenzyme + cofactor
SAQ 4. What is an active site?
The active site is the three-dimensional region of an enzyme where the substrate binds and
catalysis occurs.
Functions: Binds substrate, catalyzes reaction, releases product.
SAQ 5. Define activation energy.
Activation energy is the minimum energy required to convert reactants into the transition
state before products can form. Enzymes lower activation energy and increase reaction rates.
SAQ 6. Mention three functions of enzymes.
Enzymes participate in:
– Digestion of food
– ATP production
– DNA replication
– Hormone synthesis
– Muscle contraction
SAQ 7. Define specificity and list its types.

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 Specificity refers to the ability of enzymes to act only on particular substrates.
Types: Absolute specificity, stereospecificity, bond specificity.

Moderate SAQs (8–14)

SAQ 8. What are cofactors? Classify them with examples.
Cofactors are non-protein substances required for enzyme activity.
1. Metal ions: Mg²⁺, Zn²⁺, Fe²⁺
2. Coenzymes: NAD⁺, FAD, Coenzyme A
SAQ 9. Define coenzymes and give four examples.
Coenzymes are organic cofactors, usually derived from vitamins.
Examples: NAD⁺, FAD, Pyridoxal phosphate, Tetrahydrofolate
SAQ 10. Classify enzymes according to IUBMB.
The six major classes are: Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases,
Ligases.
Mnemonic: Old Teachers Hate Learning Interesting Lessons
SAQ 11. Differentiate between lock-and-key and induced-fit theories.
Origin — Lock-and-Key: proposed by Fischer, active site rigid, exact fit (older concept) vs.
Induced-Fit: proposed by Koshland, active site flexible, shape changes occur (more accepted
model)
SAQ 12. What are zymogens? Give examples.
Zymogens are inactive enzyme precursors activated by proteolytic cleavage.
Examples: Pepsinogen → Pepsin; Trypsinogen → Trypsin; Plasminogen → Plasmin
Importance: Prevents autodigestion.
SAQ 13. Define allosteric regulation.
Allosteric regulation is the modification of enzyme activity by binding of regulatory molecules
at sites other than the active site.
Effectors may be: Positive activators or negative inhibitors.
SAQ 14. Explain feedback inhibition.
Feedback inhibition is a type of allosteric regulation in which the end product of a metabolic
pathway inhibits an earlier enzyme in that pathway.
Importance: Prevents overproduction and conserves energy.

Difficult SAQs (15–20)

SAQ 15. Define Km and state its significance.
Km is the substrate concentration required to achieve half of Vmax.
Significance: Indicates enzyme affinity. Low Km = high affinity. High Km = low affinity.
SAQ 16. Define Vmax.
Vmax is the maximum reaction velocity attained when all enzyme active sites are saturated
with substrate.
Importance: Reflects enzyme catalytic capacity.
SAQ 17. Differentiate between competitive and noncompetitive inhibition.
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 Binding site — Competitive: active site vs. Noncompetitive: allosteric site
Vmax — Competitive: unchanged vs. Noncompetitive: decreased
Km — Competitive: increased vs. Noncompetitive: unchanged
Overcome by substrate — Competitive: yes vs. Noncompetitive: no
Example — Competitive: sulfonamides vs. Noncompetitive: lead
SAQ 18. What are isoenzymes?
Isoenzymes are different molecular forms of the same enzyme that catalyze identical reactions
but differ in structure, physical properties, and tissue distribution.
Clinical importance: Helps identify tissue damage (e.g. CK isoenzymes, LDH isoenzymes).
SAQ 19. Write the CK isoenzymes and their clinical importance.
CK-BB: Brain — indicates CNS disease
CK-MB: Heart — indicates myocardial infarction
CK-MM: Skeletal muscle — indicates muscular disorders
SAQ 20. Enumerate the important diagnostic enzymes and their clinical uses.
ALT: Hepatitis
AST: Liver disease / MI
ALP: Obstructive jaundice, bone disease
GGT: Alcoholic liver disease
ACP: Prostate disease
CK: Muscle injury
LDH: Tissue damage
Amylase: Acute pancreatitis

