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Literature summary extracted from

  • Eisenstein, E.
    Cloning, expression, purification, and characterization of biosynthetic threonine deaminase from Escherichia coli (1991), J. Biol. Chem., 266, 5801-5807.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.3.1.19 L-Val activates Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.1.19 expression in Brevibacterium flavum Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.1.19 Ile negative allosteric effector Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.1.19 56000
-
 4 * 56000, SDS-PAGE Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.19 Escherichia coli
-
-
-
4.3.1.19 Escherichia coli
-
 biosynthetic threonine deaminase
-
4.3.1.19 Escherichia coli K 12
-
-
-

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
-
 ?
4.3.1.19 L-threonine
-
 Escherichia coli K 12 2-oxobutanoate + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
4.3.1.19 tetramer 4 * 56000, SDS-PAGE Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.1.19 pyridoxal 5'-phosphate cofactor Escherichia coli
4.3.1.19 pyridoxal 5'-phosphate enzyme contains 1 mol of pyridoxal 5'-phosphate per 56000 Da subunit Escherichia coli