Kinetic analysis of inhibition of cAMP-dependent protein kinase catalytic subunit by the peptide-nucleoside conjugate AdcAhxArg6. Kuznetsov, A.; Uri, A.; Raidaru, G.; and Järv, J. Bioorganic chemistry, 32(6):527-35, 2004.
Kinetic analysis of inhibition of cAMP-dependent protein kinase catalytic subunit by the peptide-nucleoside conjugate AdcAhxArg6. [link]Website  abstract   bibtex   
Kinetic analysis of the inhibition of the phosphorylation of Kemptide, (LRRASLG), catalyzed by the catalytic subunit of cAMP-dependent protein kinase, by a peptide-nucleoside conjugate inhibitor AdcAhxArg6 was carried out over a wide range of ATP and peptide concentrations. A simple procedure was proposed for characterization of the interaction of this inhibitor with the free enzyme, and with the enzyme-ATP and enzyme-peptide complexes. The second-order rate constants, calculated from the steady-state reaction kinetics, were used for this analysis to avoid the complications related to the complex catalytic mechanism of the protein kinase catalyzed reaction.
@article{
 title = {Kinetic analysis of inhibition of cAMP-dependent protein kinase catalytic subunit by the peptide-nucleoside conjugate AdcAhxArg6.},
 type = {article},
 year = {2004},
 identifiers = {[object Object]},
 keywords = {Adenosine Triphosphate,Adenosine Triphosphate: chemistry,Catalysis,Cyclic AMP-Dependent Protein Kinases,Cyclic AMP-Dependent Protein Kinases: antagonists,Cyclic AMP-Dependent Protein Kinases: chemistry,Enzyme Inhibitors,Enzyme Inhibitors: chemistry,Enzyme Inhibitors: pharmacology,Kinetics,Molecular Structure,Nucleosides,Nucleosides: chemistry,Oligopeptides,Oligopeptides: chemistry,Peptides,Peptides: chemistry,Phosphorylation,Protein Subunits,Protein Subunits: antagonists & inhibitors,Protein Subunits: chemistry,Structure-Activity Relationship},
 pages = {527-35},
 volume = {32},
 websites = {http://www.ncbi.nlm.nih.gov/pubmed/15530993},
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 abstract = {Kinetic analysis of the inhibition of the phosphorylation of Kemptide, (LRRASLG), catalyzed by the catalytic subunit of cAMP-dependent protein kinase, by a peptide-nucleoside conjugate inhibitor AdcAhxArg6 was carried out over a wide range of ATP and peptide concentrations. A simple procedure was proposed for characterization of the interaction of this inhibitor with the free enzyme, and with the enzyme-ATP and enzyme-peptide complexes. The second-order rate constants, calculated from the steady-state reaction kinetics, were used for this analysis to avoid the complications related to the complex catalytic mechanism of the protein kinase catalyzed reaction.},
 bibtype = {article},
 author = {Kuznetsov, Aleksei and Uri, Asko and Raidaru, Gerda and Järv, Jaak},
 journal = {Bioorganic chemistry},
 number = {6}
}
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