Abstract:Molecular defects have been reported for five of the eight enzymes involved in heme biosynthesis that provide a molecular basis for the corresponding porphyria(s): δ-aminolevulinate dehydratase, porph...Molecular defects have been reported for five of the eight enzymes involved in heme biosynthesis that provide a molecular basis for the corresponding porphyria(s): δ-aminolevulinate dehydratase, porphobilinogen synthase deficiency; porphobilinogen deaminase, acute intermittent porphyria; uroporphyrinogen decarboxylase, hepatoerythropoietic porphyria and familial porphyria cutanea tarda; and ferrochelatase, erythropoietic protoporphyria. In general, missense mutations, deletions, or insertions have been reported. Future investigation is required to determine the consequences of the mutations on enzyme structure and function and types of mutations in patients who have two distinct types of porphyria.Read More
Publication Year: 1993
Publication Date: 1993-10-01
Language: en
Type: article
Indexed In: ['crossref']
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Cited By Count: 3
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