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@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},
 id = {aed8cbe7-c9e6-3fd4-9760-8f5a5c09f96b},
 created = {2016-01-28T12:02:01.000Z},
 file_attached = {false},
 profile_id = {dd94ede8-8057-3021-b774-e8e1019e0a90},
 last_modified = {2016-01-28T12:02:03.000Z},
 read = {false},
 starred = {false},
 authored = {true},
 confirmed = {true},
 hidden = {false},
 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}
}