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Literature summary for 4.2.1.51 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

General Stability Organism
unstable to freezing/thawing Escherichia coli

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

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

Storage Stability

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

Substrates and Products (Substrate)

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

Subunits

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