EPSP synthase: Difference between revisions

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== Function ==
== Function ==


'''5-enolpyruvylshikimate 3-phosphate (EPSP) synthase''' is a key enzyme for the biosynthesis of aromatic amino acids in plants and many microbes.  Consequently. EPSP synthase catalyzes the addition of phosphoenol pyruvate (PEP) to shikimate-3-phosphate (S3P), generating 5-enolpyruvylshikimate-3-phosphate, which is a precursor for phenylalanine and tyrosine<ref>PMID:16225867</ref>.  
'''5-enolpyruvylshikimate 3-phosphate (EPSP) synthase''' is a key enzyme for the biosynthesis of aromatic amino acids in plants and many microbes. EPSP synthase catalyzes the addition of phosphoenol pyruvate (PEP) to shikimate-3-phosphate (S3P), generating 5-enolpyruvylshikimate-3-phosphate, which is a precursor for phenylalanine and tyrosine<ref>PMID:16225867</ref>. EPSP synthase is a target for herbicides like '''Roundup''', which contain glyphosate, an inhibitor of EPSP synthase.  Herbicide resistant plants contain an glyphosate insensitive version of EPSP synthase derived from ''Agrobacterium'' sp strain CP4, so it is called CP4 EPSP synthase. <ref>PMID:16916934</ref>,
 
== Relevance ==
 
EPSP synthase is a target for drugs and herbicides like '''Roundup'''.


== Structural insights ==
== Structural insights ==

Revision as of 16:40, 14 August 2018

Function

5-enolpyruvylshikimate 3-phosphate (EPSP) synthase is a key enzyme for the biosynthesis of aromatic amino acids in plants and many microbes. EPSP synthase catalyzes the addition of phosphoenol pyruvate (PEP) to shikimate-3-phosphate (S3P), generating 5-enolpyruvylshikimate-3-phosphate, which is a precursor for phenylalanine and tyrosine[1]. EPSP synthase is a target for herbicides like Roundup, which contain glyphosate, an inhibitor of EPSP synthase. Herbicide resistant plants contain an glyphosate insensitive version of EPSP synthase derived from Agrobacterium sp strain CP4, so it is called CP4 EPSP synthase. [2],

Structural insights

The enzyme has two domains, with the active site found in the interdomain cleft . There is a substantial structural change upon substrate binding, resulting in a conformation. . Glyphosate (also known as Roundup) occupies the of the second substrate, phosphoenol pyruvate [3].

Structure of E. coli EPSP synthase complex with shikimate-3-phosphate, the herbicide glyphosate and formic acid (PDB entry 1g6s)

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3D structures of EPSP synthase3D structures of EPSP synthase

Updated on 14-August-2018

ReferencesReferences

  1. ↑ Priestman MA, Healy ML, Funke T, Becker A, Schonbrunn E. Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate. FEBS Lett. 2005 Oct 24;579(25):5773-80. PMID:16225867 doi:10.1016/j.febslet.2005.09.066
  2. ↑ Funke T, Han H, Healy-Fried ML, Fischer M, Schonbrunn E. Molecular basis for the herbicide resistance of Roundup Ready crops. Proc Natl Acad Sci U S A. 2006 Aug 29;103(35):13010-5. Epub 2006 Aug 17. PMID:16916934
  3. ↑ Schonbrunn E, Eschenburg S, Shuttleworth WA, Schloss JV, Amrhein N, Evans JN, Kabsch W. Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail. Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1376-80. PMID:11171958 doi:http://dx.doi.org/10.1073/pnas.98.4.1376

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