Kinetic analysis of inhibition of cAMP-dependent protein kinase catalytic subunit by the peptide-nucleoside conjugate AdcAhxArg6. Kuznetsov, A., Uri, A., Raidaru, G., & 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]](https://bibbase.org/img/filetypes/link.svg "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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