An adenosine kinase mutation in baby hamster kidney cells causing increased sensitivity to adenosine.

A class of arabinosyladenine (araA)-resistant mutants of baby hamster kidney (BHK 21/C13) cells exhibits multiple phenotypes: resistance to araA and deoxyadenosine, extreme sensitivity to adenosine (Ado) and varying degrees of deficiency in adenosine kinase (AK) activity. One of these Ados/araAr strains, ara-S10d, was isolated without mutagenesis and was shown to possess about 59% level of the wild-type AK activity. The AK from ara-S10d had an altered Km and pH optimum and was stimulated by K+ cations. A number of Ados to Ador revertants were isolated from ara-S10d, and in all of the 7 examined, the AK activity was reduced to a nondetectable level. The altered kinetic parameters of the AK enzyme in ara-S10d cells suggest a mutation of the AK gene that leads to the synthesis of an altered enzyme. The loss of AK activity in the Ador revertants suggests an association of the enhanced Ado sensitivity to the AK mutation.