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Literature summary extracted from

  • Pagani, R.; Leoncini, R.; Pizzichini, M.; Vannoni, D.; Tabucchi, A.; Marinello, E.
    Properties of rat liver L-threonine deaminase (1994), Enzyme Protein, 48, 90-97.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.1.19 61
-
 L-Ser
-
 Rattus norvegicus
4.3.1.19 129
-
 L-Thr
-
 Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.19 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.1.19
-
 Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.3.1.19 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.19 L-serine
-
 Rattus norvegicus pyruvate + NH3
-
 ?
4.3.1.19 L-threonine
-
 Rattus norvegicus 2-oxobutanoate + NH3
-
 ?

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.3.1.19 7.5 9.5 activity increases from pH 7.5 to pH 9.5 Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.1.19 pyridoxal 5'-phosphate activates Rattus norvegicus
4.3.1.19 pyridoxal 5'-phosphate reactivates after dissociation of the coenzyme Rattus norvegicus
4.3.1.19 pyridoxamine 5'-phosphate reactivates after dissociation of the coenzyme Rattus norvegicus