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. 1974 Sep;71(9):3649-53.
doi: 10.1073/pnas.71.9.3649.

An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues

T Lindahl

An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues

T Lindahl. Proc Natl Acad Sci U S A. 1974 Sep.

Abstract

An enzyme that liberates uracil from single-stranded and double-stranded DNA containing deaminated cytosine residues and from deoxycytidylate-deoxyuridylate copolymers in the absence of Mg(++) has been purified 30-fold from cell extracts of E. coli. The enzyme does not release uracil from deoxyuridine, dUMP, uridine, or RNA, nor does it liberate the normally occurring pyrimidine bases, cytosine and thymine, from DNA. The enzymatic cleavage of N-glycosidic bonds in DNA occurs without concomitant cleavage of phosphodiester bonds, resulting in the formation of free uracil and DNA strands of unaltered chain length that contain apyrimidinic sites as reaction products. The enzyme may be active in DNA repair, converting deaminated dCMP residues to an easily repairable form.

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References

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    1. J Biol Chem. 1974 Mar 10;249(5):1530-5 - PubMed
    1. Proc Natl Acad Sci U S A. 1974 May;71(5):2022-6 - PubMed
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