Phosphorus nuclear-magnetic-resonance studies of a transition-state analogue complex of creatine kinase
- 1 December 1977
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 167 (3) , 827-829
- https://doi.org/10.1042/bj1670827
Abstract
31P NMR spectra of MgADP bound to rabbit skeletal muscle creatine kinase in the presence of creatine and NO3- ions show that there are 2 non-identical forms of the bound nucleotide. The sites have different affinities for the nucleotide. MgADP at the high affinity site is in slow exchange (k [rate] < 125 s-1 at 27.degree. C) with free MgADP.This publication has 10 references indexed in Scilit:
- Heterogeneity of rabbit muscle creatine kinase and limited proteolysis by proteinase KBiochemical Journal, 1977
- 31P nuclear magnetic resonance of bound substrates of arginine kinase reaction: chemical shifts in binary, ternary, quaternary, and transition state analog complexes.Journal of Biological Chemistry, 1977
- 31P NMR studies of the arginine kinase reaction. Equilibrium constants and exchange rates at stoichiometric enzyme concentration.Journal of Biological Chemistry, 1976
- Binding of adenosine 5'-diphosphate to creatine kinase. An investigation using intermolecular nuclear Overhauser effect measurementsBiochemistry, 1976
- Non-identical behaviour of the subunits of rabbit muscle creatine kinaseBiochimica et Biophysica Acta (BBA) - Enzymology, 1976
- Creatine kinase. Modification of the working enzymeBiochemical Journal, 1976
- TRANSITION STATE ANALOG INHIBITORS AND ENZYME CATALYSISAnnual Review of Biophysics and Bioengineering, 1976
- The interaction of 8-anilino-1-naphthalenesulfonate with creatine kinase. Evidence for cooperativitiy of nucleotide binding.1974
- Inhibition of adenosine 5′-triphosphate–creatine phosphotransferase by substrate–anion complexes. Evidence for the transition-state organization of the catalytic siteBiochemical Journal, 1971
- Thermodynamic Studies of the Formation and Ionization of the Magnesium(II) Complexes of ADP and ATP over the pH Range 5 to 91Journal of the American Chemical Society, 1966