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Literature summary for 1.1.1.14 extracted from
- alpha-Crystallin: an ATP-independent complete molecular chaperone toward sorbitol dehydrogenase (2005), Cell. Mol. Life Sci., 62, 599-605.
General Stability
| General Stability | Organism |
|---|---|
| complete renaturation, alpha-crystallin has the ability to elicit protein refolding. This action of alpha-crystallin appears not to be dependent on ATP as energy donor, but essentially associated with intrinsic structural features of this chaperone molecule | Bos taurus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
- |
Bos taurus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| lens | - |
Bos taurus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-fructose + NADH + H+ | - |
Bos taurus | D-sorbitol + NAD+ | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SDH | - |
Bos taurus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | - |
Bos taurus | |
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Release 2023.1 (January 2023)
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