Cloned (Comment) | Organism |
---|---|
overexpression in Escherichia coli | Sulfolobus acidocaldarius |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sulfolobus acidocaldarius | P35028 | - |
- |
Sulfolobus acidocaldarius DSM 639 | P35028 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + AMP | - |
Sulfolobus acidocaldarius | 2 ADP | - |
r | |
ATP + AMP | - |
Sulfolobus acidocaldarius DSM 639 | 2 ADP | - |
r |
Subunits | Comment | Organism |
---|---|---|
More | investigation of the oligomerization behaviour of the recombinant enzyme. The preferred native form of the adenylate kinase is a homotrimer, whose existence is detected by a specific MALDI-MS strategy, correlating with the published results on adenylate oligomerization using X-ray structure analysis | Sulfolobus acidocaldarius |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ADP | the adenylate kinase protein preparation contains non-covalently bound ADP | Sulfolobus acidocaldarius |