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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1 | - |
NAD+ | - |
Sus scrofa | |
13 | - |
L-threonine | - |
Sus scrofa | |
16 | - |
L-allothreonine | - |
Sus scrofa |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Sus scrofa | - |
- |
- |
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 |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Sus scrofa | - |
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 Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
23.3 | - |
L-threonine | - |
Sus scrofa |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Sus scrofa |