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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Sus scrofa | - |
- |
- |
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 | 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 | 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 |