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FSC Biology: Enzymes, questions with answers

Practise 16 real Federal Board questions on Enzymes from 2023 to 2026. See the answer and explanation as soon as you answer.

16real questions
4multiple choice
5exam sessions

About Enzymes in FSC Biology

Enzymes is one of the 15 main chapters in our Federal Board FSC Biology question bank (11th class), and about 3% of its real questions come from it. Tayyari Karo has 16 real questions on this chapter from 2023 to 2026; 4 are multiple choice and marked instantly, and the rest are short and long questions with a model answer. By difficulty: 15 medium, 1 easy.

Work through the questions below, then open the explanation for each one. Redo the ones you missed a few days later.

Try 8 real questions

These are real past-paper questions. Think of your answer first, then open the explanation.

2026 Annual · 11th · Enzymes

The minimum energy required to start a chemical reaction is called:

  1. Potential energy
  2. Activation energy
  3. Kinetic energy
  4. Heat energy
Show answer and explanation

Answer: B. Activation energy

Activation energy is the energy barrier that must be overcome for reactant molecules to be converted into products; enzymes work by lowering this barrier.

2025 1st Annual · 11th · Enzymes

The compound malonate is a competitive inhibitor of:

  1. Fumarate
  2. Succinate
  3. Succinic dehydrogenase
  4. Histidine decarboxylase
Show answer and explanation

Answer: C. Succinic dehydrogenase

Malonate closely resembles succinate in shape and competitively binds the active site of succinate dehydrogenase, blocking the Krebs-cycle conversion of succinate to fumarate.

2025 2nd Annual · 11th · Enzymes

Which model explains enzyme action by showing a change in the active site to fit the substrate?

  1. Lock and Key Model
  2. Induced Fit Model
  3. Michaelis-Menten Model
  4. Transition State Model
Show answer and explanation

Answer: B. Induced Fit Model

The induced fit model proposes the active site is flexible and changes shape as the substrate binds, improving the fit; the lock-and-key model assumes a rigid, pre-fitting active site.

2023 Annual · 11th · Enzymes

They catalyze the breakdown of specific covalent bonds and removal of groups without hydrolysis:

  1. Lyases
  2. Ligases
  3. Transferases
  4. Hydrolases
Show answer and explanation

Answer: A. Lyases

Lyases break bonds (e.g. C–C, C–O) and remove groups non-hydrolytically, often forming a double bond or ring.

2026 Annual · 11th · Enzymes

Classify enzymes on the basis of the substrates they act upon, giving any three examples.

Show model answer

(1) Carbohydrases — act on carbohydrate substrates, e.g. amylase (breaks down starch).
(2) Proteases — act on protein substrates, e.g. pepsin (breaks down proteins in the stomach).
(3) Lipases — act on lipid substrates, e.g. lipase (breaks down fats into fatty acids and glycerol).

2025 1st Annual · 11th · Enzymes

Compare the characteristics of cofactors of enzymes with one example of each.

Show model answer

TypeCharacteristicExampleInorganic cofactorA metal ion required for enzyme activity/stabilising its structureZn²⁺ (in carbonic anhydrase)CoenzymeAn organic, loosely-bound cofactor, often derived from a vitamin, that carries chemical groups between reactionsNAD⁺ (in dehydrogenases)Prosthetic groupAn organic cofactor tightly/permanently bound to the enzymeHeme group (in catalase)

2025 2nd Annual · 11th · Enzymes

What are the three types of cofactors? Give one example of each.

Show model answer

(1) Inorganic ion (metal) cofactor — a metal ion needed for activity, e.g. Zn²⁺ in carbonic anhydrase.
(2) Coenzyme — a loosely-bound organic molecule (often vitamin-derived) that carries chemical groups between reactions, e.g. NAD⁺.
(3) Prosthetic group — an organic cofactor tightly/permanently bound to the enzyme, e.g. the heme group in catalase.

2025 2nd Annual · 11th · Enzymes

Briefly explain importance of competitive inhibitors.

Show model answer

Competitive inhibitors are molecules structurally similar to the normal substrate that compete with it for binding to the enzyme's active site, reducing reaction rate (an effect that can be overcome by increasing substrate concentration). Their importance: (1) they help regulate metabolic pathways (e.g. end-product/feedback inhibition controlling flux through a pathway); (2) they are exploited in drug design — many medicines (e.g. some antibiotics, statins) work as competitive inhibitors of specific target enzymes; (3) studying them helps researchers understand enzyme active-site structure and specificity.

Sessions with Enzymes questions

SessionQuestions
2026 Annual3
2025 1st Annual4
2025 2nd Annual4
2024 Annual3
2023 Annual2

Common questions

What does the Enzymes chapter cover on this page?

16 real Federal Board (FBISE) Biology questions on Enzymes from 2023 to 2026, for 11th class. Each one shows the session it came from.

Are the answers official?

No. We could not find an official FBISE marking scheme for these papers, so the answers and explanations are written by Tayyari Karo for practice. Check anything important with your teacher or textbook.

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