title: Lead poisoning, haem synthesis and 5-aminolaevulinic acid dehydratase.
abstract: In mammals and yeast, 5-aminolaevulinic acid dehydratase is a zinc-dependent enzyme that catalyses the synthesis of porphobilinogen-the pyrrole building block that is incorporated into all modified tetrapyrroles, including haem, chlorophyll and vitamin B12. The X-ray structure of this enzyme reveals how substitution of the catalytically important zinc ion by lead inactivates the enzyme and causes a form of pseudo-porphyria.
authors.affiliation: Dept of Molecular Genetics, Institute of Ophthalmology, London, UK. warren@ucl.ac.uk
authors.forename: M J
authors.initials: MJ
authors.lastname: Warren
authors.forename: J B
authors.initials: JB
authors.lastname: Cooper
authors.forename: S P
authors.initials: SP
authors.lastname: Wood
authors.forename: P M
authors.initials: PM
authors.lastname: Shoolingin-Jordan
mesh_terms: D000818:Animals; D006418:Heme / Q000096:biosynthesis*; D006801:Humans; D007854:Lead / Q000378:metabolism; D007855:Lead Poisoning / Q000378:metabolism*; D008956:Models, Chemical; D008958:Models, Molecular; D000623:Porphobilinogen Synthase / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation
chemical_list: D007854:Lead; D006418:Heme; D000623:Porphobilinogen Synthase