Enzymes & Metabolism (AQA GCSE Biology): Revision Note

Exam code: 8461

Enzymes & metabolism

  • Enzymes are biological catalysts made from protein that speed up chemical reactions in cells without being used up

  • Without enzymes the metabolic reactions that occur at body temperature would take place too slowly

    • Examples of essential metabolic reactions that are controlled by enzymes include:

      • breaking down carbohydrates, lipids and proteins in digestion

      • respiration

      • production of new proteins

Enzymes: How they work

  • The lock and key theory is one simplified model that is used to explain enzyme action

  • In this model the substrate, or reactant, fits into the enzyme's active site like a key into a lock

  • An enzyme-controlled chemical reaction occurs as follows

    1. Enzymes and substrates move about randomly in solution

    2. When an enzyme and its complementary substrate collide, the substrate attaches to the active site of the enzyme

    3. After the substrate has attached to the active site, the chemical reaction occurs

    4. A product forms from the substrate, which is then released from the active site; the enzyme is unchanged and will go on to catalyse further reactions

Four-stage “Lock & Key Model”: enzyme and substrate approach, fit together at the active site, react, then the enzyme releases two products unchanged. Labels read “substrate fits exactly into active site” and “reaction takes place”.
During a chemical reaction a substrate fits into an active site like a key into a lock

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Enzyme specificity

  • Each type of enzyme catalyses a specific process in living organisms

  • This is because the shape of an enzyme's active site is complementary to its substrate

    • Proteins are formed from chains of amino acids held together by bonds

    • The order of amino acids determines the shape of an enzyme's active site

Diagram showing a substrate molecule fitting the active site of enzyme 1 and not the active site of enzyme 2, illustrating complementary enzyme–substrate specificity
Enzymes catalyse specific reactions in living organisms due to the shape of their active site.

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Effect of temperature and pH on enzyme activity

The effect of temperature

  • Enzymes work fastest at their optimum temperature – in the human body, the optimum temperature is around 37 °C

  • Heating to high temperatures (beyond the optimum) will start to break the bonds that hold the enzyme together – the enzyme's active site will lose its shape, reducing the effectiveness of substrate binding

  • Eventually the shape of the active site is lost completely and the enzyme is described as having been denatured

    • Substrates cannot fit into denatured enzymes as the specific shape of their active site has been lost

Diagram showing how increasing temperature breaks the bonds between the amino acids in an enzyme's unique structure, distorting its active site shape and preventing the substrate from fitting, causing denaturation
Denaturation is irreversible: once enzymes are denatured they cannot regain their original shape and activity will stop

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  • Increasing temperature from 0 °C to the optimum increases the activity of enzymes; this is because the more energy the molecules have, the faster they move and the more collisions there are between enzymes and substrate molecules

  • Low temperatures do not denature enzymes, but at lower temperatures there is less kinetic energy available, so enzymes and their substrates move more slowly and collide at a lower rate

Graph showing rate of enzyme activity versus temperature.

At lower temperatures:
* there are fewer successful collisions
* enzymes + substrates have less kinetic energy
* therefore low enzyme activity and  less substrate turned into product

Increasing temperatures:
* More successful collisions
* Enzymes + substrates have more kinetic energy = more substrate turned into product

At temperatures above optimum:
* there are more collisions
* but active site being deformed by higher temperature
* = number of successful collisions decrease
* (Substrate + active site no longer complementary)
Higher temperature means more kinetic energy, which initially increases enzyme activity until enzymes begin to be denatured

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The effect of pH

  • Enzymes activity is highest when the enzymes are at their optimum pH

    • Many human enzymes have an optimum pH of 7

    • Stomach enzymes have an optimum pH of 2

    • Small intestine enzymes have a higher optimum pH of 8 or 9

  • If the pH is too high or too low the bonds that hold the amino acid chain together to make up the protein can break

  • This changes the shape of the active site, so the substrate can no longer fit into it

    • The enzymes and substrate are no longer complementary

    • The enzyme has denatured

Diagram showing that increasing pH far above optimum changes an enzyme’s active site from complementary to non‑complementary to its substrate
At pH far from optimum, then the shape of the enzyme is altered and it becomes less complementary to its substrate

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  • As conditions deviate further from an enzyme's optimum pH, enzyme activity gradually slows

  • At extreme pH levels there will be no enzyme activity

Graph of enzyme activity against pH, showing a peak at optimum pH around 8–9 (depending on what enzyme and where it works in the body) and reduced activity at very low or very high pH due to denaturation and distortion of the active site
An enzyme from the small intestine has an optimum pH of 8-9; activity is reduced at pH levels that are higher or lower than this.

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Lára graduated from Oxford University in Biological Sciences and has now been a science tutor working in the UK for several years. Lára has a particular interest in the area of infectious disease and epidemiology, and enjoys creating original educational materials that develop confidence and facilitate learning.

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