作者: Peter M. Jordan
DOI: 10.1016/0959-440X(94)90273-9
关键词: Tetrapyrrole 、 Acute intermittent porphyria 、 Messenger RNA 、 Enzyme 、 Porphobilinogen deaminase 、 Biochemistry 、 Haem biosynthesis 、 ATP synthase 、 Ferrochelatase 、 Biology 、 Molecular biology 、 Structural biology
摘要: Abstract The haem biosynthesis pathway continues to provide surprises, from the first enzyme, 5-aminolaevulinic acid synthase, mRNA of which contains an iron-responsive element, last, ferrochelatase, that iron sulphur cluster. 5-Aminolaevulinate dehydratases animals are zinc-dependent enzymes while those plants require magnesium. X-ray structure a synthesis porphobilinogen deaminase, has not only yielded clues about mechanism tetrapyrrole assembly but also provided insight into molecular basis human disease acute intermittent porphyria. Evidence is growing suggest previously unsuspected alternative may exist.