5.1 Enzymes
- Syllabus
- 0610–2026–2027
- Topic
- 5.1
- Level
- —
A catalyst is a substance that increases the rate of a chemical reaction and is not changed by the reaction.
| Feature | Meaning |
|---|---|
| increases reaction rate | products form faster |
| unchanged at the end | it is not used up and can act again |
If the catalyst is present before and after the reaction while the substrate decreases and products increase, it has sped up the conversion without becoming a product.
A catalyst changes the rate, not the identity of the products, and 'not changed' does not mean it cannot temporarily interact with reactants during the reaction.
Enzymes are proteins that function as biological catalysts in all metabolic reactions.
Metabolism is the set of chemical reactions in cells and organisms. Enzymes control reactions in processes such as digestion, respiration and the building or breakdown of molecules.
| Question | Enzyme answer |
|---|---|
| type of molecule | protein |
| function | biological catalyst |
| where needed | metabolic reactions in living organisms |
| fate after a reaction | unchanged and reusable |
An enzyme is not a carbohydrate, substrate or product. It catalyses a reaction but is not consumed by it.
Enzymes make metabolic reactions proceed fast enough at the temperatures inside organisms to sustain life.
| Life process | Why sufficient reaction rate matters |
|---|---|
| respiration | releases energy quickly enough for cell activities |
| digestion | produces soluble nutrients quickly enough for absorption |
| synthesis | builds cell materials needed for growth and repair |
| breakdown and detoxification | removes or converts substances before harmful accumulation |
Without enzymes, many necessary reactions would be too slow under normal biological conditions. Raising body temperature enough to speed them chemically would damage cells, so biological catalysts are essential.
Do not say enzymes create energy or make impossible reactions happen. They increase the rate of reactions needed for life and remain unchanged overall.
An enzyme has an active site whose shape is complementary to its substrate.
| Step | Event |
|---|---|
| 1 | the correctly shaped substrate fits into the active site |
| 2 | the enzyme catalyses conversion of the substrate |
| 3 | product molecules form and leave the active site |
| 4 | the unchanged enzyme can act again |
Complementary means the shapes fit one another; it does not mean they are identical shapes. The substrate occupies the active site because their outlines match.
Products are formed from the substrate, not from the enzyme. The enzyme is not permanently joined to them or used up.
Enzyme activity usually rises to an optimum and then falls; high temperature can denature an enzyme, while each enzyme also has an optimum pH.
| Investigation | Change | Measure | Control |
|---|---|---|---|
| temperature | water-bath temperature | product per time or time to a fixed endpoint | pH, enzyme/substrate concentration and volume |
| pH | buffer pH | product per time or time to a fixed endpoint | temperature, enzyme/substrate concentration and volume |
Use a range of values, allow solutions to reach the target condition before mixing, start timing on mixing, repeat, calculate mean rates and plot rate against temperature or pH.
The optimum is the condition giving the highest rate—or shortest time to a fixed endpoint. Above the temperature optimum, activity falls sharply as enzymes denature.
A shorter reaction time means a faster rate. Low temperature usually slows an enzyme without denaturing it; boiling can cause permanent loss of activity.
The substrate binds at the enzyme's active site to form a temporary enzyme–substrate complex; the substrate is converted into product, which leaves the enzyme.
| Term | Role |
|---|---|
| enzyme | protein catalyst |
| active site | region where the substrate binds |
| substrate | molecule changed by the reaction |
| enzyme–substrate complex | temporary joined state |
| product | molecule or molecules released after conversion |
enzyme + substrate → enzyme–substrate complex → enzyme + product(s)
The active site becomes free after products leave, so the same enzyme molecule can catalyse another reaction.
The complex is temporary. Do not label the substrate as a product before conversion or treat the active site as a separate molecule.
An enzyme is specific because the shape of its active site is complementary to the shape of its substrate.
| Molecule reaches active site | Outcome |
|---|---|
| complementary substrate | fits, binds and can form an enzyme–substrate complex |
| non-complementary molecule | does not fit correctly, so the enzyme does not catalyse its conversion |
Different substrates have different shapes, so organisms require different enzymes for different reactions.
Specificity depends on the three-dimensional fit at the active site, not on the whole enzyme and substrate having the same outline.
Complementary means matching like interlocking shapes, not identical. A change to active-site shape can therefore remove specificity and activity.
Temperature affects enzyme activity through particle kinetic energy, effective-collision frequency and, above the optimum, denaturation.
| Temperature region | Molecular explanation |
|---|---|
| below optimum, warming | particles gain kinetic energy, move faster and collide more frequently |
| approaching optimum | more collisions have the correct orientation and sufficient energy, so more enzyme–substrate complexes form per second |
| above optimum | bonds maintaining enzyme shape are disrupted; active-site shape changes |
| high temperature | substrate no longer fits; effective collisions fall and the enzyme is denatured |
The rise is gradual because collision frequency increases progressively; the fall can be steep because denaturation removes correctly shaped active sites.
High temperature does not kill an enzyme—it is not living. It denatures the protein by changing its shape; low temperature mainly reduces kinetic energy and collision frequency.
Each enzyme has an optimum pH at which its active site has the best shape for its substrate and activity is highest.
| pH condition | Effect |
|---|---|
| at optimum | active-site shape and substrate fit support the greatest activity |
| moving away from optimum | active-site shape changes, fit becomes poorer and fewer enzyme–substrate complexes form |
| extreme pH | bonds maintaining enzyme shape are disrupted; the enzyme may be denatured |
Different enzymes can have different optimum pH values because they work in different environments and have different protein structures.
Describe a pH graph using its active range, optimum pH and changes on both sides, then explain the changes through active-site shape, fit and denaturation.
Changing pH does not merely slow all enzymes in the same direction. Activity falls on either side of that enzyme's optimum, and extreme pH may denature it.