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Literature summary for 4.3.1.19 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
Search for more literature for 4.3.1.19

Protein Variants

Protein Variants Comment Organism
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

Inhibitors Comment Organism Structure
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]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 regulatory mutant CU18
-

Purification (Commentary)

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