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Literature summary extracted from
- alpha-Crystallin: an ATP-independent complete molecular chaperone toward sorbitol dehydrogenase (2005), Cell. Mol. Life Sci., 62, 599-605.
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 1.1.1.14 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.1.14 | Bos taurus | - |
- |
- |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 1.1.1.14 | - |
Bos taurus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.1.1.14 | lens | - |
Bos taurus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.14 | D-fructose + NADH + H+ | - |
Bos taurus | D-sorbitol + NAD+ | - |
? |  |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.1.14 | SDH | - |
Bos taurus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.14 | NADH | - |
Bos taurus | |
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Release 2023.1 (January 2023)
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