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EPSP synthase
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EPSP synthase
5-enolpyruvylshikimate-3-phosphate (EPSP) synthase is an enzyme produced by plants and microorganisms. EPSPS catalyzes the chemical reaction:
Thus, the two substrates of this enzyme are phosphoenolpyruvate (PEP) and 3-phosphoshikimate, whereas its two products are phosphate and 5-enolpyruvylshikimate-3-phosphate.
This enzyme is absent from animal genomes, making it an attractive target for herbicides such as glyphosate. A glyphosate-resistant version of the enzyme's gene has been incorporated into genetically modified crops.
The enzyme belongs to the family of transferases, to be specific those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is phosphoenolpyruvate:3-phosphoshikimate 5-O-(1-carboxyvinyl)-transferase. Other names in common use include:
EPSP synthase is a monomeric enzyme with a molecular mass of approximately 46,000. It consists of two domains connected by protein strands that function as a hinge, allowing the two domains to move closer together. When a substrate binds to the enzyme, the conformational change causes the domains to clamp around the substrate at the active site.
EPSP synthase is classified into two groups based on sensitivity to glyphosate. Class I enzymes, found in plants and some bacteria, are inhibited by low micromolar concentrations of glyphosate. Class II enzymes, found in other bacteria, are resistant to glyphosate inhibition.
EPSP synthase participates in the biosynthesis of the aromatic amino acids phenylalanine, tyrosine, and tryptophan via the shikimate pathway in bacteria, fungi, and plants. EPSP synthase is produced only by plants and micro-organisms; the gene coding for it is not in the mammalian genome. Gut flora of some animals contain EPSPS.
EPSP synthase catalyzes the reaction which converts shikimate-3-phosphate plus phosphoenolpyruvate to 5-enolpyruvylshikimate-3-phosphate (EPSP) by way of an acetal-like tetrahedral intermediate. Basic and acidic amino acids in the active site are involved in deprotonation of the hydroxyl group of PEP and in the proton-exchange steps related to the tetrahedral intermediate itself, respectively.
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EPSP synthase
5-enolpyruvylshikimate-3-phosphate (EPSP) synthase is an enzyme produced by plants and microorganisms. EPSPS catalyzes the chemical reaction:
Thus, the two substrates of this enzyme are phosphoenolpyruvate (PEP) and 3-phosphoshikimate, whereas its two products are phosphate and 5-enolpyruvylshikimate-3-phosphate.
This enzyme is absent from animal genomes, making it an attractive target for herbicides such as glyphosate. A glyphosate-resistant version of the enzyme's gene has been incorporated into genetically modified crops.
The enzyme belongs to the family of transferases, to be specific those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is phosphoenolpyruvate:3-phosphoshikimate 5-O-(1-carboxyvinyl)-transferase. Other names in common use include:
EPSP synthase is a monomeric enzyme with a molecular mass of approximately 46,000. It consists of two domains connected by protein strands that function as a hinge, allowing the two domains to move closer together. When a substrate binds to the enzyme, the conformational change causes the domains to clamp around the substrate at the active site.
EPSP synthase is classified into two groups based on sensitivity to glyphosate. Class I enzymes, found in plants and some bacteria, are inhibited by low micromolar concentrations of glyphosate. Class II enzymes, found in other bacteria, are resistant to glyphosate inhibition.
EPSP synthase participates in the biosynthesis of the aromatic amino acids phenylalanine, tyrosine, and tryptophan via the shikimate pathway in bacteria, fungi, and plants. EPSP synthase is produced only by plants and micro-organisms; the gene coding for it is not in the mammalian genome. Gut flora of some animals contain EPSPS.
EPSP synthase catalyzes the reaction which converts shikimate-3-phosphate plus phosphoenolpyruvate to 5-enolpyruvylshikimate-3-phosphate (EPSP) by way of an acetal-like tetrahedral intermediate. Basic and acidic amino acids in the active site are involved in deprotonation of the hydroxyl group of PEP and in the proton-exchange steps related to the tetrahedral intermediate itself, respectively.
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