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Literature summary for 4.3.1.19 extracted from

  • Koerner, K.; Rahimi-Laridjani, I.; Grimminger, H.
    Purification of biosynthetic threonine deaminase from Escherichia coli (1975), Biochim. Biophys. Acta, 397, 220-230.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
4 * 50000, SDS-PAGE Escherichia coli
214000
-
meniscus depletion equilibrium sedimentation, analytical ultracentrifugation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
biosynthetic threonine deaminase
-

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
230
-
-
Escherichia coli

Storage Stability

Storage Stability Organism
-20°C, 50% loss of activity after 3 weeks Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-threonine
-
Escherichia coli 2-oxobutanoate + NH3
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 50000, SDS-PAGE Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate contains 2 mol of pyridoxal 5'-phosphate per mol of enzyme Escherichia coli