Bovine skeletal muscle adenosine deaminase: kinetic and thermodynamic studies.
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 (Ki) obtained for inosine and ammonia were 316 mumol/l and 2 mol/l, respectively. The activation energy of the reaction has been calculated as 10 kcal/mol, delta H* and delta F* as 7.9 and 15.6 kcal/mol, respectively, and delta S* as -23 cal/mol/degrees K.
Martinez
C
C
Departamento de Bioquímica y Tecnología de los Alimentos, Facultad de Veterinaria, Universidad de León, España.
Zumalacárregui
J M
JM
Diez
V
V
D000243:Adenosine Deaminase / Q000378:metabolism*; D058892:Adenosine Deaminase Inhibitors; D000641:Ammonia / Q000494:pharmacology; D000818:Animals; D002417:Cattle; D007288:Inosine / Q000494:pharmacology; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D009700:Nucleoside Deaminases / Q000378:metabolism*; D013696:Temperature; D013816:Thermodynamics
D058892:Adenosine Deaminase Inhibitors; D007288:Inosine; D000641:Ammonia; D009700:Nucleoside Deaminases; D000243:Adenosine Deaminase