Enzyme Action and the Active Site
An enzyme speeds a reaction because its active site has complementary shape and chemical properties for a substrate. Covers specificity, induced fit, and why an enzyme is not used up by the reaction it catalyses.
What a learner can do afterwards
- Explains specificity through the active site's complementary shape and chemical properties, not enzyme strength.
- States what happens to an enzyme once its reaction has finished.
- Predicts what a change in active site shape does to the reaction.
1 · Read
Enzymes are usually proteins that act as catalysts. They speed reactions by lowering activation energy, and the reaction does not use up the enzyme. A substrate binds at an active site, a pocket with particular shape and chemical properties.
The lock-and-key picture is a useful first sketch, but it is not exact. As a substrate approaches, the active site can shift a little to make a better fit. This is called induced fit. Specificity comes from the fit between site and substrate, not from enzyme strength. After the reaction, the products leave and the enzyme is released unchanged, so it can catalyse the same reaction again.
An enzyme can bind a particular substrate because its active site matches that substrate's shape and chemistry. Salivary amylase acts on starch, while a protein-digesting enzyme has a different site. A change in the site can reduce or stop the reaction.
For specificity, explain shape and chemical fit. For reuse, say the enzyme leaves unchanged after the reaction.
An active site gives an enzyme its specific job. The enzyme helps the reaction, releases its products, and can work again.
Original enzyme lesson and assessment text authored for the Hoofer taxonomy.
The rewritten readings were written for this dataset. Videos are linked from Khan Academy. License terms for these sources are not recorded.
2 · Watch
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