Cloned (Comment) | Organism |
---|---|
wild-type and mutant enzymes K54E, S53K54-K53S54 and E192Q, overexpression in Escherichia coli | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
E192Q | specific activity is markedly decreased, less than 5% of the wild-type activity, Km-values for lipoamide and dihydrolipoamide are markedly reduced | Homo sapiens |
K54E | about 25% less bound FAD compared to wild-type, specific activity is markedly decreased, less than 5% of the wild-type activity, Km-value for lipoamide is increased by about twofold | Homo sapiens |
S53K/K54S | about 25% less bound FAD compared to wild-type, specific activity is markedly decreased, less than 5% of the wild-type activity, Km-values for lipoamide and dihydrolipoamide are markedly reduced. The catalytic rate constant, turnover number/Km, is significantly lower than wild-type | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.05 | - |
dihydrolipoamide | mutant enzyme S53K/K54S | Homo sapiens | |
0.071 | - |
NADH | mutant enzyme E192Q | Homo sapiens | |
0.12 | - |
dihydrolipoamide | mutant enzyme E192Q | Homo sapiens | |
0.13 | - |
NADH | mutant enzyme S53K/K54S | Homo sapiens | |
0.31 | - |
NAD+ | mutant enzyme E192Q | Homo sapiens | |
0.31 | - |
Lipoamide | mutant enzyme E192Q | Homo sapiens | |
0.4 | - |
NAD+ | wild-type enzyme | Homo sapiens | |
0.55 | - |
NAD+ | mutant enzyme S53K/K54S | Homo sapiens | |
0.63 | - |
Lipoamide | mutant enzyme S53K/K54S | Homo sapiens | |
0.88 | - |
dihydrolipoamide | wild-type enzyme | Homo sapiens | |
2.25 | - |
Lipoamide | wild-type enzyme | Homo sapiens | |
5 | - |
Lipoamide | mutant enzyme K54E | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
wild-type and mutant enzymes K54E, S53K54-K53S54 and E192Q | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dihydrolipoamide + NAD+ | - |
Homo sapiens | lipoamide + NADH | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
6.75 | - |
NAD+ | mutant enzyme S53K/K54S | Homo sapiens | |
8.5 | - |
dihydrolipoamide | mutant enzyme S53K/K54S | Homo sapiens | |
14.4 | - |
Lipoamide | mutant enzyme S53K/K54S | Homo sapiens | |
19.8 | - |
NADH | mutant enzyme S53K/K54S | Homo sapiens | |
23 | - |
Lipoamide | mutant enzyme K54E | Homo sapiens | |
26.2 | - |
NADH | mutant enzyme E192Q | Homo sapiens | |
29.7 | - |
dihydrolipoamide | mutant enzyme E192Q | Homo sapiens | |
30 | - |
NAD+ | mutant enzyme E192Q | Homo sapiens | |
81.3 | - |
Lipoamide | mutant enzyme E192Q | Homo sapiens | |
340 | - |
NADH | wild-type enzyme | Homo sapiens | |
567 | - |
dihydrolipoamide | wild-type enzyme | Homo sapiens | |
574 | - |
NAD+ | wild-type enzyme | Homo sapiens | |
649 | - |
Lipoamide | wild-type enzyme | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | wild-type enzyme contains 1 FAD per subunit, mutant enzymes K54E and S53K/K54S have about 25% less bound FAD | Homo sapiens | |
NAD+ | - |
Homo sapiens |