doi: 10.1002/j.1460-2075.1988.tb03240.x.
DNA deoxyribophosphodiesterase
Affiliations
- PMID: 2850170
- PMCID: PMC454866
- DOI: 10.1002/j.1460-2075.1988.tb03240.x
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DNA deoxyribophosphodiesterase
EMBO J.
1988 Nov.
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.
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