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Literature summary for 2.7.11.1 extracted from

  • Haile, J.D.; Kennelly, P.J.
    The activity of an ancient atypical protein kinase is stimulated by ADP-ribose in vitro (2011), Arch. Biochem. Biophys., 511, 56-63.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
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
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

Cloned(Commentary)

Cloned (Comment) Organism
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Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
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
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

Metals/Ions

Metals/Ions Comment Organism Structure
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
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

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97ZY9
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-
Saccharolobus solfataricus P2 Q97ZY9
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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
-
?
ATP + casein
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Saccharolobus solfataricus ADP + phopshorylated cysein
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?
ATP + casein
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Saccharolobus solfataricus P2 ADP + phopshorylated cysein
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?
ATP + reduced carboxymethylated lysozyme
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Saccharolobus solfataricus ADP + phopshorylated reduced carboxymethylated lysozyme
-
?
ATP + reduced carboxymethylated lysozyme
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Saccharolobus solfataricus P2 ADP + phopshorylated reduced carboxymethylated lysozyme
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?

Synonyms

Synonyms Comment Organism
SSO0433 locus name Saccharolobus solfataricus
SsoPK5
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Saccharolobus solfataricus