Inhibitors | Comment | Organism | Structure |
---|---|---|---|
alpha-ketoglutarate | substrate inhibition, uncompetitive versus NADH | Saccharomyces cerevisiae | |
L-lysine | substrate inhibition, competitive versus NADH | Saccharomyces cerevisiae | |
additional information | detailed analysis of inhibition patterns for product and dead end inhibitors | Saccharomyces cerevisiae | |
saccharopine | product inhibition, uncompetitive versus NADH | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.019 | - |
NADH | 25°C, pH 7.0 | Saccharomyces cerevisiae | |
0.9 | - |
NAD+ | 25°C, pH 7.0 | Saccharomyces cerevisiae | |
1.1 | - |
L-lysine | 25°C, pH 7.0 | Saccharomyces cerevisiae | |
6.7 | - |
N6-(L-1,3-dicarboxypropyl)-L-lysine | 25°C, pH 7.0 | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH + H+ | ordered addition of NAD followed by saccharopine in the physiologic reaction direction. In the opposite direction, NADH adds to the enzyme first, while there is no preference for the order of binding of alpha-ketoglutarate and lysine | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-lysine + 2-oxoglutarate + NADH | - |
Saccharomyces cerevisiae | N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O | - |
? | |
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O | - |
Saccharomyces cerevisiae | L-lysine + 2-oxoglutarate + NADH | - |
r |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
27.8 | - |
L-lysine | 25°C, pH 7.0 | Saccharomyces cerevisiae | |
28 | - |
alpha-ketoglutarate | 25°C, pH 7.0 | Saccharomyces cerevisiae |