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Literature summary extracted from

  • Baldwin, G.S.; McKenzie, G.H.; Davidson, B.E.
    The self-association of chorismate mutase/prephenate dehydratase from Escherichia coli K12 (1981), Arch. Biochem. Biophys., 211, 76-85.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.51 90000 273000 ultracentrifugation at various experimental conditions, depending on pH, temperature, salt concentration, protein concentration the enzyme undergoes self-association 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 ?
-
?