1988
DOI: 10.1159/000469119
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Bovine Skeletal Muscle Adenosine Deaminase: Kinetic and Thermodynamic Studies

Abstract: Adenosine deaminase from bovine skeletal muscle catalyzes the hydrolytic deamination of adenosine to inosine and ammonia via an ordered Uni-Bi mechanism, if water is not considered as a true second substrate, as deduced from the inhibition pattern products. The inhibition constants (K(i)) obtained for inosine and ammonia were 316 jxmol/l and 2 mol/1, respectively. The activation energy of the reaction has been calculated as 10 kcal/mol, ΔH* and ΔF* as 7.9 and 15.6 kcal/mol, respectively, and ΔS* as-23 cal/mol/… Show more

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“…Likewise, with a kcat of 375 s −1 and a kcat/Km of 1.4 ×10 7 M −1 s −1 , ADA catalysis is close to being encounter‐limited . Given its apparent simplicity and catalytic efficiency, ADA has been the focus of extensive investigations in an effort to understand its substrate specificity and enzymatic stability, the kinetic mechanism and the Michaelis–Menten parameters of the ADA reaction, the action of different inhibitors, and the comparison of several physicochemical properties of the enzyme from different sources …”
Section: Ada As An Enzyme Structural and Catalytic Characteristicsmentioning
confidence: 99%
“…Likewise, with a kcat of 375 s −1 and a kcat/Km of 1.4 ×10 7 M −1 s −1 , ADA catalysis is close to being encounter‐limited . Given its apparent simplicity and catalytic efficiency, ADA has been the focus of extensive investigations in an effort to understand its substrate specificity and enzymatic stability, the kinetic mechanism and the Michaelis–Menten parameters of the ADA reaction, the action of different inhibitors, and the comparison of several physicochemical properties of the enzyme from different sources …”
Section: Ada As An Enzyme Structural and Catalytic Characteristicsmentioning
confidence: 99%