Literature summary for 2.5.1.19 extracted from

Marques, M.R.; Pereira, J.H.; Oliveira, J.S.; Basso, L.A.; de Azevedo, W.F.; Santos, D.S.; Palma, M.S.
The inhibition of 5-enolpyruvylshikimate 3-phosphate synthase as a model for development of novel antimicrobials (2007), Curr. Drug Targets, 8, 445-457.

Search for more literature for 2.5.1.19

Application

Application	Comment	Organism
drug development	more experimental data needed for effective structure-based drug design	Bacteria

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular docking using known structures of EPSPS in complex with (R)-phosphonate analogue of the tetrahedral reaction intermediate	Bacteria

Inhibitors

Inhibitors	Comment	Organism	Structure
glyphosate	3-phosphoshikimate binding is prerequisite for glyphosate binding	Bacteria

Organism

Organism	UniProt	Comment	Textmining
Bacteria	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate	ordered substrate binding with 3-phosphoshikimate being bound first	Bacteria	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
shikimate 3-phosphate + phosphoenolpyruvate	shikimate 3-phosphate binding site primarily at the N-terminal domain of the enzyme, phosphoenolpyruvate-binding mainly a the C-terminal domain	Bacteria	phosphate + 5-enolpyruvylshikimate 3-phosphate	-	?

Synonyms

Synonyms	Comment	Organism
5-enolpyruvylshikimate 3-phosphate synthase	-	Bacteria
EPSP synthase	-	Bacteria
EPSPS	-	Bacteria

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Release 2023.1 (January 2023)