DNA deoxyribophosphodiesterase.

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Abstract
A previously unrecognized enzyme acting on damaged termini in DNA is present in Escherichia coli. The enzyme catalyses the hydrolytic release of 2‐deoxyribose‐5‐phosphate from single‐strand interruptions in DNA with a base‐free residue on the 5′ side. The partly purified protein appears to be free from endonuclease activity for apurinic/apyrimidinic sites, exonuclease activity and DNA 5′‐phosphatase activity. The enzyme has a mol. wt of approximately 50,000‐55,000 and has been termed DNA deoxyribophosphodiesterase (dRpase). The protein presumably is active in DNA excision repair to remove a sugar‐phosphate residue from an endonucleolytically incised apurinic/apyrimidinic site, prior to gap filling and ligation.