Kinetic analysis of inhibition of cAMP-dependent protein kinase catalytic subunit by the peptide-nucleoside conjugate AdcAhxArg6.
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.
Kuznetsov
Aleksei
A
Institute of Organic and Bioorganic Chemistry, University of Tartu, 2 Jakobi Str, 51014, Estonia.
Uri
Asko
A
Raidaru
Gerda
G
Järv
Jaak
J
D000255:Adenosine Triphosphate / Q000737:chemistry; D002384:Catalysis; D017868:Cyclic AMP-Dependent Protein Kinases / Q000037:antagonists & inhibitors* / Q000737:chemistry*; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D007700:Kinetics; D015394:Molecular Structure; D009705:Nucleosides / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D010766:Phosphorylation; D021122:Protein Subunits / Q000037:antagonists & inhibitors / Q000737:chemistry; D013329:Structure-Activity Relationship
D004791:Enzyme Inhibitors; D009705:Nucleosides; D009842:Oligopeptides; D010455:Peptides; D021122:Protein Subunits; C037642:kemptide; D000255:Adenosine Triphosphate; D017868:Cyclic AMP-Dependent Protein Kinases