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Literature summary for 1.3.1.12 extracted from

  • Sampathkumar, P.; Morrison, J.F.
    Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Purification and properties of the bifunctional enzyme (1982), Biochim. Biophys. Acta, 702, 204-211.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
78000 100000 chorismate mutase-prephenate dehydrogenase bifunctional enzyme, gel electrophoresis Escherichia coli
78000 100000 chorismate mutase-prephenate dehydrogenase bifunctional enzyme, sedimentation equilibrium centrifugation Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
chorismate mutase-prephenate dehydrogenase bifunctional enzyme Escherichia coli

Storage Stability

Storage Stability Organism
-20°C, 0.1 M N-ethylmorpholine, pH 7.0, 21 mM citrate, 10% v/v glycerol, 1 mM EDTA, 1 mM DTT Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 39000-42000, SDS-PAGE Escherichia coli

Synonyms

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