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Literature summary for 4.3.1.19 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
Search for more literature for 4.3.1.19

Inhibitors

Inhibitors Comment Organism Structure
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]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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
203800
-
 sedimentation equilibrium experiments Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 a genetically derepressed mutant strain of Escherichia coli K12
-
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
-
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
210
-
-
 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 * 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

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