5-aminolevulinate synthase: catalysis of the first step of heme biosynthesis.
5-Aminolevulinate synthase is a homodimeric pyridoxal 5'-phosphate-dependent enzyme that catalyzes the first step of the heme biosynthetic pathway in animals, fungi, and the alpha-subclass of the photosynthetic purple bacteria. The reaction cycle involves condensation of glycine with succinyl-coenzyme A to yield 5-aminolevulinate, carbon dioxide, and CoA. Mutations in the human erythroid-specific aminolevulinate synthase gene are associated with the erythropoietic disorder X-linked sideroblastic anemia. Recent kinetic and crystallographic data have facilitated an unprecedented understanding of how this important enzyme produces 5-aminolevulinate, and suggest possible directions for future research that may lead to treatments not only for X-linked sideroblastic anemia, but also other diseases.
Hunter
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Department of Molecular Medicine, College of Medicine, University of South Florida, Tampa, Florida 33612, USA.
Ferreira
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GC
D000624:5-Aminolevulinate Synthetase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000622:Aminolevulinic Acid / Q000378:metabolism; D000756:Anemia, Sideroblastic / Q000201:enzymology / Q000235:genetics; D006418:Heme / Q000096:biosynthesis*; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D009154:Mutation; D013329:Structure-Activity Relationship
D006418:Heme; D000622:Aminolevulinic Acid; D000624:5-Aminolevulinate Synthetase