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Literature summary for 1.8.1.4 extracted from
- Characterization of lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S (1995), Biochemistry, 34, 11757-11765.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C44S | 0.003% of the activity of wild-type enzyme with NAD+ and dihydrolipoamide. Enzyme is capable to catalyze reactions with NADH as electron donor and ferricyanide, thio-NAD+, 2,6-dichlorophenol indophenol and O2 as electron acceptor. The fluorescence of FAD in oxidized wild-type enzyme is markedly temperature dependent, while the fluorescence of FAD in mutants C44S and C49S is independent of temperature | Escherichia coli |
| C49S | 0.012% of the activity of wild-type enzyme with NAD+ and dihydrolipoamide. Enzyme is capable to catalyze reactions with NADH as electron donor and ferricyanide, thio-NAD+, 2,6-dichlorophenol indophenol and O2 as electron acceptor. The fluorescence of FAD in oxidized wild-type enzyme is markedly temperature dependent, while the fluorescence of FAD in mutants C44S and C49S is independent of temperature | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 ferricyanide + NADH | activity with wild-type enzyme and mutant enzymes C44S and C49S | Escherichia coli | 2 ferrocyanide + NAD+ + H+ | - |
? |  |
| dihydrolipoamide + NAD+ | mutant enzymes C44S and C49S show minute activity | Escherichia coli | lipoamide + NADH | - |
? | |
| O2 + NADH | activity with wild-type enzyme and mutant enzymes C44S and C49S | Escherichia coli | ? | - |
? | |
| oxidized 2,6-dichlorophenolindophenol + NADH | activity with wild-type enzyme and mutant enzymes C44S and C49S | Escherichia coli | ? + NAD+ | - |
? | |
| thio-NAD+ + NADH | activity with wild-type enzyme and mutant enzymes C44S and C49S | Escherichia coli | thio-NADH + NAD+ | - |
? | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | the fluorescence of FAD in oxidized wild-type enzyme is markedly temperature dependent, while the fluorescence of FAD in mutants C44S and C49S is independent of temperature | Escherichia coli | |
| NAD+ | - |
Escherichia coli | |
| NADH | - |
Escherichia coli | |
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