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Studies on the 5-Enolpyruvylshikimate-3-Phosphate Synthase Genes of Higher Plants and Engineering of Glyphosate Resistance

  • Charles S. Gasser
  • Dilip M. Shah
  • Guy Della-Cioppa
  • Stephen M. Padgette
  • Ganesh M. Kishore
  • Harry J. Klee
  • Stephen G. Rogers
  • Robert B. Horsch
  • Robert T. Fraley
Part of the Recent Advances in Phytochemistry book series (RAPT, volume 22)

Abstract

5-Enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the addition of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to shikimate-3-phosphate (S-3-P) (Fig. 1). This reaction constitutes one step of the shikimate pathway. Products of the shikimate pathway are necessary precursors for the synthesis of aromatic amino acids, and other aromatic compounds. EPSP synthase is an essential enzyme in organisms such as plants, bacteria, and fungi which must synthesize aromatic amino acids de novo. In plants the enzyme is primarily localized in the plastids which are the major sites of synthesis of aromatic compounds. EPSP synthase is not found in animals.

Keywords

Aromatic Amino Acid Transit Peptide Shikimate Pathway Glyphosate Resistance Petunia Plant 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • Charles S. Gasser
    • 1
  • Dilip M. Shah
    • 1
  • Guy Della-Cioppa
    • 1
  • Stephen M. Padgette
    • 1
  • Ganesh M. Kishore
    • 1
  • Harry J. Klee
    • 1
  • Stephen G. Rogers
    • 1
  • Robert B. Horsch
    • 1
  • Robert T. Fraley
    • 1
  1. 1.Plant Molecular BiologyMonsanto CompanySt. LouisUSA

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