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  • 5-aminolevulinate synthase: catalysis of the first step of heme biosynthesis
  • Hunter GA; Ferreira GC
  • Cell Mol Biol (Noisy-le-grand) 2009[Feb]; 55 (1): 102-10
  • 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.
  • |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]

  • *{{pmid19268008}}
    *<b>[ 5-aminolevulinate synthase: catalysis of the first step of heme biosynthesis ]</b> Cell Mol Biol (Noisy-le-grand) 2009; 55(1) ; 102-10 Hunter GA; Ferreira GC


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    Cell Mol Biol (Noisy-le-grand)

    102 1.55 2009