Literature summary for 2.5.1.19 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.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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	-	?

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?
phosphoenolpyruvate + 3-phosphoshikimate	phosphate induces conformational change on the MtEPSPS structure	Mycobacterium tuberculosis	phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate	-	?

Synonyms

Synonyms	Comment	Organism
EPSPS	-	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)