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Literature summary for 3.6.4.10 extracted from
- Switches, catapults, and chaperones: Steady-state kinetic analysis of Hsp70-substrate interactions. [Erratum to document cited in CA143:262085] (2005), Biochemistry, 44, 13224.
No PubMed abstract available
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.052 | - |
ATP | - |
Escherichia coli |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | ATP binding drives the chaperone in one direction and peptide binding pushes the chaperone back in the opposite direction (and thus increases Km) | Escherichia coli | ADP + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DnaK | - |
Escherichia coli |
| Hsp70 chaperone | - |
Escherichia coli |
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