Protein Variants | Comment | Organism |
---|---|---|
E122A | mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type | Saccharomyces cerevisiae |
E122Q | mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type | Saccharomyces cerevisiae |
E78A | mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism differs from wild-type, 2-oxoglutarate binds to enzyme and enzyme-NADH | Saccharomyces cerevisiae |
E78A/E122A | mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type | Saccharomyces cerevisiae |
E78Q | mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type | Saccharomyces cerevisiae |
E78Q/E122Q | mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type | Saccharomyces cerevisiae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Saccharomyces cerevisiae | |
NADH | - |
Saccharomyces cerevisiae | |
oxalylglycine | competitive against lysine with mutant E78A, noncompetitive with mutants E78Q, E122Q, E78Q/E122Q, E122A, E78A/E122A | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.014 | - |
NADH | mutant E78Q, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.019 | - |
NADH | wild-type, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.025 | - |
NADH | mutant E122Q, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.036 | - |
NADH | mutant E78A, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.062 | - |
NADH | mutant E122A, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.11 | - |
2-oxoglutarate | wild-type, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.12 | - |
NADH | mutant E78Q/E122Q, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.133 | - |
NADH | mutant E78A/E122A, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.18 | - |
2-oxoglutarate | mutant E78A, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.23 | - |
2-oxoglutarate | mutant E78Q, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.3 | - |
2-oxoglutarate | mutant E122Q, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.55 | - |
2-oxoglutarate | mutant E122A, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.62 | - |
L-lysine | mutant E78A, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.9 | - |
NAD+ | wild-type, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
1.1 | - |
NAD+ | mutant E78Q, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
1.1 | - |
L-lysine | wild-type, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
2 | - |
N6-(L-1,3-dicarboxypropyl)-L-lysine | mutant E78Q, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
2 | - |
2-oxoglutarate | mutant E78Q/E122Q, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
3.3 | - |
NAD+ | mutant E122Q, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
4 | - |
L-lysine | mutant E78Q, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
4.8 | 5 | 2-oxoglutarate | mutant E78A/E122A, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
6.7 | - |
N6-(L-1,3-dicarboxypropyl)-L-lysine | wild-type, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
11 | - |
L-lysine | mutant E122Q, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
14 | - |
N6-(L-1,3-dicarboxypropyl)-L-lysine | mutant E122Q, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
27.1 | - |
L-lysine | mutant E78Q/E122Q, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
36.5 | - |
L-lysine | mutant E122A, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
190.7 | - |
L-lysine | mutant E78A/E122A, 25°C, pH 7.2 | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-lysine + 2-oxoglutarate + NADH + H+ | - |
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 + H+ | - |
? |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.015 | - |
NADH | mutant E78A/E122A, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.017 | - |
NADH | wild-type, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.019 | - |
NADH | mutant E122A, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.038 | - |
NADH | mutant E78A, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
0.5 | - |
NAD+ | mutant E78Q, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
1.1 | - |
NAD+ | wild-type, 25°C, pH 7.2 | Saccharomyces cerevisiae | |
1.9 | - |
NAD+ | mutant E122Q, 25°C, pH 7.2 | Saccharomyces cerevisiae |