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Literature summary for 4.1.1.68 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
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Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Specific Activity [micromol/min/mg]

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

Storage Stability

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

Substrates and Products (Substrate)

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

Subunits

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