IB Biology HL C1.1 Enzymes and metabolism Questions

Practise IB Biology HL C1.1 by explaining enzyme specificity, metabolic reactions, rate evidence, inhibition and feedback control in biological pathways.

162 questions in this syllabus scope, with question parts counted together.

Syllabus
First assessment 2025
Course
Biology HL
Level
HL

Exam analysis

HL · 2010–2025
Papers with this topic67 / 117in the analysed sample
Latest appearanceNovember 2025
Tagged question parts112
Paper types5

Most tested objectives

  1. C1.1.8—Effects on enzyme activity19 papers
  2. C1.1.15 (HL)—Competitive inhibition19 papers
  3. C1.1.9—Measuring enzyme reactions14 papers
  4. C1.1.16 (HL)—Feedback inhibition10 papers
  5. C1.1.10—Effect of enzymes on activation energy7 papers

Common question formats

  • Calculation
  • Data analysis
  • Definition or recall
  • Diagram interpretation
  • Experimental design
  • Extended response
  • Graph interpretation
  • Structured response

Recent exam appearances

November 2025Paper 2 HL · TZ3Q9(b)[ 7 ]
November 2025Paper 2 HL · TZ1Q1(f), 1(g), 8(a)[ 8 ]
November 2025Paper 1A HL · TZ3Q6[ 1 ]

117 papers analysed · Tagging incomplete

Exam points

  • Explain enzyme catalysis through activation-energy reduction and relate active-site specificity to substrate binding and induced fit.
  • Interpret metabolic pathways and classify enzyme-controlled reactions, including condensation, hydrolysis and oxidation, as anabolic or catabolic.
  • Explain how tertiary-structure and active-site changes affect enzyme binding and activity.
  • Interpret enzyme-rate graphs and data for temperature, pH, substrate concentration, optima and saturation; evaluate assay reliability.
  • Interpret enzyme energy profiles to identify reduced activation energy without a change in reactant or product energy.
  • Distinguish intracellular and extracellular enzymes using digestive-enzyme examples and pepsinogen activation.
  • Relate basal metabolic rate and heat production to climate, body mass and surface-area-to-volume ratio.
  • Distinguish linear from cyclical metabolic pathways by whether an intermediate is regenerated.
  • Compare competitive and non-competitive inhibition using binding site and substrate-response evidence.
  • Explain feedback inhibition by end-product binding to an earlier pathway enzyme, including isoleucine synthesis.

Exam points

  • Define enzymes as biological catalysts; most are proteins, although some RNA molecules are catalytic.
  • Explain that enzymes act in small amounts and remain unchanged after catalysis.

Question 1

[Maximum number: 4]

Outline the action of enzymes.

Exam points

  • Define metabolism as the complete set of enzyme-controlled chemical reactions in cells.
  • Explain that specific enzymes determine which metabolic reactions occur and when.

Question 1

[Maximum number: 1]

Metabolic pathways are dependent on enzyme-catalysed reactions. Which term corresponds with the description?

Term

Description

allosteric inhibition

the inhibitor binds to the active site of an enzyme

competitive inhibition

the maximum rate of a reaction is lowered as the substrate concentration increases

non-competitive inhibition

raises the maximum rate of reaction of a given enzyme reaction

end-product inhibition

the end-product in a metabolic pathway binds to an allosteric site of the first enzyme

Exam points

  • Explain how anabolism builds complex molecules by condensation and requires energy.
  • Explain how catabolism breaks molecules by hydrolysis or oxidation and releases energy.

Question 1

[Maximum number: 1]

Cell metabolism involves anabolic and catabolic reactions. Which process directly involves anabolism?

A

Active transport of ions

B

Release of energy from glucose

C

Production of intracellular enzymes

D

Breakdown of worn-out cell organelles by lysosomes

Exam points

  • Describe enzymes as usually globular proteins with a small active-site pocket that binds a substrate.
  • Explain that binding forms an enzyme–substrate complex and allows the reaction to be catalysed.

