EC Number   |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
|---|
   3.2.2.21 | 749893 |
Base excision repair enzymes protect abasic sites in duplex DNA from interstrand cross-links |
Biochemistry |
54 |
1849-1857 |
2015 |
Escherichia coli |
25679877 |
| 3.2.2.21 | 749893 |
Base excision repair enzymes protect abasic sites in duplex DNA from interstrand cross-links |
Biochemistry |
54 |
1849-1857 |
2015 |
Homo sapiens |
25679877 |
| 3.2.2.21 | 749911 |
Evaluating the substrate selectivity of alkyladenine DNA glycosylase the synergistic interplay of active site flexibility and water reorganization |
Biochemistry |
55 |
798-808 |
2016 |
Homo sapiens |
26765542 |
| 3.2.2.21 | 751390 |
QM/MM study of the reaction catalyzed by alkyladenine DNA glycosylase examination of the substrate specificity of a DNA repair enzyme |
J. Phys. Chem. B |
121 |
11096-11108 |
2017 |
Homo sapiens |
29148771 |
| 3.2.2.21 | 646890 |
1,N(2)-ethenoguanine, a mutagenic DNA adduct, is a primary substrate of Escherichia coli mismatch-specific uracil-DNA glycosylase and human alkylpurine-DNA-N-glycosylase |
J. Biol. Chem. |
277 |
26987-26993 |
2002 |
Homo sapiens |
12016206 |
| 3.2.2.21 | 646885 |
3-Methyladenine DNA glycosylases: structure, function, and biological importance |
Bioessays |
21 |
668-676 |
1999 |
Arabidopsis thaliana |
10440863 |
| 3.2.2.21 | 646885 |
3-Methyladenine DNA glycosylases: structure, function, and biological importance |
Bioessays |
21 |
668-676 |
1999 |
Saccharomyces cerevisiae |
10440863 |
| 3.2.2.21 | 646885 |
3-Methyladenine DNA glycosylases: structure, function, and biological importance |
Bioessays |
21 |
668-676 |
1999 |
Escherichia coli |
10440863 |
| 3.2.2.21 | 646885 |
3-Methyladenine DNA glycosylases: structure, function, and biological importance |
Bioessays |
21 |
668-676 |
1999 |
Homo sapiens |
10440863 |
| 3.2.2.21 | 646885 |
3-Methyladenine DNA glycosylases: structure, function, and biological importance |
Bioessays |
21 |
668-676 |
1999 |
Mus musculus |
10440863 |
