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 |
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 |
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 |
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.103 | Sus scrofa | - |
- |
- |
2.3.1.29 | Sus scrofa | - |
- |
- |
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 | |
2.3.1.29 | acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate | reaction mechanism | Sus scrofa | |
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 |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.1.1.103 | liver | - |
Sus scrofa | - |
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 | - |
? |
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 |
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 |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.103 | NAD+ | - |
Sus scrofa |