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Enzymes and Metabolism · Paper 2 — Free Biology HL Practice Questions

1MasterySAQ-SMetabolic pathways: Anabolism and catabolism5 marksPaper 2~8 min
The shows a metabolic pathway in Escherichia coli that synthesises product Z from substrate X via intermediate Y.
(a)
Identify the site at which product Z acts and state the term for this type of enzyme regulation. [2 marks]
(b)
Describe how end-product inhibition controls the concentration of product Z in the cell. [2 marks]
(c)
Evaluate the advantage of regulating Enzyme 1 rather than Enzyme 2 in this pathway. [1 mark]
diagram

Solutions

2ChallengeSAQ-LEnzyme kinetics and inhibition10 marksPaper 2~15 min
A pharmaceutical company is testing drug Y as a potential treatment for hypertension. Drug Y inhibits angiotensin-converting enzyme (ACE), which converts angiotensin I to angiotensin II. The kinetics of ACE were studied in vitro at fixed enzyme concentration. 1v=KmVmax⋅1[S]+1Vmax\frac{1}{v} = \frac{K_m}{V_{max}} \cdot \frac{1}{[S]} + \frac{1}{V_{max}} [Angiotensin I] (nM)[\text{Angiotensin I}]\ (\text{nM}) — v (nmol min−1)v\ (\text{nmol min}^{-1}) — no drug — v (nmol min−1)v\ (\text{nmol min}^{-1}) — with 10 nM10\ \text{nM} drug Y 22 — 0.800.80 — 0.500.50 55 — 1.501.50 — 1.001.00 1010 — 2.202.20 — 1.701.70 2020 — 2.802.80 — 2.502.50 5050 — 3.303.30 — 3.203.20
(a)
Using the Lineweaver–Burk linearisation, calculate VmaxV_{max} and KmK_m for ACE both in the absence and in the presence of 10 nM10\ \text{nM} drug Y. [4 marks]
(b)
Using your values from (a), deduce whether drug Y acts a competitive or non-competitive inhibitor of ACE. [2 marks]
(c)
Evaluate the use of non-competitive ACE inhibitors antihypertensive drugs, considering both their pharmacological advantages over competitive inhibitors and the limitations arising from their mechanism of action. [4 marks]
diagram

Solutions

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