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Literature summary for 3.6.4.10 extracted from
- The Agrobacterium tumefaciens DnaK: ATPase cycle, oligomeric state and chaperone properties (2008), Int. J. Biochem. Cell Biol., 40, 804-812.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| V431F | mutant is unable to suppress the thermosensitivity of an Escherichia coli dnak103 deletion strain. Mutant is able to prevent the thermal aggregation of malate dehydrogenase | Agrobacterium tumefaciens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Agrobacterium tumefaciens | - |
isoform DnaK | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | ATP hydrolysis is the rate limiting step in the ATPase cycle of DnaK | Agrobacterium tumefaciens | ADP + phosphate | - |
? |  |
| additional information | DnaK is very effective in preventing thermal aggregation of malate dehydrogenase | Agrobacterium tumefaciens | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the C-terminal alpha-helical subdomain is involved in higher order associations, while the substrate binding domain is possibly involved in dimerisation | Agrobacterium tumefaciens |
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Release 2023.1 (January 2023)
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