Sandbox Reserved 764: Difference between revisions
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'''Symbol''': EPSP synthase or EPSPS | '''Symbol''': EPSP synthase or EPSPS | ||
<Structure load='2AA9' size='500' frame='true' align='right' caption='EPSP synthase liganded with shikimate-3-phosphate' scene='56/564040/Lys22/1' /> | |||
The monomeric enzyme '''5-Enolpyruvlyshikimate-3-phosphate synthase (EPSP synthase)''' is an enzyme involved in the shikimate pathway found only in plants and microorganisms. The shikimate pathway is essential for the biosynthesis of chorismate, a molecule that is a precursor to majority of the aromatic compounds produced in the cell, including the aromatic amino acids (L-tyrosine, L-phenylalanine, L-tryptophan) <ref>PMID:10353849</ref>. These aromatic compounds are essential for the synthesis of proteins thereby making chorismate and the shikimate pathway essential for plants and microorganisms. EPSP synthase is a transferase or an enzyme that catalyzes the transfer of a specific functional group from one molecule to another. EPSP synthase catalyzes the transfer of the enolpyruvyl group from phosphonenolpyruvate (PEP) to shikimate-3-phosphate (S3P) to form 5-enolpyruvylshikimate-3-phosphate (EPSP) and inorganic phosphate. EPSP is converted into chorismate, which is then introduced into synthesis pathways of aromatic compounds <ref>PMID:10353849</ref>. EPSP synthase has two distinct globular <scene name='56/564040/Two_domains/1'>domains</scene>, composed of beta sheets and alpha helices <ref>PMID:11607190</ref>. Each of the domains are composed of three protein folding subunits. The subunits contain two alpha helices and four beta sheets <ref>PMID:11607190</ref>. As shown in Figure 3 below, each domain has six alpha helices and twelve beta sheets. The two domains, which are linked together by two crossover chain segments, exist in an open conformation until the binding of shikimate-3-phosphate, which is the enzyme's binding substrate <ref>PMID:17348837</ref>. Upon the binding of shikimate-3-phosphate, the domains close together to form the active site in an interdomain cleft. Phosphoenolpyruvate then enters the active site enabling EPSP synthase to catalyze the transfer of the enolpyruvyl group through an addition-elimination reaction. EPSP synthase is attractive for drug research because of its potential to serve as a selective target for antimicrobial drugs <ref>PMID:17348837</ref>. Because EPSP synthase is found only in plants and microorganisms, its use in antimicrobial drugs will limit the harmful side effects for humans. | The monomeric enzyme '''5-Enolpyruvlyshikimate-3-phosphate synthase (EPSP synthase)''' is an enzyme involved in the shikimate pathway found only in plants and microorganisms. The shikimate pathway is essential for the biosynthesis of chorismate, a molecule that is a precursor to majority of the aromatic compounds produced in the cell, including the aromatic amino acids (L-tyrosine, L-phenylalanine, L-tryptophan) <ref>PMID:10353849</ref>. These aromatic compounds are essential for the synthesis of proteins thereby making chorismate and the shikimate pathway essential for plants and microorganisms. EPSP synthase is a transferase or an enzyme that catalyzes the transfer of a specific functional group from one molecule to another. EPSP synthase catalyzes the transfer of the enolpyruvyl group from phosphonenolpyruvate (PEP) to shikimate-3-phosphate (S3P) to form 5-enolpyruvylshikimate-3-phosphate (EPSP) and inorganic phosphate. EPSP is converted into chorismate, which is then introduced into synthesis pathways of aromatic compounds <ref>PMID:10353849</ref>. EPSP synthase has two distinct globular <scene name='56/564040/Two_domains/1'>domains</scene>, composed of beta sheets and alpha helices <ref>PMID:11607190</ref>. Each of the domains are composed of three protein folding subunits. The subunits contain two alpha helices and four beta sheets <ref>PMID:11607190</ref>. As shown in Figure 3 below, each domain has six alpha helices and twelve beta sheets. The two domains, which are linked together by two crossover chain segments, exist in an open conformation until the binding of shikimate-3-phosphate, which is the enzyme's binding substrate <ref>PMID:17348837</ref>. Upon the binding of shikimate-3-phosphate, the domains close together to form the active site in an interdomain cleft. Phosphoenolpyruvate then enters the active site enabling EPSP synthase to catalyze the transfer of the enolpyruvyl group through an addition-elimination reaction. EPSP synthase is attractive for drug research because of its potential to serve as a selective target for antimicrobial drugs <ref>PMID:17348837</ref>. Because EPSP synthase is found only in plants and microorganisms, its use in antimicrobial drugs will limit the harmful side effects for humans. | ||
antimicrobial drugs | antimicrobial drugs | ||
==EPSP Synthase Structure== | ==EPSP Synthase Structure== | ||
