Abstract
Abstract The potency of inhibition of deoxyadenosine kinase by nucleotides of cytosine is dependent on the nature of the pentose moiety (deoxyribose g arabinose g ribose). Kinetic data suggest that deoxyadenosine (dAdo), deoxyguanosine (dGuo), and cytidine (Cyd) are substrates for dAdo kinase. The apparent Km values for these phosphate acceptors are: dAdo (0.7 mm), dGuo (1.1 mm), and Cyd (0.6 mm). The inhibition of deoxyadenosine kinase by dATP, dGTP, and dCTP appears to be noncompetitive with the phosphate acceptor and competitive with the phosphate donor (ATP). Kinetic analysis indicates that the reaction catalyzed by deoxyadenosine kinase follows a ping pong mechanism.
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