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.
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© 1988 Plenum Press, New York
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Gasser, C.S. et al. (1988). Studies on the 5-Enolpyruvylshikimate-3-Phosphate Synthase Genes of Higher Plants and Engineering of Glyphosate Resistance. In: Conn, E.E. (eds) Opportunities for Phytochemistry in Plant Biotechnology. Recent Advances in Phytochemistry, vol 22. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-0274-3_3
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DOI: https://doi.org/10.1007/978-1-4757-0274-3_3
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