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Literature summary extracted from

  • Baldwin, G.S.; Davidson, B.E.
    Kinetic studies on the mechanism of chorismate mutase/prephenate dehydratase from Escherichia coli K12 (1983), Biochim. Biophys. Acta, 742, 374-383.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.51 cis-aconitate
-
Escherichia coli
4.2.1.51 citrate
-
Escherichia coli
4.2.1.51 trans-aconitate
-
Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.51 prephenate Escherichia coli biosynthesis of phenylalanine ?
-
?

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.51 prephenate
-
Escherichia coli phenylpyruvate + H2O + CO2
-
?
4.2.1.51 prephenate biosynthesis of phenylalanine Escherichia coli ?
-
?

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.2.1.51 6 9
-
Escherichia coli

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
4.2.1.51 5 6 37°C, 5 min stable Escherichia coli