Cellular and Molecular Biology 2009-03-01

5-aminolevulinate synthase: catalysis of the first step of heme biosynthesis.

GA Hunter, GC Ferreira

Index: Cell Mol. Biol. 55 , 102-110, (2009)

Full Text: HTML

Abstract

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.


Related Compounds

  • Succinyl-Coenzyme...

Related Articles:

Direct biosynthesis of adipic acid from a synthetic pathway in recombinant Escherichia coli.

2014-12-01

[Biotechnol. Bioeng. 111(12) , 2580-6, (2014)]

Functional characterization of a vitamin B12-dependent methylmalonyl pathway in Mycobacterium tuberculosis: implications for propionate metabolism during growth on fatty acids.

2008-06-01

[J. Bacteriol. 190(11) , 3886-95, (2008)]

Acetate formation in the energy metabolism of parasitic helminths and protists.

2010-03-15

[Int. J. Parasitol. 40 , 387-397, (2010)]

Acetate:succinate CoA-transferase in the hydrogenosomes of Trichomonas vaginalis: identification and characterization.

2008-01-18

[J. Biol. Chem. 283 , 1411-1418, (2008)]

Acetate:succinate CoA-transferase in the anaerobic mitochondria ofFasciola hepatica

2009-01-01

[Mol. Biochem. Parasitol. 164 , 74-79, (2009)]

More Articles...