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Literature summary 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

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.103 1
-
 NAD+
-
 Sus scrofa
1.1.1.103 13
-
 L-threonine
-
 Sus scrofa
1.1.1.103 16
-
 L-allothreonine
-
 Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.29 additional information
-
 when loaded together threonine dehydrogease and aminoacetone synthetase co-eludes at a molecular weight of 150000 Da Sus scrofa
2.3.1.29 56000
-
 gel filtration Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.103 L-threonine + NAD+ Sus scrofa
-
 (2S)-2-amino-3-oxobutanoate + NADH + H+
-
 ?
2.3.1.29 acetyl-CoA + glycine Sus scrofa involved in L-threonine catabolism, inducible CoA + 2-amino-3-oxobutanoate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.103 Sus scrofa
-
-
-
2.3.1.29 Sus scrofa
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.103 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
2.3.1.29 acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate reaction mechanism Sus scrofa
a
2.3.1.29 acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate physical interaction between threonine dehydrogenase and aminoacetone synthetase demonstrated, the two enzymes form a complex Sus scrofa
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.103 liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.103 L-allothreonine + NAD+
-
 Sus scrofa L-2-amino-3-oxobutanoate + NADH
-
 ?
1.1.1.103 L-threonine + NAD+
-
 Sus scrofa (2S)-2-amino-3-oxobutanoate + NADH + H+
-
 ?
2.3.1.29 acetyl-CoA + glycine
-
 Sus scrofa CoA + 2-amino-3-oxobutanoate
-
 r
2.3.1.29 acetyl-CoA + glycine involved in L-threonine catabolism, inducible Sus scrofa CoA + 2-amino-3-oxobutanoate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.29 More the threonine dehydrogenase and the aminoacetone synthetase form a complex with an apparent stoichiometry of two dimers of aminoacetone synthetase to one threonine dehydrogenase tetramer Sus scrofa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.103 23.3
-
 L-threonine
-
 Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.103 NAD+
-
 Sus scrofa