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Literature summary for 4.2.1.51 extracted from

  • Gething, M.J.; Davidson, B.E.; Dopheide, T.A.A.
    Chorismate mutase/prephenate dehydratase from Escherichia coli K12. 1. The effect of NaCl and its use in a new purification involving affinity chromatography on sepharosyl-phenylalanine (1976), Eur. J. Biochem., 71, 317-325.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
KCl
-
Escherichia coli
L-phenylalanine
-
Escherichia coli
NaCl
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
prephenate Escherichia coli
-
?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
bifunctional enzyme, chorismate mutase:prephenate dehydratase Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
32
-
-
Escherichia coli

Storage Stability

Storage Stability Organism
-20°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prephenate
-
Escherichia coli phenylpyruvate + H2O + CO2
-
?
prephenate
-
Escherichia coli ?
-
?