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Literature summary 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

General Stability

EC Number General Stability Organism
1.3.1.12 citrate stabilizes Escherichia coli
1.3.1.12 glycerol stabilizes Escherichia coli
1.3.1.12 NAD+ plus tyrosine stabilizes Escherichia coli
1.3.1.12 thiols stabilize Escherichia coli
5.4.99.5 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

EC Number Inhibitors Comment Organism Structure
1.3.1.12 5,5'-dithiobis(2-nitrobenzoate)
-
 Escherichia coli
1.3.1.12 iodoacetamide
-
 Escherichia coli
1.3.1.12 L-tyrosine
-
 Escherichia coli
5.4.99.5 5,5'-dithiobis(2-nitrobenzoate)
-
 Escherichia coli
5.4.99.5 iodoacetamide
-
 Escherichia coli
5.4.99.5 L-Tyr
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.12 0.045 0.09 prephenate
-
 Escherichia coli
1.3.1.12 0.13 0.15 NAD+
-
 Escherichia coli
5.4.99.5 0.04
-
 chorismate in presence of NAD+ Escherichia coli
5.4.99.5 0.092
-
 chorismate pH 7.5, in absence of NAD+ Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.12 78000 100000 chorismate mutase-prephenate dehydrogenase bifunctional enzyme, sedimentation equilibrium centrifugation Escherichia coli
5.4.99.5 39000
-
 2 * 39000, SDS-PAGE Escherichia coli
5.4.99.5 42042
-
 2 * 42042, calculation from nucleotide sequence Escherichia coli
5.4.99.5 78000
-
 sedimentation equilibrium analysis Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.12 prephenate + NAD+ Escherichia coli biosynthesis of L-tyrosine 4-hydroxyphenylpyruvate + NADH + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.12 Escherichia coli
-
-
-
5.4.99.5 Escherichia coli
-
 bifunctional enzyme chorismate mutase/prephenate dehydratase
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.12 chorismate mutase-prephenate dehydrogenase bifunctional enzyme Escherichia coli
5.4.99.5 chorismate mutase/prephenate dehydratase Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.1.12 52 101
-
 Escherichia coli
5.4.99.5 additional information
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.12 prephenate + NAD+
-
 Escherichia coli 4-hydroxyphenylpyruvate + NADH + CO2
-
 ?
1.3.1.12 prephenate + NAD+ biosynthesis of L-tyrosine Escherichia coli 4-hydroxyphenylpyruvate + NADH + CO2
-
 ?
5.4.99.5 Chorismate
-
 Escherichia coli Prephenate
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.1.12 dimer 2 * 39000-42000, SDS-PAGE Escherichia coli
5.4.99.5 dimer 2 * 39000, SDS-PAGE Escherichia coli
5.4.99.5 dimer 2 * 42042, calculation from nucleotide sequence Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.3.1.12 chorismate mutase-prephenate dehydrogenase bifunctional enzyme complex with EC 5.4.99.5 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.99.5 NAD+ enhances activity Escherichia coli