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1,2-propanediol-DNA + H2O
?
-
-
-
?
1,3-propanediol-DNA + H2O
?
-
-
-
?
1,N6-ethenoadenine residues in alkylated DNA + H2O
ethenoadenine + DNA
3-methyladenine residues in alkylated DNA + H2O
3-methyladenine + DNA
-
-
-
-
?
7-methylguanine residues in alkylated DNA + H2O
7-methylguanine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyl-2'-deoxyadenosine + 3-deaza-3-methyl-2'-deoxyadenosine + DNA
the sequences of the oligos used in the assay are 5'-CGATAGCATCCTYCCTTCTCTCCAT-3', where Y is the location of the lesion base, and 5'-ATGGAGAGAAGGZAGGATGCTATCG-3' for the complementary strand, where Z is the base opposite the lesion
-
-
?
alkylated DNA + H2O
3-methyladenine + 3-methylguanine + 7-methyladenine + 7-methylguanine + DNA
alkylated DNA + H2O
3-methyladenine + 3-methylguanine + 7-methylguanine + 7-methyladenine + ?
-
AlkA has significant glycosylase activity towards each of the normal bases in DNA. AlkA binds nonspecifically to DNA and neither mismatches nor 7-methylguanine lesions are specifically recognized in the ground state
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + 3-methylguanine
-
AlkD has high activity towards 7-methylguanine but removes 3-methylguanine more slowly as compared with Escherichia coli AlkA
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + 7-methyladenine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + ?
-
-
ratio of 3-methyladenine/7-methylguanine is 29:1 for wild-type enzyme, 24:1 for mutant enzyme N169S and 26:1 for mutant enzyme N169A, no production of 7-methylguanine is detected with mutant enzyme N169D
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + DNA
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + hypoxanthine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + 1,N6-ethenoadenine + hypoxanthine + DNA
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
alkylated DNA + H2O
3-methyladenine + ?
-
-
-
?
alkylated DNA + H2O
3-methyladenine + N3-methylcytosine + 1,N6-ethenoadenine + DNA
-
-
excision of N3-methylcytosine is about twice as fast as excision of 3-methyladenine, and the rate for 1,N6-ethenoadenine is further 5-10 times higher
-
?
alkylated DNA + H2O
7-methyladenine + 7-methylguanine + 3-methyladenine + 3-methylguanine + purine + 6-chloropurine + xanthine + DNA
-
7-methylguanine is cleaved the most quickly
-
?
alkylated DNA + H2O
?
-
the efficiency of 3-methyladenine and 3-methylguanine removal was 510 times slower for Mag1 than for Escherichia coli AlkA whereas the rate of 7-methylguanine removal is similar to the two enzymes
-
-
?
alkylated DNA, treated with N-methyl-N'-nitro-N-nitrosoguanidine + H2O
?
DNA treated with beta-[3H]propiolactone + H2O
N1-(carboxyethyl)adenine + N7-(carboxymethyl)guanine
-
-
-
-
?
duplex oligonucleotide substrate containing ethenoadenine + H2O
ethenoadenine + oligonucleotide
-
-
-
?
duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine + H2O
ethenoadenine + hypoxanthine + oligonucleotide
ethanol-DNA + H2O
?
best substrate
-
-
?
ethylene glycol-DNA + H2O
?
-
-
-
?
glycerol-DNA + H2O
?
-
-
-
?
methanol-DNA + H2O
?
-
-
-
?
propanol-DNA + H2O
?
-
-
-
?
synthetic oligosaccharide + H2O
?
-
synthetic oligosaccharide containing a single ethano or etheno adduct (3,N4-ethanocytosine, 1,N6-ethanoadenine, 3,N4-ethenocytosine or 1,N6-ethenoadenine), 20fold lower excision activity towards 3,N4-ethanocytosine and 1,N6-ethanoadenine than that towards their structurally analogous 3,N4-ethenocytosine or 1,N6-ethenoadenine. The enzyme is capable of excising the ethano base paired with any of the four natural bases
-
-
?
additional information
?
