Dinucleosidetetraphosphatase inhibition by Zn(II).

Almost complete inhibition of partially purified dinucleoside-tetraphosphatase (EC 3. 6. 1. 17) was observed with 5 microM Zn(II). The inhibition was reversed by EDTA and was time dependent, reaching a maximum after 5 min of incubation at 37 degrees C. Zn(II) behaved as a non-competitive inhibitor of the reaction, leaving unaltered the Km value for the enzyme towards diadenosine tetraphosphate. The cellular level of this compound may be directly related to the Zn(II) content since, besides the inhibition here described, Zn(II) has been reported by others to be an activator of the synthesis of diadenosine tetraphosphate by sheep liver lysyl- and phenylalanyl-t RNA synthetases.