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Literature summary for 1.8.1.4 extracted from
- Examination of the importance of Pro-453 in human dihydrolipoamide dehydrogenase predicted from the three-dimensional structure (2006), Bull. Korean Chem. Soc., 27, 819-820.
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| P453V | 1650fold lower specific activity compared to the wild type enzyme | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Homo sapiens |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
mutant P453V shows a specific activity of 0.37 units/mg at the saturated substrate concentrations of 2 mM dihydrolipoamide and 3 mM NAD+ at 37°C in a 50 mM potassium phosphate buffer (pH 8.0) containing 1.5 mM EDTA | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dihydrolipoamide + NAD+ | - |
Homo sapiens | lipoamide + NADH + H+ | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dihydrolipoamide dehydrogenase | - |
Homo sapiens |
| dihydrolipoamide:NAD+ oxidoreductase | - |
Homo sapiens |
| E3 | - |
Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Homo sapiens | |
| NAD+ | - |
Homo sapiens | |
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Release 2023.1 (January 2023)
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