-
1,N6-ethenoadenine residues in alkylated DNA + H2O
ethenoadenine + DNA
-
-
-
-
?
1,N6-ethenoadenine residues in alkylated DNA + H2O
ethenoadenine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 3-methylguanine + 7-methyladenine + 7-methylguanine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 3-methylguanine + 7-methyladenine + 7-methylguanine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + DNA
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
-
646845, 646846, 646847, 646848, 646851, 646855, 646872, 646873, 646874, 646876, 646877, 646878, 646880, 646883, 646884, 646885, 646888, 646891, 646892 -
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
calf thymus DNA
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
DNA repair enzyme, inducible base excision repair pathway of DNA alkylation damage
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
DNA repair enzyme, inducible base excision repair pathway of DNA alkylation damage
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
induced by cell exposure to sublethal doses of alkylating agents, important role in the excision of base damage from single-stranded regions transiently formed in DNA during transcription and replication
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
inducible pathway for repair of DNA damaged by simple alkylating agents such as methylmethanesulfonate and N-methyl-N'-nitro-N-nitrosoguanidine
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
DNA repair enzyme, inducible base excision repair pathway of DNA alkylation damage
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
inducible pathway for repair of DNA damaged by simple alkylating agents such as methylmethanesulfonate and N-methyl-N'-nitro-N-nitrosoguanidine
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
short-patch base excision repair pathway, repair of alkylation and oxidative DNA damage
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
cellular repair of alkylated DNA base modifications
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
binds mismatch base-pairs in DNA
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA
-
-
-
-
?
alkylated DNA, treated with N-methyl-N'-nitro-N-nitrosoguanidine + H2O
?
-
-
-
-
?
alkylated DNA, treated with N-methyl-N'-nitro-N-nitrosoguanidine + H2O
?
-
-
-
-
?
duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine + H2O
ethenoadenine + hypoxanthine + oligonucleotide
-
-
-
-
?
duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine + H2O
ethenoadenine + hypoxanthine + oligonucleotide
-
-
-
-
?
additional information
?
-
-
excises alkylated bases only
-
-
?
additional information
?
-
-
AlkD is involved exclusively in the repair of alkylation damage
-
-
?
additional information
?
-
-
no detectable affinity for hypoxanthine, 1,N6-ethenoadenine, 8-oxoguanine and 5-formyluracil
-
-
?
additional information
?
-
-
AlkD does not excise 1,N6-ethenoadenine
-
-
?
additional information
?
-
the enzyme isoform AlkA2 possesses no activity towards 1,N6-ethenoadenine and hypoxanthine in alkylated DNA
-
-
?
additional information
?
-
-
the enzyme isoform AlkA2 possesses no activity towards 1,N6-ethenoadenine and hypoxanthine in alkylated DNA
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
removes alkylation damage from duplex and single stranded DNA
-
-
?
additional information
?
-
-
releases 3-methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, O2-methylcytosine, 7-(2-chloroethyl)guanine, 7-(2-hydroxyethyl)guanine, 7-(2-ethoxyethyl)guanine, 1,N6-ethenoadenine, hypoxanthine, adenine, guanine, thymine and cytosine from damaged and normal DNA, 3-ethenoguanine and 8-oxoguanine are not released
-
-
?
additional information
?
-
-
excises N7 guanine adducts completely, also capable of removing normal base residues from DNA
-
-
?
additional information
?
-
-
also capable to relase xanthine and oxanine, guanine lesions induced by nitrosation
-
-
?
additional information
?
-
-
with sulfur mustard treated DNA as substrate enzyme releases 7-hydroxyethylthioethyl guanine and 3-hydroxyethylthioethyl adenine, can also release carboxyethylate purines from DNA
-
-
?
additional information
?
-
-
enzyme cleaves pBR322 and pAlk10 plasmids, excises adducts formed by chloroacetaldehyde, acrolein and croton aldehyde but is not able to excise malionaldehyde and bulky p-benzochinone adducts
-
-
?
additional information
?
