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5-aminolevulinate synthase: catalysis of the first step of heme biosynthesis Hunter GA; Ferreira GCCell Mol Biol (Noisy-le-grand) 2009[Feb]; 55 (1): 102-105-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.|5-Aminolevulinate Synthetase/chemistry/genetics/*metabolism[MESH]|Aminolevulinic Acid/metabolism[MESH]|Anemia, Sideroblastic/enzymology/genetics[MESH]|Heme/*biosynthesis[MESH]|Humans[MESH]|Kinetics[MESH]|Models, Molecular[MESH]|Mutation[MESH]|Structure-Activity Relationship[MESH] |
