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Literature summary for 2.3.1.29 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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate reaction mechanism Sus scrofa
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + glycine
-
Sus scrofa CoA + 2-amino-3-oxobutanoate
-
r
acetyl-CoA + glycine involved in L-threonine catabolism, inducible Sus scrofa CoA + 2-amino-3-oxobutanoate
-
?

Subunits

Subunits Comment Organism
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