EPSP synthase

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, generating 5-enolpyruvylshikimate-3-phosphate, which is a precursor for phenylalanine and tyrosine^[1].

Relevance

EPSP synthase is a target for drugs and herbicides.

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.

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

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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

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