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Literature summary extracted from

  • Roper, D.I.; Cooper, R.A.
    Purification, nucleotide sequence and some properties of a bifunctional isomerase/decarboxylase from the homoprotocatechuate degradative pathway of Escherichia coli C (1993), Eur. J. Biochem., 217, 575-580.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.68
-
Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.68 0.032
-
5-oxopent-3-ene-1,2,5-tricarboxylate
-
Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.68 27000
-
gel filtration Escherichia coli
4.1.1.68 42100
-
sedimentation equilibrium centrifugation Escherichia coli
4.1.1.68 44514
-
1 * 44514, calculation from nucleotide sequence Escherichia coli
4.1.1.68 50000
-
1 * 50000, SDS-PAGE Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.68 Escherichia coli
-
-
-
4.1.1.68 Escherichia coli
-
bifunctional enzyme with activity of EC 5.3.3.10 and EC 4.1.1.68
-
4.1.1.68 Escherichia coli C
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.68
-
Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.68 45
-
-
Escherichia coli

Storage Stability

EC Number Storage Stability Organism
4.1.1.68 4°C, stable for at least 2 months Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.68 5-Oxopent-3-ene-1,2,5-tricarboxylate
-
Escherichia coli 2-Oxohept-3-enedioate + CO2
-
?
4.1.1.68 5-Oxopent-3-ene-1,2,5-tricarboxylate
-
Escherichia coli C 2-Oxohept-3-enedioate + CO2
-
?

Subunits

EC Number Subunits Comment Organism
4.1.1.68 monomer 1 * 50000, SDS-PAGE Escherichia coli
4.1.1.68 monomer 1 * 44514, calculation from nucleotide sequence Escherichia coli