Kinetic Properties and Equilibrium Constant of the Adenosine Triphosphate-Creatine Transphosphorylase-catalyzed Reaction
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چکیده
منابع مشابه
Kinetic properties and equilibrium constant of the adenosine triphosphate-creatine transphosphorylase-catalyzed reaction.
catalyzed by adenosine triphosphate-creatine transphosphorylase can be described by a reasonable kinetic scheme. It was shown that MgATPzis the “true substrate,” that the Michaelis constant is the dissociation constant of the enzyme-substrate complex, and that the pH-activity curve resembles a single ionization curve with pK N 6.5. It was of interest to study the kinetics of the reverse process...
متن کاملStudies on adenosine triphosphate transphosphorylases. II. Amino acid composition of adenosine triphosphate-creatine transphosphorylase.
Some of the physical and chemical properties of crystalline adenosine triphosphate-creatine transphosphorylase from rabbit muscle (1) have been previously described (2). In 1956, Friedberg reported on the amino acid composition of this enzyme (3). His data, however, were derived from analyses of only two samples hydrolyzed for the same time interval. Preliminary amino acid analyses from this la...
متن کاملThe enzymatic activity and inhibition of adenosine 5'-triphosphate-creatine transphosphorylase.
From our earlier rate measurements (l), it was not possible to develop a satisfactory kinetic scheme accounting for the dependence of reaction rate on the concentration of certain ions, such as Mg++ and Hf. Recently, however, we have found (2) that some of the anions which we were inadvertently introducing in the earlier work (e.g. in varying the concentration of Mg++ with the use of magnesium ...
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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1961
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)93996-7