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Literature summary for 2.5.1.19 extracted from

  • de Souza, A.X.; SantAnna, C.M.
    5-Enolpyruvylshikimate-3-phosphate synthase: determination of the protonation state of active site residues by the semiempirical method (2008), Bioorg. Chem., 36, 113-120.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
semiempirical molecular modelling using, among others, the crystal structure of EPSPS mutant D313A (PDB: 1Q36) as model for assignment of protonation states of all basic amino acids in the active site: in the enzyme-tetrahedral reaction intermediate (TI) complex is residue His385 in a neutral form (with protonated epsilon-N atom) while residues Lys22, Lys340 and Lys411 are protonated, hydrogen bonds occur between Lys22 and the carboxylate oxygen atom of the phosphoenolpyruvate moiety of the TI, Asp313 has only minor effects on TI positioning within the active site but mediates as a base the attack of the TI C4-hydroxyl group on the TI methyl group prior to EPSP formation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6D3
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Reaction

Reaction Comment Organism Reaction ID
phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate via formation of a tetrahedral intermediate (TI) after which residue His385 is in a neutral form while residues Lys22, Lys340 and Lys411 are protonated, Asp313 mediates attack of the TI C4-OH group (as oxyanion, shikimate-3-phosphate moiety) at the TI C3-methyl group (phosphoenolpyruvate moiety), Lys22 serves as general acid catalyst for TI breakdown Escherichia coli

Synonyms

Synonyms Comment Organism
5-enolpyruvylshikimate-3-phosphate synthase
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Escherichia coli
AroA
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Escherichia coli
EPSP synthase
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Escherichia coli
EPSPS
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Escherichia coli