Kinetics of creatine phosphokinase and adenylate kinase. A two-dimensional NMR analysis.
The kinetics of creatine phosphokinase and adenylate kinase catalyzed reactions were studied at equilibrium by two-dimensional Fourier transform phosphorus-31 nuclear magnetic resonance. For the creatine phosphokinase reaction, a pseudo-first-order rate constant of 0.29 s-1 was determined for the transfer of a phosphate group from adenosine triphosphate to creatine phosphate. For the adenylate kinase reaction two slow rate processes were required to describe the experimental results. The conversion of adenosine diphosphate to adenosine monophosphate was found to have a pseudo-first-order rate constant of 1.2 s-1, whereas that for the release of adenosine triphosphate from its enzyme complex occurred at a rate of 14 s-1.
D000227:Adenine Nucleotides / Q000378:metabolism; D000263:Adenylate Kinase / Q000378:metabolism*; D000818:Animals; D003402:Creatine Kinase / Q000378:metabolism*; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008433:Mathematics; D009132:Muscles / Q000201:enzymology; D010770:Phosphotransferases / Q000378:metabolism*; D011817:Rabbits
D000227:Adenine Nucleotides; D010770:Phosphotransferases; D003402:Creatine Kinase; D000263:Adenylate Kinase