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Literature summary for 5.4.99.5 extracted from

  • Davidson, B.E.
    Chorismate mutase-prephenate dehydratase from Escherichia coli (1987), Methods Enzymol., 142, 432-439.
    View publication on PubMed
Search for more literature for 5.4.99.5

Inhibitors

Inhibitors Comment Organism Structure
L-Phe
-
 Escherichia coli
L-Phe
-
 Klebsiella aerogenes
prephenate competitive Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information when the pH increases from pH 6.2 to pH 8.6 the Km-values for prephenate and chorismate increase substantially Escherichia coli
0.47 1 prephenate
-
 Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 x * 40000, the smallest native species of the enzyme, determined by sedimentation equilibrium, appears to be a dimer Escherichia coli

Organism

Organism UniProt Comment Textmining
Cupriavidus necator
-
 basonym Alcaligenes eutrophus
-
Escherichia coli
-
 K12
-
Escherichia coli
-
 bifunctional enzyme chorismate mutase/prephenate dehydratase
-
Klebsiella aerogenes
-
-
-
Pseudomonas sp.
-
-
-
Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-
Xanthomonas campestris
-
-
-

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
additional information
-
-
 Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
? x * 40000, the smallest native species of the enzyme, determined by sedimentation equilibrium, appears to be a dimer Escherichia coli