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Literature summary extracted from

  • Osborne, A.; Thorneley, R.N.; Abell, C.; Bornemann, S.
    Studies with substrate and cofactor analogues provide evidence for a radical mechanism in the chorismate synthase reaction (2000), J. Biol. Chem., 275, 35825-35830.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.3.5 (6R)-6-fluoro-5-enoylpyruvylshikimate 3-phosphate IC50 is 0.0005 mM when the enzyme is preincubated with the inhibitor, the IC50 is 0.25 mM when the enzyme is not preincubated with the inhibitor, inhibition is not absolutely irreversible Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.5 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.5 O5-(1-carboxyvinyl)-3-phosphoshikimate evidence for a radical mechanism Escherichia coli chorismate + phosphate
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.3.5 FMN cofactor Escherichia coli
4.2.3.5 additional information no activity with 5-deaza-FMN Escherichia coli

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
4.2.3.5 0.25
-
 IC50 is 0.0005 mM when the enzyme is preincubated with the inhibitor, the IC50 is 0.25 mM when the enzyme is not preincubated with the inhibitor, inhibition is not absolutely irreversible Escherichia coli (6R)-6-fluoro-5-enoylpyruvylshikimate 3-phosphate