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Literature summary extracted from

  • Calhoun, D.H.; Rimerman, R.A.; Hatfield, G.W.
    Threonine deaminase from Escherichia coli. I. Purification and properties (1973), J. Biol. Chem., 248, 3511-3516.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.1.19 Ile competitive allosteric inhibitor, the enzyme exists in two distinct catalytically active species: a tetramer sensitive to L-Ile inhibition and a dimer insensitive to L-Ile inhibition Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.1.19 53000
-
 4 * 53000, the enzyme exists in two distinct catalytically active species: a tetramer sensitive to L-Ile inhibition and a dimer insensitive to L-Ile inhibition, SDS-PAGE Escherichia coli
4.3.1.19 203800
-
 sedimentation equilibrium experiments Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.19 Escherichia coli
-
 a genetically derepressed mutant strain of Escherichia coli K12
-
4.3.1.19 Escherichia coli
-
 the enzyme exists in two distinct catalytically active species: a tetramer sensitive to L-Ile inhibition and a dimer insensitive to L-Ile inhibition
-
4.3.1.19 Escherichia coli
-
 biosynthetic threonine deaminase
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.1.19
-
 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3.1.19 210
-
-
 Escherichia coli

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
4.3.1.19 tetramer 4 * 53000, the enzyme exists in two distinct catalytically active species: a tetramer sensitive to L-Ile inhibition and a dimer insensitive to L-Ile inhibition, SDS-PAGE Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.1.19 pyridoxal 5'-phosphate cofactor Escherichia coli