-
-
enzyme releases N1-(carboxyethyl)adenine and N7-(carboxymethyl)guanine from DNA treated with beta-propiolactone, but does not release the aflatoxin B-1 adduct at N-7 of guanine, release of 3-methyladenine from single-stranded DNA is 9% of the rate from double-stranded DNA, enzyme will not release 2,6-diamino-4-hydroxy-5-(N-methylformamido)pyrimidine, the alkali-induced derivative of 7-methylguanine, in which the imidazole ring is opened
-
-
?
additional information
?
-
-
enzyme also excises thymine residues oxidized in the methyl group like 5-formyluracil and 5-hydroxymethyluracil
-
-
?
additional information
?
-
-
repairs 5-formyluracil, a major thymine lesion produced by reactive oxygen radicals and photosensitized oxidation, 5-hydroxymethyluracil, another major thymine methyl oxidation product, is not a substrate
-
-
?
additional information
?
-
-
repairs 5-formyluracil, a major thymine lesion produced by reactive oxygen radicals and photosensitized oxidation, 5-hydroxymethyluracil, another major thymine methyl oxidation product, is not a substrate
-
-
?
additional information
?
-
-
the enzyme is induced in response to DNA alkylation, and it protects cells from alkylated nucleobases by catalyzing their excision
-
-
?
additional information
?
-
-
the enzyme binds preferentially DNA ends, more tightly than hypoxanthine lesions, exhibits significant product inhibition under multiple-turnover conditions, and binds approximately 10fold more tightly to an abasic site than to a hypoxanthine lesion site
-
-
?
additional information
?
-
the enzyme has little activity on correctly base-paired adenine. N3-deazaadenine is not substantially cleaved opposite cytosine or thymidine
-
-
?
additional information
?
-
-
the enzyme has little activity on correctly base-paired adenine. N3-deazaadenine is not substantially cleaved opposite cytosine or thymidine
-
-
?
additional information
?
-
the enzyme is able to hydrolyze O-glycosidic bonds in addition to N-glycosyl bonds
-
-
?
additional information
?
-
-
the enzyme is able to hydrolyze O-glycosidic bonds in addition to N-glycosyl bonds
-
-
?
additional information
?
-
-
repairs 5-formyluracil, a major thymine lesion produced by reactive oxygen radicals and photosensitized oxidation, 5-hydroxymethyluracil, another major thymine methyl oxidation product, is not a substrate
-
-
?
additional information
?
-
-
enzyme releases N1-(carboxyethyl)adenine and N7-(carboxymethyl)guanine from DNA treated with beta-propiolactone, but does not release the aflatoxin B-1 adduct at N-7 of guanine, release of 3-methyladenine from single-stranded DNA is 9% of the rate from double-stranded DNA, enzyme will not release 2,6-diamino-4-hydroxy-5-(N-methylformamido)pyrimidine, the alkali-induced derivative of 7-methylguanine, in which the imidazole ring is opened
-
-
?
additional information
?
-
-
enzyme cleaves pBR322 and pAlk10 plasmids, excises adducts formed by chloroacetaldehyde, acrolein and croton aldehyde but is not able to excise malionaldehyde and bulky p-benzochinone adducts
-
-
?
additional information
?
-
-
repairs 5-formyluracil, a major thymine lesion produced by reactive oxygen radicals and photosensitized oxidation, 5-hydroxymethyluracil, another major thymine methyl oxidation product, is not a substrate
-
-
?
additional information
?
-
-
also capable to relase xanthine and oxanine, guanine lesions induced by nitrosation
-
-
?
additional information
?
-
-
removes N-alkylpurine damage, unrepaired DNA damage leads to carcinogenesis, cell death, and aging, also releases 1,N6-ethenoadenine
-
-
?
additional information
?
-
-
removes N-alkylpurine damage, unrepaired DNA damage leads to carcinogenesis, cell death, and aging, also releases 1,N6-ethenoadenine
-
-
?
additional information
?
-
-
fails to excise N7 guanine adducts
-
-
?
additional information
?
