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Literature summary extracted from

  • Eschenburg, S.; Kabsch, W.; Healy, M.L.; Schonbrunn, E.
    A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) derived from X-ray structures of their tetrahedral reaction intermediate states (2003), J. Biol. Chem., 278, 49215-49222.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.5.1.19 synthesis enzyme is a target for development and synthesis of antimicrobial drugs Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.19 overexpression of wild-type and mutant enzymes in strain BL21(DE3) Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.7 mutant D305A, in presence of phosphoenolpyruvate and UDP-N-acetyl-D-glucosamine Enterobacter cloacae
2.5.1.19 purified recombinant wild-type and mutant enzymes in complex with the substrates, at 19°C, from 4 M sodium formate in presence of 5 mM 3-phosphoshikimate and 5 mM phosphoenolpyruvate, X-ray diffraction structure determination and analysis at 1.6 A resolution Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.7 D305A crystallization data Enterobacter cloacae
2.5.1.19 D313A site-directed mutagenesis, comparison of the mutant active site and substrate binding structures to those of the wild-type enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.19 phosphoenolpyruvate + 3-phosphoshikimate Escherichia coli 6th enzyme in the shikimate pathway phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.7 Enterobacter cloacae
-
-
-
2.5.1.19 Escherichia coli P0A6D3 gene aroA
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.7 phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine tetrahedral reaction intermediate, overall addition-elimination reaction is halted after the addition step Enterobacter cloacae
a
2.5.1.19 phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate catalytic mechanism, tetrahedral reaction intermediate, active site structure, wild-type and mutant D313A Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.19 phosphoenolpyruvate + 3-phosphoshikimate 6th enzyme in the shikimate pathway Escherichia coli phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
 ?
2.5.1.19 phosphoenolpyruvate + 3-phosphoshikimate substrate binding of wild-type and mutant D313A, overview Escherichia coli phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.19 5-enolpyruvylshikimate-3-phosphate synthase
-
 Escherichia coli
2.5.1.19 AroA
-
 Escherichia coli
2.5.1.19 additional information enzyme belongs to the family of enolpyruvyl transferases Escherichia coli