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Literature summary for 1.4.1.1 extracted from
- Salt-dependent conformational changes of alanine dehydrogenase from Halobacterium salinarium (1980), FEBS Lett., 112, 183-185.
General Stability
| General Stability | Organism |
|---|---|
| 6 M urea, complete inactivation and total loss of both alpha-helic and beta-structure | Halobacterium salinarum |
| inactivation after removal of salt | Halobacterium salinarum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Halobacterium salinarum | - |
- |
- |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| partial renaturation of the enzyme denatured by 6 M urea is linked to a corresponding reappearance of alpha-helix and of beta-structure | Halobacterium salinarum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-Ala + H2O + NAD+ | - |
Halobacterium salinarum | pyruvate + NH3 + NADH | - |
r |  |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Halobacterium salinarum | |
| NADH | - |
Halobacterium salinarum | |
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