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/°K.
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