EPSP synthase: Difference between revisions

Revision as of 00:51, 20 January 2016

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^[1].

Relevance

EPSP synthase is a target for drugs and herbicides like Roundup.

Structural insights

The enzyme has , with the active site found in the interdomain cleft. There is a substantial structural change upon substrate binding, resulting in a . Glyphosate (also known as Roundup) occupies the binding site of the second substrate, phosphoenol pyruvate ^[2].

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 20-January-2016

ReferencesReferences

↑ 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
↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Ann Taylor, Michal Harel, Alexander Berchansky, Joel L. Sussman

[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] 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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[2]

@@ Line 1: / Line 1: @@
-<StructureSection load='1g6s' size='350' side='right' caption='Structure of EPSP synthase (PDB entry [[1eps]])' scene=''>
+<StructureSection load='1g6s' size='350' side='right' caption='Structure of E. coli EPSP synthase complex with shikimate-3-phosphate, the herbicide glyphosate and formic acid (PDB entry [[1g6s]])' scene=''>
 == Function ==
@@ Line 6: / Line 6: @@
 == Relevance ==
-EPSP synthase is a target for drugs and herbicides.
+EPSP synthase is a target for drugs and herbicides like '''Roundup'''.
 == Structural insights ==
-The enzyme has <scene name='57/570585/Two_domains/1'>two domains</scene>, with the active site found in the interdomain cleft.  There is a substantial structural change upon substrate binding, resulting in a <scene name='57/570585/Closed_formation/1'>closed formation</scene>.  '''Glyphosate''' (also known as '''Roundup''') occupies the binding site of the second substrate, phosphoenol pyruvate.
+The enzyme has <scene name='57/570585/Two_domains/1'>two domains</scene>, with the active site found in the interdomain cleft.  There is a substantial structural change upon substrate binding, resulting in a <scene name='57/570585/Closed_formation/1'>closed formation</scene>.  '''Glyphosate''' (also known as '''Roundup''') occupies the binding site of the second substrate, phosphoenol pyruvate <ref>PMID:11171958</ref>.
 </StructureSection>