31P NMR studies of enzyme-bound substrates of rabbit muscle pyruvate kinase. Equilibrium constants, exchange rates, and NMR parameters.
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منابع مشابه
31P NMR of enzyme-bound substrates of rabbit muscle creatine kinase. Equilibrium constants, interconversion rates, and NMR parameters of enzyme-bound complexes.
The reaction catalyzed by rabbit muscle creatine kinase ATP + creatine in equilibrium ADP + P-creatine has been investigated by 31P NMR. At pH 8.0 and 4 degrees C, the equilibrium constant of the overall reaction [P1][P2]/[S1] [S2] is found to be 0.08, while that for the interconversion step between enzyme-bound substrates and products [E.P1. P2]/[E.S1.S2] is estimated to be approximately 1; th...
متن کامل31P NMR Studies of the Arginine Kinase Reaction EQUILIBRIUM CONSTANTS AND EXCHANGE RATES AT STOICHIOMETRIC
The arginine kinase reaction, the reversible transfer of the terminal phosphoryl group of ATP to L-arginine, has been investigated by the technique of 31P NMR at catalytic and stoichiometric concentrations of the enzyme. Three of the four substrates, ATP, ADP, and P-arginine produce easily distinguishable resonances in the 31P NMR spectrum, thus permitting a determination of equilibrium constan...
متن کامل31P NMR studies of the arginine kinase reaction. Equilibrium constants and exchange rates at stoichiometric enzyme concentration.
The arginine kinase reaction, the reversible transfer of the terminal phosphoryl group of ATP to L-arginine, has been investigated by the technique of 31P NMR at catalytic and stoichiometric concentrations of the enzyme. Three of the four substrates, ATP, ADP, and P-arginine produce easily distinguishable resonances in the 31P NMR spectrum, thus permitting a determination of equilibrium constan...
متن کامل31P NMR studies of the structure of cation-nucleotide complexes bound to porcine muscle adenylate kinase.
The paramagnetic effects on the spin-relaxation rates of 31P nuclei in complexes of porcine muscle adenylate kinase with ATP, GTP, GDP, and AMP were measured in the presence of two dissimilar activating paramagnetic cations, Mn(II) and Co(II), to examine the structures of the enzyme-bound complexes. Experiments were performed exclusively on enzyme-bound complexes to limit contributions to obser...
متن کامل7Li, 31P, and 1H NMR studies of interactions between ATP, monovalent cations, and divalent cation sites on rabbit muscle pyruvate kinase.
The interactions between ATP, monovalent cations, and divalent cations on rabbit muscle pyruvate kinase have been examined using 7Li, 31P, and 1H nuclear magnetic resonance. Water proton nuclear relaxation studies are consistent with the binding of Li+ to the K+ site on pyruvate kinase with an affinity of 120 mM in the absence of substrates and 16 mM in the presence of P-enolpyruvate. Titration...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1979
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)30127-8