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Literature summary for 4.3.1.19 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

Activating Compound Comment Organism Structure
L-Val activates Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
expression in Brevibacterium flavum Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Ile negative allosteric effector Escherichia coli

Molecular Weight [Da]

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

Organism

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

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

Subunits

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

Cofactor

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