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Literature summary extracted from

  • Borges, J.C.; Pereira, J.H.; Vasconcelos, I.B.; dos Santos, G.C.; Olivieri, J.R.; Ramos, C.H.; Palma, M.S.; Basso, L.A.; Santos, D.S.; de Azevedo, W.F.
    Phosphate closes the solution structure of the 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) from Mycobacterium tuberculosis (2006), Arch. Biochem. Biophys., 452, 156-164.
    View publication on PubMed

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 Mycobacterium tuberculosis the 5-enolpyruvylshikimate-3-phosphate synthase catalyses the sixth step of the shikimate pathway that is responsible for synthesizing aromatic compounds phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
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Organism

EC Number Organism UniProt Comment Textmining
2.5.1.19 Mycobacterium tuberculosis
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.19 phosphoenolpyruvate + 3-phosphoshikimate the 5-enolpyruvylshikimate-3-phosphate synthase catalyses the sixth step of the shikimate pathway that is responsible for synthesizing aromatic compounds Mycobacterium tuberculosis phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
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 ?
2.5.1.19 phosphoenolpyruvate + 3-phosphoshikimate phosphate induces conformational change on the MtEPSPS structure Mycobacterium tuberculosis phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
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Synonyms

EC Number Synonyms Comment Organism
2.5.1.19 EPSPS
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 Mycobacterium tuberculosis