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1.4.1Biological Molecules

Many Proteins are Enzymes — AQA A Level Biology 7402 Revision Notes & Topical Questions

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1.4.1 Many Proteins are Enzymes — AQA A Level Biology 7402 notes: Define enzymes as biological catalysts, explain how they lower activation energy, and compare the lock-and-key and induced-fit models.An enzyme is a globular protein that acts as a biological catalyst: it speeds up…

  • intracellularly
  • extracellularly
  • active site
  • enzyme-substrate complex
  • Exam-style question 1
  • Exam-style question 2

Section 1 of 9Enzymes as biological catalysts

An enzyme is a globular protein that acts as a biological catalyst: it speeds up a metabolic reaction without being used up.

Without enzymes, reactions in cells at 37 °C would be too slow to sustain life.
Each enzyme catalyses one reaction or a group of similar reactions.
Intracellularly
They can work intracellularly (inside cells, for example catalase breaking down hydrogen peroxide in peroxisomes) or extracellularly (secreted outside cells, for example amylase and trypsin in digestion).

Section 2 of 9Activation energy

Reacting molecules must collide with enough energy to break existing bonds; this minimum energy is the activation energy.

Activation energy
Heating provides it in a test tube, but would damage cells.
Enzymes lower the activation energy by providing an alternative pathway, so more collisions are successful at body temperature.
They do not change the overall energy released or taken in, the position of equilibrium,
  • or the products formed, only the rate at which equilibrium is reached.

Enzymes lower activation energy in several ways: bringing substrates close together in the right orientation, straining bonds in the substrate, and providing a micro-environment (charge or pH) in the active site that favours the reaction.

Section 3 of 9The active site

The active site is a small region, usually a cleft or pocket, on the surface of the enzyme formed by the folding of the polypeptide (tertiary structure).

Substrate
A few R groups in the active site have specific charges and shapes, and bind the substrate, the molecule on which the enzyme acts.
Enzyme-substrate complex
The substrate and active site form a temporary enzyme-substrate complex, the reaction occurs, and the products leave,
  • so the enzyme is free to be reused.
The model is enzyme + substrate → enzyme-substrate complex → enzyme-product complex → enzyme + products.

Section 4 of 9Models of enzyme action

FeatureLock-and-keyInduced fit
Active site shapeFixed, exactly complementary to substrateNot exactly complementary at first; moulds around the substrate
ExplainsSpecificitySpecificity and how bonds are strained to lower activation energy
EvidenceEarly experimentsBetter fits modern data, e.g. enzymes that act on several related substrates

The induced-fit model is now preferred. The substrate causes small changes in the shape of the active site, so the R groups fit around it more tightly and put strain on the substrate bonds. After the products leave, the active site returns to its original shape.

Section 5 of 9Types and examples

Types and examples
Catabolic
Catabolic enzymes break molecules down by hydrolysis (amylase, lipase, proteases).
Anabolic
Anabolic enzymes build molecules by condensation (DNA polymerase, ATP synthase).
Catalase
Catalase splits toxic hydrogen peroxide into water and oxygen, and is used in practical work.

Because the active site depends on the tertiary structure, anything that damages that structure (heat, extreme pH) alters the enzyme's activity. Link forward to the lessons on temperature, pH, concentration and inhibitors.

Section 6 of 9Enzymes in context

Enzymes control the rate of nearly every reaction in a cell, so living organisms can regulate metabolism by controlling them.

Enzymes in context
A metabolic pathway is a chain of reactions, each catalysed by a different enzyme, so one product becomes the substrate for the next.
Because enzymes are made from genes, changes in gene expression change which reactions are active in a cell.
Some enzymes are made as inactive precursors, such as pepsinogen and trypsinogen,
  • which are activated only where they are needed; this prevents the enzymes digesting the cells that make them.

Enzymes have many uses in industry.

Enzymes in context
Amylase converts starch to sugar syrup, proteases and lipases in biological detergents break down protein and fat stains, lactase removes lactose from milk for people with lactose intolerance,
  • and immobilised enzymes in alginate beads can be reused and separated easily from the product.
These applications use the same ideas of specificity and optimum conditions that you meet in practical work.

For the exam, an effective definition of an enzyme includes three ideas: it is a protein, it is a catalyst, and it works by lowering activation energy. Naming the enzyme-substrate complex shows you understand the mechanism, and mentioning that the enzyme is unchanged at the end shows you understand catalysis.

Section 7 of 9Exam-style questions

  1. Explain how an enzyme speeds up a reaction. [3]3 marks

  2. Describe the induced-fit model and explain why it is preferred to lock and key. [3]3 marks

  3. The enzyme catalase was added to hydrogen peroxide and 12 cm3 of oxygen was collected in 30 seconds. Calculate the mean rate and state what would happen to the final volume of oxygen if the enzyme concentration were doubled. [2]2 marks

Section 8 of 9Key terms

TermMeaning
EnzymeA protein that acts as a biological catalyst.
SubstrateThe molecule that an enzyme acts upon.
Active siteThe region of the enzyme where the substrate binds.
Activation energyThe minimum energy needed for a reaction to occur.
Enzyme-substrate complexThe temporary structure formed when substrate binds to the active site.
Induced-fit modelModel where the active site changes shape to fit the substrate.
Intracellular enzymeAn enzyme that works inside the cell.
Extracellular enzymeAn enzyme secreted to work outside the cell.

Section 9 of 9Exam technique

1
Saying that enzymes provide energy for reactions. They lower the activation energy.
2
Writing that the enzyme is used up or changed by the reaction.
3
Stating that the substrate has to be exactly the same shape as the active site in the induced-fit model.
4
Describing the active site as the whole enzyme.

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