In Escherichia coli W3110 polA1, an enzyme possessing the following catalytic properties has been found: (a) The enzyme catalyzes the formation of polydeoxyadenylate, polydeoxycytidylate, polydeoxyguanylate, and polydeoxythymidylate from corresponding deoxyribonucleoside diphosphates. The rate of formation of the polydeoxyribonucleotide containing deoxyadenylate, deoxycytidylate, deoxyguanylate, and deoxythymidylate is relatively slow. (b) The phosphorolysis of deoxyribonucleic acid and the exchange between inorganic phosphate and the terminal phosphate of deoxyribonucleoside diphosphates in the presence of the enzyme proceed at an extremely slow rate. (c) Polymerization of deoxyribonucleoside diphosphates requires the presence of manganous ion; magnesium ion is almost without effect on the reaction.
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W.T. Hsieh (1971) studied this question.