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Literature summary for 4.2.3.5 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

Inhibitors Comment Organism Structure
(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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Cofactor

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

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
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