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Enzymes: what a catalyst can and cannot do questions
Enzymes as globular protein catalysts, activation energy and what lowering it does and does not change, the active site and the enzyme-substrate complex, the lock-and-key model and the induced fit model that replaced it, and where specificity comes from.
5 original questions · 16 marks · the enzymes: what a catalyst can and cannot do notes · Enzymes and metabolic control
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Explain why a given enzyme catalyses only one reaction, using the terms active site, complementary and enzyme-substrate complex in your answer.
Mark scheme
- B1 the active site is a region formed by the tertiary structure of the enzyme, with a particular shape
- B1 only a substrate whose shape is complementary to the active site can bind to it
- B1 when it binds, an enzyme-substrate complex forms and the reaction is catalysed
- B1 a molecule that is not complementary cannot enter the site, so no complex forms and that reaction is not catalysed
Compare the lock-and-key model of enzyme action with the induced fit model.
Mark scheme
- B1 in lock and key the active site is already exactly complementary to the substrate, whereas in induced fit it is only close to complementary before binding
- B1 in lock and key nothing moves, whereas in induced fit the active site changes shape as the substrate binds
- B1 both models account for specificity, but only induced fit accounts for the rise in rate, because the closing of the site strains the substrate's bonds
- B1 induced fit is supported by enzymes photographed with and without their substrate, such as hexokinase closing around glucose, which lock and key is not
Explain why every enzyme is a globular protein, and why a fibrous protein such as collagen cannot be one.
Mark scheme
- B1 a globular protein folds with hydrophilic side chains facing outwards, so it dissolves in cytoplasm or plasma where the reaction happens
- B1 its amino acid sequence is irregular, so the surface it presents is irregular and can carry an active site of a particular shape
- B1 a fibrous protein has a repetitive sequence and forms long insoluble strands, so it is neither soluble nor able to present such a pocket
A molecule built to resemble the strained, half-reacted form of a substrate binds to its enzyme far more tightly than the substrate itself does. Suggest what this tells us about the shape of the active site, and suggest why such a molecule would slow the enzyme down.
State what an enzyme does to the activation energy of a reaction, and state one quantity that an enzyme does not change.
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