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Literature summary for 5.4.99.5 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
L-Phe
-
Escherichia coli
NaCl inhibition is cooperative, NaCl also increases the sensitivity of the enzyme to inhibition by Phe Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
K12
-
Escherichia coli
-
bifunctional enzyme chorismate mutase/prephenate dehydratase
-

Purification (Commentary)

Purification (Comment) Organism
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
52
-
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Chorismate
-
Escherichia coli Prephenate
-
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