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Literature summary extracted from

  • Calhoun, D.H.; Kuska, J.S.; Hatfield, G.W.
    Threonine deaminase from Escherichia coli. II. Maturation and physical properties of the enzyme from a mutant altered in its regulation of gene expression (1974), J. Biol. Chem., 250, 127-131.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.3.1.19 additional information the enzyme from the regulatory mutant CU18 is indistinguishable from the wild type enzyme in molecular weight and subunit composition Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.1.19 Ile 0.5 mM, wild type enzyme is completely inhibited at both pH 8.0 and pH 6.5, the mutant enzyme is sensitive only at pH 6.5. In contrast to the wild type enzyme 1 mM Val does not reverse L-Ile inhibition of the mutant enzyme Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.1.19 49800
-
 4 * 49800, equilibrium sedimentation of the enzyme dialyzed against 6 M guanidine hydrochloride Escherichia coli
4.3.1.19 201000
-
 equilibrium sedimentation Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.19 Escherichia coli
-
 regulatory mutant CU18
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.1.19
-
 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 * 49800, equilibrium sedimentation of the enzyme dialyzed against 6 M guanidine hydrochloride Escherichia coli