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Literature summary for 3.6.4.10 extracted from
- How potassium affects the activity of the molecular chaperone Hsc70 II. Potassium binds specifically in the ATPase active site (1995), J. Biol. Chem., 270, 2251-2257.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| 44-kDa wild-type Hsc70 ATPase fragment | Bos taurus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 44000 | - |
ATPase domain of Hsc70 | Bos taurus |
| 70000 | - |
- |
Bos taurus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Bos taurus | - |
ADP + phosphate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Bos taurus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + H2O = ADP + phosphate | highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin | Bos taurus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Bos taurus | ADP + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| eukaryotic Hsc70 ATPase | - |
Bos taurus |
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Release 2023.1 (January 2023)
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