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Literature summary for 2.7.13.3 extracted from
- The two active sites of thermotoga maritima CheA dimers bind ATP with dramatically different affinities (2009), Biochemistry, 48, 6412-6422 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Thermotoga maritima |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermotoga maritima | Q56310 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermotoga maritima |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + protein L-histidine | the two active sites of CheA homodimers exhibit large differences in their interactions with ATP | Thermotoga maritima | ADP + protein N-phospho-L-histidine | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | - |
Thermotoga maritima |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CheA | - |
Thermotoga maritima |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | CheA is a central component of the chemotaxis signal transduction pathway that allows prokaryotic cells to control their movements in response to environmental cues | Thermotoga maritima |
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Release 2023.1 (January 2023)
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