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Flashcards · 5090 · Topic 5

Enzymes flashcards

10 cards on Topic 5, subtopics 5.1 to 5.2. Pick a subtopic or study them all.

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5.1 Enzyme action

Catalyst
A substance that increases the rate of a chemical reaction and is not changed (not used up) by the reaction.
Enzyme
A protein that functions as a biological catalyst.
How an enzyme works (lock and key)
The substrate fits into the active site, whose shape is complementary to it. An enzyme-substrate complex forms, the reaction occurs, and the products are released. The enzyme is unchanged and reused.
Why are enzymes specific?
Each active site has a shape complementary to one particular substrate, so only that substrate can bind and form an enzyme-substrate complex.
Two ways to follow the progress of an enzyme reaction
Measure the disappearance of substrate (e.g. sample amylase and starch into iodine until no blue-black forms) or the appearance of product (e.g. collect oxygen from catalase and hydrogen peroxide in a gas syringe).

5.2 Effects of temperature and pH

Effect of temperature below the optimum
Rate increases with temperature: molecules have more kinetic energy, so there are more frequent successful collisions between enzyme and substrate.
Effect of temperature above the optimum
Rate falls sharply. The active site changes shape, the substrate no longer fits and no enzyme-substrate complexes form: the enzyme is denatured.
Is denaturation reversible? Are enzymes "killed"?
Denaturation is permanent: cooling does not restore activity. Enzymes are denatured, never killed, because they were never alive.
Effect of pH on enzyme activity
Each enzyme has an optimum pH. Either side of it activity falls; extremes of pH denature the enzyme by changing the shape of the active site.
Approximate optimum pH of pepsin, amylase and trypsin
Pepsin: about 2 (stomach). Amylase: about 7 (mouth, small intestine). Trypsin: about 8 (small intestine).