PART 3
10 Viva Questions and Answers (Examiner Style)
Viva 1
Examiner: What is an enzyme?
Candidate: An enzyme is a biological catalyst that accelerates biochemical reactions without being
consumed.
Viva 2
Examiner: What is the difference between apoenzyme and holoenzyme?
Candidate: Apoenzyme is the inactive protein part of an enzyme, whereas holoenzyme is the
active enzyme consisting of apoenzyme plus cofactor.
Viva 3
Examiner: Why are enzymes highly specific?
Candidate: Because their active sites have a three-dimensional structure complementary to
particular substrates.
Viva 4
Examiner: State the six classes of enzymes.
Candidate: Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases, and Ligases.
Viva 5

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Examiner: What is Km?
Candidate: Km is the substrate concentration required to achieve half of Vmax and reflects
enzyme affinity for substrate.
Viva 6
Examiner: What happens to Km and Vmax in competitive inhibition?
Candidate: Km increases while Vmax remains unchanged.
Viva 7
Examiner: Give examples of zymogens.
Candidate: Pepsinogen, trypsinogen, and plasminogen.
Viva 8
Examiner: What is the coenzyme required by AST and ALT?
Candidate: Pyridoxal phosphate, the active form of Vitamin B6.
Viva 9
Examiner: What is CK-MB used for?
Candidate: It is a marker of myocardial infarction.
Viva 10
Examiner: Why is ALT more liver-specific than AST?
Candidate: Because AST is also found in cardiac and skeletal muscle, whereas ALT is
predominantly located in hepatocytes.

PART 4
10 Clinical Case Scenarios (Easy to Difficult)
Case 1 (Easy)
A child develops bloating and diarrhea after drinking milk.
Diagnosis: Lactose intolerance
Deficient enzyme: Lactase
Case 2
A patient presents with severe epigastric pain radiating to the back. Serum amylase is markedly
elevated.
Diagnosis: Acute pancreatitis
Additional marker: Serum lipase
Case 3
A patient has chest pain for 6 hours. CK-MB is elevated.
Diagnosis: Acute myocardial infarction
Tissue involved: Myocardium
Case 4
A patient presents with jaundice and dark urine. ALT = 1500 IU/L. AST = 400 IU/L.
Diagnosis: Acute hepatitis
Explanation: Marked ALT elevation indicates hepatocellular injury

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Case 5
A chronic alcoholic has elevated GGT.
Diagnosis: Alcohol-induced liver disease
Significance: GGT is induced by alcohol
Case 6
A patient has jaundice with markedly elevated ALP and GGT.
Diagnosis: Obstructive jaundice
Explanation: ALP elevation with GGT confirms hepatobiliary origin
Case 7
A patient with bone pain has elevated ALP.
Possible diagnoses: Rickets, osteomalacia, bone metastases, healing fracture
Source of ALP: Osteoblasts
Case 8
A patient presents with anemia and neuropathy. Laboratory tests reveal Vitamin B12 deficiency.
Biochemical consequence: Impaired DNA synthesis
Diagnosis: Megaloblastic anemia
Case 9
A farmer exposed to pesticides develops excessive salivation, sweating, and muscle fasciculations.
Diagnosis: Organophosphate poisoning
Mechanism: Irreversible inhibition of acetylcholinesterase
Treatment: Atropine, Pralidoxime
Case 10 (Difficult)
A patient ingests antifreeze (ethylene glycol).
Enzyme that metabolizes it: Alcohol dehydrogenase
Toxic product formed: Oxalic acid
Treatment: Fomepizole (4-methylpyrazole) or ethanol
Discussion: Blocking alcohol dehydrogenase prevents formation of toxic metabolites and protects
the kidneys

Complied by Abdul Kitto Page 23 of 23