-
-
removes also hypoxanthine and 1,N6-ethenoadenine
-
-
?
additional information
?
-
-
enzyme is involved in DNA excision repair
-
-
?
additional information
?
-
-
no activity on O2-methylcytosine, O2-methylthymine, O4-methylthymine or O6-methylguanine
-
-
?
additional information
?
-
-
removes also N-alkylpurines and cyclic ethenoadducta of adenine, guanine and cytosine
-
-
?
additional information
?
-
-
fails to excise N7 guanine adducts
-
-
?
additional information
?
-
-
releases 3-methyladenine, 3-methylguanine, 7-methylguanine, 7-(2-chloroethyl)guanine, 7-(2-hydroxyethyl)guanine, 1,N6-ethenoadenine, hypoxanthine, and guanine from damaged and normal DNA, adenine, thymine, cytosine,3-ethenoguanine, 8-oxoguanine, 7-(2-ethoxyethyl)guanine, O2-methylthymine, and O2-methylcytosine are not released
-
-
?
additional information
?
-
-
no significant activity is found towards deamination products, ethenoadducts or oxidation products
-
-
?
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Evensen, G.; Seeberg, E.
Adaptation to alkylation resistance involves the induction of a DNA glycosylase
Nature
296
773-775
1982
Escherichia coli
brenda
Karran, P.; Hjelmgren, T.; Lindahl, T.
Induction of a DNA glycosylase for N-methylated purines is part of the adaptive response to alkylating agents
Nature
296
770-773
1982
Escherichia coli, no activity in Escherichia coli
brenda
Thomas, L.; Yang, C.H.; Goldthwait, D.A.
Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine
Biochemistry
21
1162-1169
1982
Escherichia coli, Escherichia coli BW 9062
brenda
Clarke, N.D.; Kvaal, M.; Seeberg, E.
Cloning of Escherichia coli genes encoding 3-methyladenine DNA glycosylases I and II
Mol. Gen. Genet.
197
368-372
1984
Escherichia coli
brenda
Riazuddin, S.; Athar, A.; Ahmed, Z.; Lali, S.M.; Sohail, A.
DNA glycosylase enzymes induced during chemical adaptation of M. luteus
Nucleic Acids Res.
15
6607-6624
1987
Escherichia coli, Micrococcus luteus
brenda
Bjelland, S.; Seeberg, E.
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
brenda
Yamagata, Y.; Odawara, K.; Tomita, K.; Nakabeppu, Y.; Sekiguchi, M.
Crystallization and preliminary X-ray diffraction studies of 3-methyladenine-DNA glycosylase II from Escherichia coli
J. Mol. Biol.
204
1055-1056
1988
Escherichia coli
brenda
Bjelland, S.; Birkeland, N.K.; Benneche, T.; Volden, G.; Seeberg, E.
DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the AlkA enzyme in Escherichia coli
J. Biol. Chem.
269
30489-30495
1994
Escherichia coli
brenda
Schaerer, O.D.; Ortholand, J.Y.; Ganesan, A.; Ezaz-Nikpay, K.; Verdine, G.L.
Specific binding of the DNA repair enzyme AlkA to a pyrrolidine-based inhibitor
J. Am. Chem. Soc.
117
6623-6624
1995
Escherichia coli
-
brenda
Matijasevic, Z.; Stering, A.; Niu, T.Q.; Austin-Ritchie, P.; Ludlum, D.B.
Release of sulfur mustard-modified DNA bases by Escherichia coli 3-methyladenine DNA glycosylase II
Carcinogenesis
17
2249-2252
1996
Escherichia coli
brenda
Yamagata, Y.; Kato, M.; Odawara, K.; Tokuno, Y.; Nakashima, Y.; Matsushima, N.; Yasumura, K.; Tomita, K.; Ihara, K.; Fujii, Y.; Nakabeppu, Y.; Sekiguchi, M.; Fujii, S.
Three-dimensional structure of a DNA repair enzyme, 3-methyladenine DNA glycosylase II, from Escherichia coli
Cell
86
311-319
1996
Escherichia coli
brenda
Borys, E.; Kusmierek, J.T.
