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Literature summary extracted from

  • Davidson, B.E.; Blackburn, E.H.; Dopheide, T.A.A.
    Chorismate mutase-prephenate dehydratase from Escherichia coli K-12. I. Purification, molecular weight, and amino acid composition (1972), J. Biol. Chem., 247, 4441-4446.
    View publication on PubMed

General Stability

EC Number General Stability Organism
4.2.1.51 unstable to freezing/thawing Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.51 40000
-
 2 * 40000, SDS-PAGE Escherichia coli
4.2.1.51 85000
-
 major component, gel filtration Escherichia coli
4.2.1.51 137000
-
 minor component, gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.51 prephenate Escherichia coli
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.51 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.51 bifunctional enzyme, 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
4.2.1.51 28
-
-
 Escherichia coli

Storage Stability

EC Number Storage Stability Organism
4.2.1.51 -20°C, 3 mg protein/ml Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.51 prephenate
-
 Escherichia coli phenylpyruvate + H2O + CO2
-
 ?
4.2.1.51 prephenate
-
 Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.51 dimer 2 * 40000, SDS-PAGE Escherichia coli