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Literature summary for 5.4.99.5 extracted from

  • Davidson, B.E.; Hudson, G.S.
    Chorismate mutase-prephenate dehydrogenase from Escherichia coli (1987), Methods Enzymol., 142, 440-450.
    View publication on PubMed
Search for more literature for 5.4.99.5

General Stability

General Stability Organism
the enzyme is stable in high concentrations of glycerol, above 10% v/v, pH 7.5-8.0, and in the presence of thiols, citrate, and NAD+ Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
5,5'-dithiobis(2-nitrobenzoate)
-
 Escherichia coli
iodoacetamide
-
 Escherichia coli
L-Tyr
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
 chorismate in presence of NAD+ Escherichia coli
0.092
-
 chorismate pH 7.5, in absence of NAD+ Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39000
-
 2 * 39000, SDS-PAGE Escherichia coli
42042
-
 2 * 42042, calculation from nucleotide sequence Escherichia coli
78000
-
 sedimentation equilibrium analysis Escherichia coli

Organism

Organism UniProt Comment Textmining
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
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
dimer 2 * 39000, SDS-PAGE Escherichia coli
dimer 2 * 42042, calculation from nucleotide sequence Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+ enhances activity Escherichia coli