Endogenous and exogenous DNA lesions recognized by N-alkylpurine-DNA glycosylases
Acta Biochim. Pol.
45
579-586
1998
Escherichia coli, Escherichia coli JM105
brenda
Cerda, S.R.; Turk, P.W.; Thor, A.D.; Weitzman, S.A.
Altered expression of the DNA repair protein, N-methylpurine-DNA glycosylase (MPG) in breast cancer
FEBS Lett.
431
12-18
1998
Homo sapiens
brenda
Je, K.H.; Son, J.K.; O'Connor, T.R.; Lee, C.S.
Hepsulfam induced DNA adducts and its excision repair by bacterial and mammalian 3-methyladenine DNA glycosylases
Mol. Cells
8
691-697
1998
Escherichia coli, Homo sapiens, Rattus norvegicus
brenda
Kim, N.K.; Lee, S.H.; Cha, K.Y.; Seo, J.S.
Tissue-specific expression and activation of N-methylpurine-DNA glycosylase in thymic carcinomas of transgenic mice expressing the SV40 large T-antigen gene
Mol. Cells
8
383-387
1998
Mus musculus
brenda
Roy, R.; Biswas, T.; Hazra, T.K.; Roy, G.; Grabowski, D.T.; Izumi, T.; Srinivasan, G.; Mitra, S.
Specific interaction of wild-type and truncated mouse N-methylpurine-DNA glycosylase with ethenoadenine-containing DNA
Biochemistry
37
580-589
1998
Mus musculus
brenda
Masaoka, A.; Terato, H.; Kobayashi, M.; Honsho, A.; Ohyama, Y.; Ide, H.
Enzymatic repair of 5-formyluracil. I. Excision of 5-formyluracil site-specifically incorporated into oligonucleotide substrates by alka protein (Escherichia coli 3-methyladenine DNA glycosylase II)
J. Biol. Chem.
274
25136-25143
1999
Escherichia coli, Escherichia coli MV1161
brenda
Terato, H.; Masaoka, A.; Kobayashi, M.; Fukushima, S.; Ohyama, Y.; Yoshida, M.; Ide, H.
Enzymatic repair of 5-formyluracil. II. Mismatch formation between 5-formyluracil and guanine during dna replication and its recognition by two proteins involved in base excision repair (AlkA) and mismatch repair (MutS)
J. Biol. Chem.
274
25144-25150
1999
Escherichia coli, Escherichia coli AB1157
brenda
Wyatt, M.D.; Allan, J.M.; Lau, A.Y.; Ellenberger, T.E.; Samson, L.D.
3-Methyladenine DNA glycosylases: structure, function, and biological importance
Bioessays
21
668-676
1999
Arabidopsis thaliana, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Mus musculus, Rattus norvegicus, Schizosaccharomyces pombe
brenda
Hollis, T.; Ichikawa, Y.; Ellenberger, T.
DNA bending and a flip-out mechanism for base excision by the helix-hairpin-helix DNA glycosylase, Escherichia coli AlkA
EMBO J.
19
758-766
2000
Escherichia coli (P04395), Escherichia coli
brenda
Roy, R.; Biswas, T.; Lee, J.C.; Mitra, S.
Mutation of a unique aspartate residue abolishes the catalytic activity but not substrate binding of the mouse N-methylpurine-DNA glycosylase (MPG)
J. Biol. Chem.
275
4278-4282
2000
Homo sapiens, Mus musculus
brenda
Birkeland, N.K.; Anensen, H.; Knaevelsrud, I.; Kristoffersen, W.; Bjoras, M.; Robb, F.T.; Klungland, A.; Bjelland, S.
Methylpurine DNA glycosylase of the hyperthermophilic archaeon Archaeoglobus fulgidus
Biochemistry
41
12697-12705
2002
Archaeoglobus fulgidus, Escherichia coli
brenda
Biswas, T.; Clos, L.J.2nd.; SantaLucia, J.Jr.; Mitra, S.; Roy, R.
