Ion Binding by Adenosine Triphosphate-Creatine Phosphotransferase
نویسندگان
چکیده
منابع مشابه
Adenosine Triphosphate : Guanosine Monophosphate Phosphotransferase
Several laboratories have reported studies on individual enzymes that belong to the general class of adenosine triphosphate : nucleoside monophosphate phosphotransferases (EC 2.7.4.4), commonly termed nucleoside monophosphate kinases (l-7). Studies with partially purified enzyme preparations have indicated that a variety of nucleoside monophosphates can serve as alternative substrates for nucle...
متن کاملThe mechanism of the reaction catalysed by adenosine triphosphate-creatine phosphotransferase.
1. The forward and reverse reactions catalysed by ATP-creatine phosphotransferase have been studied kinetically at pH8.0 in the presence and absence of products, under conditions in which the free Mg(2+) concentration was maintained constant at 1mm. Thus at fixed pH the reaction may be considered as being bireactant and expressed as:MgATP(2-)+creatine(0)right harpoon over left harpoonMgADP(-)+p...
متن کاملIsotope exchange studies of the mechanism of the reaction catalyzed by adenosine triphosphate: creatine phosphotransferase.
The mechanism of the reaction catalyzed by adenosine triphosphate : creatine phosphotransferase has been studied by measuring the initial velocities of the exchange with isotopically labeled substrates. The rates of the creatine-phosphocreatine, ATP-ADP, and ADP-ATP exchanges at equilibrium are approximately equal and dependent on the concentrations of Mg2+ and ADP”. The ADP-ATP exchange rate i...
متن کاملKinetic Studies of the Reverse Reaction Catalysed by Adenosine Triphosphate-creatine Phosphotransferase. the Inhibition by Magnesium Ions and Adenosine Diphosphate.
1. Kinetic investigations of the reaction catalysed by ATP-creatine phosphotransferase have been carried out. 2. No firm conclusions could be reached about the reaction of Mg(2+) at the nucleotide-binding site of the enzyme. The value of the kinetic constant for this reaction depends on the value used for the apparent stability constant of the metal ion-nucleotide complex and, to a smaller exte...
متن کاملPurification and properties of adenosine triphosphate-creatine phosphotransferase from muscle of the dogfish Scylliorhinus canicula.
1. Creatine kinase occurs in high concentration in the soluble proteins of dogfish muscle. A fourfold purification gives essentially pure enzyme but with a low specific activity. This appears to be a property of the native enzyme and not a result of the isolation procedures used. 2. The amino acid composition is similar to that of other phosphagen kinases, but the enzyme differs from mammalian ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1966
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)96375-1