EPSP synthase
From Proteopedia
(Difference between revisions)
(New page: == Structure of EPSP Synthase == <StructureSection load='1eps' size='350' side='right' caption='Structure of EPSP synthase (PDB entry 1eps)' scene=''> 5-enolpyruvylshikimate 3-phospha...) |
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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. | 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. | + | 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. |
| - | </StructureSection | + | </StructureSection> |
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Revision as of 04:15, 2 December 2013
Structure of EPSP Synthase
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