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Literature summary for 2.5.1.7 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

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant D305A, in presence of phosphoenolpyruvate and UDP-N-acetyl-D-glucosamine Enterobacter cloacae

Protein Variants

Protein Variants Comment Organism
D305A crystallization data Enterobacter cloacae

Organism

Organism UniProt Comment Textmining
Enterobacter cloacae
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Reaction

Reaction Comment Organism Reaction ID
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