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Biochemistry · Haem synthesis: delta-aminolevulinate synthase
Sample itemA man on antituberculous therapy develops a microcytic hypochromic anaemia with ring sideroblasts in the marrow. Isoniazid has depleted a vitamin, impairing the first enzyme of haem synthesis. Which enzyme is affected?
Original practice item, not a recalled exam question. Nothing here is recorded.
The answer and the reasoning
A. Delta-aminolevulinate synthase
Isoniazid binds pyridoxal phosphate and increases its excretion, so the first haem enzyme, which depends on that cofactor, falls. Iron then accumulates in mitochondria as ring sideroblasts. Pyridoxine supplementation prevents and corrects this.
Option by option
A. Delta-aminolevulinate synthase (correct)
Correct. This enzyme needs pyridoxal phosphate, which isoniazid depletes.
B. Ferrochelatase
Ferrochelatase is inhibited by lead and depends on iron, not pyridoxal phosphate.
C. Porphobilinogen deaminase
Porphobilinogen deaminase needs no pyridoxal phosphate and is deficient in acute intermittent porphyria.
D. Delta-aminolevulinate dehydratase
The dehydratase depends on zinc and is inhibited by lead, not by lack of pyridoxine.
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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