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Literature summary for 1.1.1.103 extracted from

  • Tressel, T.; Thompson, R.; Zieske, L.R.; Menendez, M.I.T.S.; Davis, L.
    Interaction between L-threonine dehydrogenase and aminoacetone synthetase and mechanism of aminoacetone production (1986), J. Biol. Chem., 261, 16428-16437.
    View publication on PubMed
Search for more literature for 1.1.1.103

Inhibitors

Inhibitors Comment Organism Structure
aminoacetone uncompetitive inhibition vs. NAD+ or L-threonine Sus scrofa
HCO3- noncompetitive inhibition vs. NAD+ or L-threonine Sus scrofa
NADH competitive inhibition vs. NAD+, noncompetitive vs. L-threonine Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1
-
 NAD+
-
 Sus scrofa
13
-
 L-threonine
-
 Sus scrofa
16
-
 L-allothreonine
-
 Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-threonine + NAD+ Sus scrofa
-
 (2S)-2-amino-3-oxobutanoate + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+ it is suggested that the unstable L-2-amino-3-oxobutanoate spontaneousely decarboxylates to the stable aminoacetone, there is also some evidence that L-threonine is oxidatively decarboxylated by threonine dehydrogenase to produce aminoacetone Sus scrofa
a

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-allothreonine + NAD+
-
 Sus scrofa L-2-amino-3-oxobutanoate + NADH
-
 ?
L-threonine + NAD+
-
 Sus scrofa (2S)-2-amino-3-oxobutanoate + NADH + H+
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
23.3
-
 L-threonine
-
 Sus scrofa

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Sus scrofa