Enzymes
Enzymes are proteins that act as biological catalysts: they speed up reactions without being used up. Each enzyme has an active site with a shape complementary to its substrate (lock and key), forming an enzyme–substrate complex. Activity rises with temperature up to an optimum (about 37 °C for human enzymes) as molecules collide more often; above it the enzyme denatures: the active site changes shape and the substrate no longer fits. Each enzyme also has an optimum pH.
Learning objectives
- Describe enzymes as biological catalysts.
- Explain enzyme action and specificity with the lock and key model.
- Explain the effects of temperature and pH, including denaturation.
A high fever above 42 °C can be fatal. Why?
Core idea
Without enzymes, digesting a single meal would take decades. Enzymes speed up reactions millions of times, at body temperature, without being used up.
Each enzyme's active site fits one substrate. Temperature and pH change how fast enzymes work; too much heat or the wrong pH changes the active site's shape permanently.
1. How enzymes work
The enzyme is unchanged and can be reused.
2. Temperature and pH
Amylase: rate 2 units at 20 °C, 6 at 37 °C, 1 at 60 °C.
- Goal
- Explain the pattern.
- Strategy
- Below optimum: collisions. Above: denaturation.
- More kinetic energy, more frequent successful collisions.
- Active site changes shape; substrate no longer fits.
Why do we store food in a freezer rather than just a fridge for longer periods?
Summary
- Biological catalysts.
- Specific active site.
- Optimum T and pH; denaturation.
- Active site
- Region of an enzyme where the substrate binds.
- Substrate
- Molecule an enzyme acts on.
- Denatured
- Active site permanently changed shape.
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