EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.7.11.1 | 5'-AMP | activity is increased several-fold upon preincubation with millimolar concentrations of 5'-AMP. Activation is enhanced by the presence of ATP | Saccharolobus solfataricus | |
2.7.11.1 | ADPribose | activity is increased several-fold upon preincubation with submicromolar concentrations of ADPribose. Activation is enhanced by the presence of ATP. ADP-ribose acts by evoking a conformational transition in the enzyme. Other mono- and di-nucleotides are ineffective | Saccharolobus solfataricus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.11.1 | - |
Saccharolobus solfataricus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.7.11.1 | T151A | activity with reduced carboxymethylated lysozyme is much lower than wild-type activity. The stoichiometry of autophosphorylation is roughly half that of the unmodified protein | Saccharolobus solfataricus |
2.7.11.1 | T151D | activity with reduced carboxymethylated lysozyme is much lower than wild-type activity. The stoichiometry of autophosphorylation is roughly half that of the unmodified protein | Saccharolobus solfataricus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.11.1 | Mg2+ | activity requires the presence of a divalent metal ion cofactor. Mn2+ is most effective at supporting protein kinase activity. Mg2+ is moderately effective, while Ca2+, Ni2+, and Zn2+ are ineffective as cofactors | Saccharolobus solfataricus | |
2.7.11.1 | Mn2+ | activity requires the presence of a divalent metal ion cofactor. Mn2+ is most effective at supporting protein kinase activity. Mg2+ is moderately effective, while Ca2+, Ni2+, and Zn2+ are ineffective as cofactors | Saccharolobus solfataricus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.11.1 | Saccharolobus solfataricus | Q97ZY9 | - |
- |
2.7.11.1 | Saccharolobus solfataricus P2 | Q97ZY9 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.11.1 | ATP + a protein | protein kinase activity, with a noticeable preference for phosphorylating proteins of acidic character. No activity with basic proteins such as histones or myelin basic protein. The protein kinase also can phosphorylate itself on serine and threonine residues. No autophosphorylation of the protein kinase can be detected prior to addition of exogenous substrate proteins. Thr-151 is a site of autophosphorylation, and that autophosphorylation of this residue enhances the catalytic efficiency of the enzyme | Saccharolobus solfataricus | ADP + a phosphoprotein | - |
? | |
2.7.11.1 | ATP + a protein | protein kinase activity, with a noticeable preference for phosphorylating proteins of acidic character. No activity with basic proteins such as histones or myelin basic protein. The protein kinase also can phosphorylate itself on serine and threonine residues. No autophosphorylation of the protein kinase can be detected prior to addition of exogenous substrate proteins. Thr-151 is a site of autophosphorylation, and that autophosphorylation of this residue enhances the catalytic efficiency of the enzyme | Saccharolobus solfataricus P2 | ADP + a phosphoprotein | - |
? | |
2.7.11.1 | ATP + casein | - |
Saccharolobus solfataricus | ADP + phopshorylated cysein | - |
? | |
2.7.11.1 | ATP + casein | - |
Saccharolobus solfataricus P2 | ADP + phopshorylated cysein | - |
? | |
2.7.11.1 | ATP + reduced carboxymethylated lysozyme | - |
Saccharolobus solfataricus | ADP + phopshorylated reduced carboxymethylated lysozyme | - |
? | |
2.7.11.1 | ATP + reduced carboxymethylated lysozyme | - |
Saccharolobus solfataricus P2 | ADP + phopshorylated reduced carboxymethylated lysozyme | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.11.1 | SSO0433 | locus name | Saccharolobus solfataricus |
2.7.11.1 | SsoPK5 | - |
Saccharolobus solfataricus |