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Literature summary for 4.3.1.19 extracted from

  • Leoncini, R.; Vannoni, D.; di Pietro, C.; Guerranti, R.; Rosi, F.; Pagani, R.; Marinello, E.
    Restoration of rat liver L-threonine dehydratase activity by pyridoxamine 5 -phosphate: the half-transaminating activity of L-threonine dehydratase and its regulatory role (1998), Biochim. Biophys. Acta, 1425, 411-418.
    View publication on PubMed
Search for more literature for 4.3.1.19

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
61.8
-
 L-Ser
-
 Rattus norvegicus
99.5
-
 L-Thr
-
 Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine
-
 Rattus norvegicus pyruvate + NH3
-
 ?
L-threonine
-
 Rattus norvegicus 2-oxobutanoate + NH3
-
 ?
additional information when pyridoxamine 5'-phosphate is incubated with the apoenzyme in the presence of small quantities of keto acids, e.g. pyruvate or 2-oxobutanoate, small amounts of L-Ala or L-aminobutanoate are formed, the reaction is not reversible Rattus norvegicus ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
243
-
 L-Ser
-
 Rattus norvegicus
287
-
 L-Thr
-
 Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate Km: 0.000682 mM Rattus norvegicus
pyridoxal 5'-phosphate reactivates after dissociation of the coenzyme Rattus norvegicus
pyridoxamine 5'-phosphate reactivates after dissociation of the coenzyme Rattus norvegicus