Biosynthesis of amino acids derived from phosphoglyceric acid and pyruvic acid

  • Georges N. Cohen

Abstract

The use of appropriate mutants and an adequate enzyme analysis has enabled to decide which of these amino acids is synthesized first, since the final step in the pathway, the interconversion of serine and glycine, is catalyzed by a single enzyme, serine hydroxymethyltransferase, and since mutations affecting the biosynthesis of serine result in a nutritional requirement which can be satisfied by one or the other of these amino acids. However mutations deficient in hydroxymethyltransferase require specifically glycine and cannot grow with serine.

Keywords

Cysteine Folate Homocysteine Threonine Thymine 

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Selected references

Serine biosynthesis

  1. J. K. Bell, P. J. Pease, J. E. Bell, G. A. Grant and L. J. Banaszak, Eur. J. Biochem., 269, 4176–4184 (2002).PubMedCrossRefGoogle Scholar
  2. G. Hester, W. Stark, M. Moser, J. Kallen, Z. Markovic-Housley and J. N. Jansonius, J. Mol. Biol., 286, 829–50 (1999).PubMedCrossRefGoogle Scholar

Serine hydroxymethylase

  1. L. Schirch, Advances in Enzymology, 53, 83–112 (1982).Google Scholar
  2. G. V. Stauffer, in Amino acids: Biosynthesis and Genetic Regulation (K. M. Herrmann and R. L. Somerville, eds.), Addison-Wesley Publishing Company, Inc. Reading, Massachusetts, pp. 103–113 (1983).Google Scholar
  3. J. N. Scarsdale, S. Radaev, G. Kazanina, V. Schirch and H. T. Wright, J. Mol. Biol., 296, 155–168 (2000).PubMedCrossRefGoogle Scholar

Sulfite reductase

  1. L. M. Siegel, M. J. Murphy and H. Kamin, J. Biol. Chem., 248, 251–261 (1973).Google Scholar
  2. I. Guillouard, S. Auger, M. F. Hullo, F. Chetouani, A. Danchin and I. Martin-Verstraete, J. Bacteriol., 184, 4681–4689 (2002).Google Scholar

Valine and Leucine

  1. H. E. Umbarger, in Escherichia coli and Salmonella typhimurium, Cellular and Molecular Biology, (J. L. Ingraham, K. B. Low, B. Magasanik, M. Schachter and H. E. Umbarger, eds.) American Society for Microbiology, pp. 352–367, Washington, D. C., (1987).Google Scholar

Aspartate-ß-decarboxylase

  1. S. S. Tate and A. Meister, Advances in Enzymology, 35, 503–543 (1971)Google Scholar

Copyright information

© Springer Science+Business Media Dordrecht 2004

Authors and Affiliations

  • Georges N. Cohen
    • 1
    • 2
  1. 1.Centre National de la Recherche ScientifiqueParisFrance
  2. 2.Institut PasteurParisFrance

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