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A pyrimidine dimer-DNA glycosylase has been purified 20,000-fold from Micrococcus luteus. The enzyme is a single polypeptide chain with Mr = 18,000 that acts specifically on pyrimidine dimers, preferring those in double-stranded DNA to those in single-stranded DNA. The glycosylase cleaves the 5' residue of a pyrimidine dimer generating an apyrimidinic site and a mixed pyrimidine/pyrimidine nucleotide dimer. Under conditions of substrate excess, dimers containing a 5'-thymine are preferred to those with a 5'-cytosine residue. The glycosylase has an associated apyrimidinic/apurinic (AP) endonuclease that prefers apyrimidinic sites at the site of glycosylase action to either apurinic or apyrimidinic residues. This endonuclease is a Class I AP endonuclease in that it cleaves 3' to the AP site generating a 3'-deoxyribose moiety and a 5'-phosphate.
R H Grafstrom, and
L Park, and
L Grossman
January 1997,
Proceedings of the National Academy of Sciences of the United States of America,
R H Grafstrom, and
L Park, and
L Grossman
May 1981,
Proceedings of the National Academy of Sciences of the United States of America,
R H Grafstrom, and
L Park, and
L Grossman
June 1987,
Biochemistry,
R H Grafstrom, and
L Park, and
L Grossman
October 1981,
Journal of virology,
R H Grafstrom, and
L Park, and
L Grossman
April 1982,
The Journal of biological chemistry,
R H Grafstrom, and
L Park, and
L Grossman
June 1980,
Nature,
R H Grafstrom, and
L Park, and
L Grossman
January 1980,
Methods in enzymology,
R H Grafstrom, and
L Park, and
L Grossman
October 1987,
Biochemistry,
R H Grafstrom, and
L Park, and
L Grossman
January 1986,
Gene,
R H Grafstrom, and
L Park, and
L Grossman
September 1977,
The Journal of biological chemistry,
