EPSP synthase
From Proteopedia
Structure of EPSP Synthase
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References
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Proteopedia Page Contributors and Editors (what is this?)
Ann Taylor, Michal Harel, Alexander Berchansky, Joel L. Sussman
5-enolpyruvylshikimate 3-phosphate (EPSP) synthase is a key enzyme for the biosynthesis of aromatic amino acids in plants and many microbes. Consequently, it is a target for drugs and herbicides. 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. 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 closed formation. Glyphosate (also known as Roundup) occupies the binding site of the second substrate, phosphoenol pyruvate.
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Ann Taylor, Michal Harel, Alexander Berchansky, Joel L. Sussman
This page was last modified 03:57, 2 December 2013.