Learning Outcomes

Students should be able to:

(a)   Explain the mode of action of enzymes in terms of an active site, enzyme-substrate complex, lowering of activation energy and enzyme specificity using the lock-and-key and induced-fit hypotheses.

(b)   Investigate and explain the effects of temperature, pH, enzyme concentration and substrate concentration on the rate of an enzyme-catalysed reaction by measuring rates of formation of products (e.g. measuring gas produced using catalase) or rate of disappearance of substrate (e.g. using amylase, starch and iodine).

(c)   Describe the structure of competitive and non-competitive inhibitors with reference to the binding sites of the inhibitor. [H2 only]

(d)   Explain the effects of competitive and non-competitive inhibitors (including allosteric inhibitors) on the rate of enzyme activity. [H2 only]

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