Question 1

[Maximum number: 1]

Define the active site of an enzyme.

Exam points

  • Explain that substrate binding induces shape changes in both the enzyme and substrate.
  • Explain how induced fit aligns catalytic groups and raises the substrate towards the transition state.

Question 1

[Maximum number: 6]

(a) Draw a labelled diagram to show the molecular structure of a membrane.

Some proteins in membranes act as enzymes. Describe a model that accounts for the ability of enzymes to catalyse reactions.

Exam points

  • Explain how active-site amino acid arrangement determines substrate specificity.
  • Explain how denaturation changes tertiary structure and active-site shape without breaking peptide bonds.

Question 1

[Maximum number: 1]

The image shows leucyl-tRNA synthetase from Thermus thermophilus complexed with a tRNA. This tRNA-activating enzyme joins the amino acid leucine to tRNA using ATP.

Figure for Question 1 — IB Biology HL

Why is leucyl-tRNA synthetase not used to join the amino acid valine to tRNA?

A

Phosphorylation of valine occurs at a later stage.

B

Valine does not need to be activated to attach to tRNA.

C

Leucyl-tRNA synthetase is substrate-specific.

D

Valine has a different anticodon from leucine.

Exam points

  • Explain how increasing temperature raises enzyme activity to an optimum, after which denaturation lowers the rate.
  • Explain how pH changes alter bonding at the enzyme active site and affect enzyme activity.
  • Interpret substrate-concentration data to explain the rise in enzyme activity to a saturation plateau.

Question 1

[Maximum number: 1]

A solution of laundry detergent containing enzymes was used to soak some blood-stained clothes in order to remove the stains. Each item of stained clothing was soaked in a solution of a different temperature. After one hour, the stains remaining on the clothes were measured on a colour intensity scale.

Table for Question 1 — IB Biology HL
Figure for Question 1 — IB Biology HL
Table for Question 1 — IB Biology HL

What is a valid explanation for these results?

A

At 10∘C10^{\circ} \mathrm{C} the enzymes denature.

B

At 20∘C20^{\circ} \mathrm{C} the shape of some enzyme active sites change.

C

At 30∘C30^{\circ} \mathrm{C} the enzyme and substrate molecules have the greatest kinetic energy.

D

At 50∘C50^{\circ} \mathrm{C} the chance of successful binding between enzyme and substrate is low.

Exam points

  • Measure enzyme activity as substrate loss or product formation per unit time.
  • Use an initial rate from amylase or catalase assay graphs to compare enzyme activity.
  • Use replicates and controlled variables when measuring enzyme reactions to assess result reliability.

Question 1

[Maximum number: 3]

The inhibitory effect of three different statins ( S1, S2 and S3 ) on the activity of HMG-CoA reductase, an enzyme involved in cholesterol metabolism in the liver, was investigated.

Figure for Question 1 — IB Biology HL

Question (a)

(a)

Identify an independent variable in this investigation.

[ 1 ]

Question (b)

(b)

State one variable that needs to be controlled.

[ 1 ]

Question (c)

(c)

Outline how the rate of reaction of HMG-CoA reductase can be calculated.

[ 1 ]

Exam points

  • Explain that enzymes lower activation energy by providing an alternative reaction pathway.
  • Explain how enzyme binding stabilises the transition state, lowering activation energy and increasing reaction rate.

Question 1

[Maximum number: 1]

The graph shows the energy changes during a chemical reaction. The horizontal lines represent the original energy values.

Figure for Question 1 — IB Biology HL

Which graph represents the energy changes once a suitable enzyme has been added?

A
Figure for Question 1 — IB Biology HL — Option A
B
Figure for Question 1 — IB Biology HL — Option B
C
Figure for Question 1 — IB Biology HL — Option C
D
Figure for Question 1 — IB Biology HL — Option D

Exam points

  • Distinguish intracellular enzymes acting in cytoplasm, organelles or membranes from extracellular enzymes secreted to act outside cells.
  • Identify pancreatic digestive enzymes and explain pepsinogen secretion followed by activation in the stomach as extracellular examples.

