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The monomeric enzyme '''5-Enolpyruvlyshikimate-3-phosphate synthase (EPSPS)''' 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 precursor to majority of the aromatic compounds produced in the cell, including the aromatic amino acids (L-tyrosine, L-phenylalanine, L-tryptophan),that are needed for protein synthesis. Studies suggest that the compounds produced in this pathway constitute as much as or more than 35% of the dry mass of plants. | The monomeric enzyme '''5-Enolpyruvlyshikimate-3-phosphate synthase (EPSPS)''' 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 precursor to majority of the aromatic compounds produced in the cell, including the aromatic amino acids (L-tyrosine, L-phenylalanine, L-tryptophan),that are needed for protein synthesis. Studies suggest that the compounds produced in this pathway constitute as much as or more than 35% of the dry mass of plants. | ||
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Contents |
5-Enolpyruvylshikimate-3-phosphate synthase
Formula weight:
Classification: transferase
Length: __ residues
Domains: 2
The monomeric enzyme 5-Enolpyruvlyshikimate-3-phosphate synthase (EPSPS) 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 precursor to majority of the aromatic compounds produced in the cell, including the aromatic amino acids (L-tyrosine, L-phenylalanine, L-tryptophan),that are needed for protein synthesis. Studies suggest that the compounds produced in this pathway constitute as much as or more than 35% of the dry mass of plants.
EPSP Synthase Structure
three-dimensional backbone of EPSP synthase elucidated through X-ray crystallography in 1991 by W. C. Stallings et al. (14). This provided a basis for more in-depth studies of structure and function, and it was followed by further X-ray chrystallographic analysis by Ernst Schönbrunn and coworkers who resolved in atomic detail the structure and active site of EPSP synthase bound to S3P and EPSP synthase binding S3P and glyphosate (1). NMR was used to further detail the interactions of S3P with the N-terminal domain of EPSP synthase and the conformational changes that take place upon substrate binding (15).
EPSP Synthase Mechanism
Implicatons
The implications in studying EPSP synthase involve the fact that this enzyme is not present in humans but is essential for bacteria and apicomplexan parasites. This makes EPSP synthase a selective target for antimicrobial drugs and decreases possible negative impacts of drugs in humans.
