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Biochemistry · Heme synthesis: lead poisoning
Sample itemA 4-year-old living in an old house with peeling paint has abdominal pain, constipation and microcytic anaemia with basophilic stippling. Which pair of enzymes in haem synthesis is inhibited?
Original practice item, not a recalled exam question. Nothing here is recorded.
The answer and the reasoning
A. ALA dehydratase and ferrochelatase
Lead inhibits ALA dehydratase and ferrochelatase, with ALA accumulating in urine and protoporphyrin in red cells. Poor haem synthesis causes microcytic anaemia, and lead also impairs RNA breakdown, causing stippling.
Option by option
A. ALA dehydratase and ferrochelatase (correct)
Correct. Lead blocks ALA dehydratase and ferrochelatase, the classic haem synthesis targets.
B. Porphobilinogen deaminase and ALA synthase
Porphobilinogen deaminase is the enzyme deficient in acute intermittent porphyria, while ALA synthase is not the main lead target.
C. Heme oxygenase and biliverdin reductase
Heme oxygenase and biliverdin reductase degrade haem and are not part of its synthesis.
D. ALA synthase and uroporphyrinogen decarboxylase
ALA synthase is feedback-inhibited by haem and uroporphyrinogen decarboxylase is the PCT enzyme, which lead does not target.
Source note: Original NextPrep sample item — pending expert review. This item is original practice material awaiting independent expert review, so confirm important facts in a standard textbook.
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