Question 1

[Maximum number: 1]

What is secreted by the pancreas for digestion in the small intestine?

A

Lipase to break bond between phosphate and fatty acid

B

Insulin to digest glycogen to glucose

C

Amylopectin to digest starch to maltose

D

Endopeptidase to digest proteins to peptides

Exam points

  • Explain that exergonic metabolic reactions inevitably release some energy as heat.
  • Explain how endotherms use metabolic heat to maintain body temperature.

Question 1

[Maximum number: 4]

Common bottlenose dolphins, Tursiops truncatus, are marine mammals of temperate and tropical oceans throughout the world, where they feed on fish, squid and crustaceans.

Research has been carried out on a population of these dolphins in Sarasota Bay, Florida. The table shows the mean sea surface temperature in Sarasota Bay and catch per unit effort (CPUE) in winter and summer. A large CPUE indicates it would take little effort for the dolphin to catch a lot of prey.

Table for Question 1 — IB Biology HL

Question (a)

(a)

Explain the differences in BMR between desert and polar mammals up to a mass of 103 g10^{3} \mathrm{~g}.

[ 2 ]

Question (b)

(b)

Above a body mass of 10 kg , there is little difference in BMR between desert and polar mammals.

Suggest reasons for this.

[ 2 ]

Exam points

  • Distinguish linear pathways that run from substrate to product from cyclical pathways that regenerate an acceptor or initial molecule.
  • Classify pathway descriptions such as glycolysis, Krebs cycle and Calvin cycle by whether intermediates are recycled or lead to an end product.

Question 1

[Maximum number: 1]

The reaction that produces urea in liver cells is shown.

Figure for Question 1 — IB Biology HL

This reaction forms part of a metabolic cycle. Outline one feature of a metabolic cycle that distinguishes it from a chain.

Exam points

  • Define an allosteric site as a site separate from the active site and locate non-competitive inhibitor binding there.
  • Explain that non-competitive binding changes enzyme shape, reduces active-site function and lowers activity despite substrate presence.
  • Distinguish non-competitive from competitive inhibition using binding site and substrate-response evidence.

Question 1

[Maximum number: 4]

Chemicals are involved at all levels of biology: cell functions, structure of organisms, interactions with the environment.

Distinguish between competitive and non-competitive enzyme inhibition.

Exam points

  • Explain that a competitive inhibitor resembles the substrate and binds reversibly to the enzyme active site, preventing substrate binding.
  • Interpret rate-versus-substrate evidence to identify competitive inhibition and explain why increasing substrate concentration reduces its effect.
  • Distinguish competitive from non-competitive inhibition using binding location, reversibility and substrate-response evidence.

Question 1

[Maximum number: 1]

The graph illustrates how enzyme-catalysed reactions can be affected by inhibitors. Which curve shows the effect of statins on the rate of cholesterol synthesis in the body?

Figure for Question 1 — IB Biology HL

Exam points

  • Explain that an accumulated end product inhibits an earlier enzyme in its metabolic pathway through feedback inhibition.
  • Identify end-product binding at an allosteric site and relate product concentration to slowing or stopping pathway output.
  • Apply feedback inhibition to pathway examples such as isoleucine synthesis, including the regulated first step.

Question 1

[Maximum number: 1]

The production of isoleucine from threonine is summarized in the diagram. This process involves several steps and is regulated by feedback inhibition.

Figure for Question 1 — IB Biology HL

What occurs during isoleucine production?

A

Isoleucine inhibits the conversion of intermediate W to intermediate X .

B

Isoleucine inhibits the conversion of intermediate Y to intermediate Z .

C

Threonine inhibits threonine deaminase activity.

D

Isoleucine inhibits threonine deaminase activity.

No public sample questions are available for this syllabus point yet.