EC Number | Cloned (Comment) | Organism |
---|---|---|
1.8.1.4 | wild-type and mutant enzymes K37E, H452Q and E457Q | Homo sapiens |
1.8.1.4 | wild-type and mutant enzymes K37E, H452Q and E457Q, overexpression in Escherichia coli | Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.8.1.4 | E457Q | molar ratio of FAD to enzyme is 0.9 compared to 1 for the wild-type enzyme, mutation affects the environment surrounding FAD, decrease in efficiency of electron transfer from the reduced flavin to the oxidized substrate | Homo sapiens |
1.8.1.4 | H452Q | molar ratio of FAD to enzyme is 0.94 compared to 1 for the wild-type enzyme, no production of NADH when the enzyme is reduced by dihydrolipoamide, transfer of electrons from the substrate dihydrolipoamide to NAD+ is extremely low | Homo sapiens |
1.8.1.4 | K37E | molar ratio of FAD to enzyme is 0.76 compared to 1 for the wild-type enzyme | Homo sapiens |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.8.1.4 | 0.25 | - |
NAD+ | mutant enzyme K37E | Homo sapiens | |
1.8.1.4 | 0.32 | - |
NAD+ | native enzyme and mutant enzyme E457Q | Homo sapiens | |
1.8.1.4 | 0.38 | - |
NAD+ | mutant enzyme H452Q | Homo sapiens | |
1.8.1.4 | 0.69 | - |
dihydrolipoamide | native enzyme | Homo sapiens | |
1.8.1.4 | 0.76 | - |
dihydrolipoamide | mutant enzyme K37E | Homo sapiens | |
1.8.1.4 | 2.9 | - |
dihydrolipoamide | mutant enzyme H457Q | Homo sapiens | |
1.8.1.4 | 43.6 | - |
dihydrolipoamide | mutant enzyme H452Q | Homo sapiens |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.8.1.4 | Homo sapiens | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.8.1.4 | wild-type and mutant enzymes K37E, H452Q and E457Q | Homo sapiens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.1.4 | dihydrolipoamide + NAD+ | - |
Homo sapiens | lipoamide + NADH | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.8.1.4 | additional information | - |
additional information | - |
Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.8.1.4 | FAD | wild-type enzyme contains 1 FAD per subunit, mutant enzyme K37E has about 25% less bound FAD | Homo sapiens | |
1.8.1.4 | NAD+ | - |
Homo sapiens |