Protein Variants | Comment | Organism |
---|---|---|
K53R | spectral and redox properties of FAD in the mutant enzyme as well as the interaction of the flavin with bound NAD+ are profoundly affected by the mutation, K53R does not catalyze either the dihydrolipoamide-NAD+ or the NADH-lipoamide reactions except at very low concentrations of reducing substrate. The absorbance spectrum in the visible and near-ultraviolet is little changed from that of wild-type enzyme, in contrast to wild-type enzyme the spectrum of K53R is sensitive to pH. Unlike the wild-type enzyme, the binding of beta-NAD+ to K53R alters the spectrum | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dihydrolipoamide + NAD+ | - |
Escherichia coli | lipoamide + NADH | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Escherichia coli |