Activating Compound | Comment | Organism | Structure |
---|---|---|---|
cAMP | - |
Bos taurus |
Protein Variants | Comment | Organism |
---|---|---|
D170A | site-directed mutagenesis of the regulatory subunit RIalpha, the mutation selectively reduces the negative cooperativity between the cAMP- and C-recognition sites, i.e. the KD for the regulatory-catalytic subunit complex in the presence of cAMP is reduced by more than 12fold, without significantly compromising the high affinity of the regulatory subunit for both binding partners, conformational shifts upon mutation, and physiological implications of the dual functionality of the D170A mutant, overview | Bos taurus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | - |
Bos taurus | 5737 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the regulatory subunit of PKA inhibits its kinase activity by shielding the catalytic subunit from physiological substrates, Asp170 not only plays a pivotal role in controlling the local conformation of the phosphate binding cassette, where cAMP docks, but also significantly affects the long-range cAMP-dependent interaction network that extends from the phosphate binding cassette to the three major sites of C-recognition | Bos taurus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the regulatory subunit of PKA inhibits its kinase activity by shielding the catalytic subunit from physiological substrates, interdependence between the Asp170 relay site and the regulatory-catalytic subunit interaction interface | Bos taurus |
Synonyms | Comment | Organism |
---|---|---|
PKA | - |
Bos taurus |
protein kinase A | - |
Bos taurus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Bos taurus |