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

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.

• Authors: G A Hunter, G C Ferreira
• Journal: Cellular and molecular biology (Noisy-le-Grand, France) (Cell Mol Biol (Noisy-le-grand)) Vol. 55 Issue 1 Pg. 102-10 (Feb 16 2009) ISSN: 1165-158X [Electronic] France
• PMID: 19268008 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Review)

Chemical References

• Heme
• Aminolevulinic Acid
• 5-Aminolevulinate Synthetase

Topics

• 5-Aminolevulinate Synthetase (chemistry, genetics, metabolism)
• Aminolevulinic Acid (metabolism)
• Anemia, Sideroblastic (enzymology, genetics)
• Heme (biosynthesis)
• Humans
• Kinetics
• Models, Molecular
• Mutation
• Structure-Activity Relationship