Abstract
ATP: nucleotide pyrophosphotransferase, obtained from Streptomyces adephospholyticus, characteristically transferred pyrophosphoryl group of ATP to 5'-purine nucleotides. 3'-, 2', 5'-, 3', 5'-Purine nucleotides, deoxy nucleotides, pyrimidine nucleotides or nucleosides were not pyrophosphate acceptors. Only ATP, dATP and A5P were active as pyrophosphate donor.
The properties of the enzyme with ATP (donor and acceptor) was examined. The enzyme required metal ions for its activity and an optimum ratio of concentration of metal ion to ATP was found. The optimum pH of the enzyme was 9.5 to 10.0 with Mg2+ and 7.5 to 8.0 with CO2+
