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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
3.2.2.20
750415
Selective base excision repair of DNA damage by the non-base-flipping DNA glycosylase AlkC
EMBO J.
37
63-74
2018
Bacillus cereus
29054852
3.2.2.20
750415
Selective base excision repair of DNA damage by the non-base-flipping DNA glycosylase AlkC
EMBO J.
37
63-74
2018
Pseudomonas fluorescens
29054852
3.2.2.20
646847
Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine
Biochemistry
21
1162-1169
1982
Escherichia coli
7041972
3.2.2.20
646847
Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine
Biochemistry
21
1162-1169
1982
no activity in Escherichia coli
7041972
3.2.2.20
646847
Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine
Biochemistry
21
1162-1169
1982
Escherichia coli BW 9062
7041972
3.2.2.20
646855
Different efficiencies of the Tag and AlkA DNA glycosylases from Escherichia coli in the removal of 3-methyladenine from single-stranded DNA
FEBS Lett.
397
127-129
1996
Escherichia coli
8941728
3.2.2.20
646865
The Bacillus subtilis counterpart of the mammalian 3-methyladenine DNA glycosylase has hypoxanthine and 1,N6,ethenoadenine as preferred substrates
J. Biol. Chem.
279
13601-13606
2004
Bacillus subtilis
14729667
3.2.2.20
646865
The Bacillus subtilis counterpart of the mammalian 3-methyladenine DNA glycosylase has hypoxanthine and 1,N6,ethenoadenine as preferred substrates
J. Biol. Chem.
279
13601-13606
2004
Homo sapiens
14729667
3.2.2.20
646865
The Bacillus subtilis counterpart of the mammalian 3-methyladenine DNA glycosylase has hypoxanthine and 1,N6,ethenoadenine as preferred substrates
J. Biol. Chem.
279
13601-13606
2004
Bacillus subtilis 168
14729667
3.2.2.20
670318
A new protein superfamily includes two novel 3-methyladenine DNA glycosylases from Bacillus cereus, AlkC and AlkD
Mol. Microbiol.
59
1602-1609
2006
Bacillus cereus
16468998
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