Binding of specific DNA base-pair mismatches by N-methylpurine-DNA glycosylase and its implication in initial damage recognition
J. Mol. Biol.
320
503-513
2002
Mus musculus
brenda
Saparbaev, M.; Langouet, S.; Privezentzev, C.V.; Guengerich, F.P.; Cai, H.; Elder, R.H.; Laval, J.
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
brenda
Teale, M.; Symersky, J.; DeLucas, L.
3-Methyladenine-DNA glycosylase II: the crystal structure of an AlkA-hypoxanthine complex suggests the possibility of product inhibition
Bioconjug. Chem.
13
403-407
2002
Escherichia coli
brenda
Terato, H.; Masaoka, A.; Asagoshi, K.; Honsho, A.; Ohyama, Y.; Suzuki, T.; Yamada, M.; Makino, K.; Yamamoto, K.; Ide, H.
Novel repair activities of AlkA (3-methyladenine DNA glycosylase II) and endonuclease VIII for xanthine and oxanine, guanine lesions induced by nitric oxide and nitrous acid
Nucleic Acids Res.
30
4975-4984
2002
Escherichia coli, Escherichia coli MV1161
brenda
Fishel, M.L.; Seo, Y.R.; Smith, M.L.; Kelley, M.R.
Imbalancing the DNA base excision repair pathway in the mitochondria; targeting and overexpressing N-methylpurine DNA glycosylase in mitochondria leads to enhanced cell killing
Cancer Res.
63
608-615
2003
Homo sapiens
brenda
Wozniak, K.; Blasiak, J.
Nickel impairs the repair of UV- and MNNG-damaged DNA
Cell. Mol. Biol. Lett.
9
83-94
2004
Homo sapiens
brenda
Connor, E.E.; Wilson, J.J.; Wyatt, M.D.
Effects of substrate specificity on initiating the base excision repair of N-methylpurines by variant human 3-methyladenine DNA glycosylases
Chem. Res. Toxicol.
18
87-94
2005
Homo sapiens
brenda
Guliaev, A.B.; Singer, B.; Hang, B.
Chloroethylnitrosourea-derived ethano cytosine and adenine adducts are substrates for Escherichia coli glycosylases excising analogous etheno adducts
DNA Repair
3
1311-1321
2004
Escherichia coli
brenda
O'Brien, P.J.; Ellenberger, T.
The Escherichia coli 3-methyladenine DNA glycosylase AlkA has a remarkably versatile active site
J. Biol. Chem.
279
26876-26884
2004
Escherichia coli
brenda
Alseth, I.; Rognes, T.; Lindback, T.; Solberg, I.; Robertsen, K.; Kristiansen, K.I.; Mainieri, D.; Lillehagen, L.; Kolsto, A.B.; Bjoras, M.
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
brenda
Alseth, I.; Osman, F.; Korvald, H.; Tsaneva, I.; Whitby, M.C.; Seeberg, E.; Bjoras, M.
Biochemical characterization and DNA repair pathway interactions of Mag1-mediated base excision repair in Schizosaccharomyces pombe
Nucleic Acids Res.
33
1123-1131
2005
Schizosaccharomyces pombe
brenda
Leiros, I.; Nabong, M.P.; Gr?svik, K.; Ringvoll, J.; Haugland, G.T.; Uldal, L.; Reite, K.; Olsbu, I.K.; Knaevelsrud, I.; Moe, E.; Andersen, O.A.; Birkeland, N.K.; Ruoff, P.; Klungland, A.; Bjelland, S.
Structural basis for enzymatic excision of N1-methyladenine and N3-methylcytosine from DNA
EMBO J.
26
2206-2217
2007
Archaeoglobus fulgidus
brenda
Harrison, J.F.; Rinne, M.L.; Kelley, M.R.; Druzhyna, N.M.; Wilson, G.L.; Ledoux, S.P.
Altering DNA base excision repair: use of nuclear and mitochondrial-targeted N-methylpurine DNA glycosylase to sensitize astroglia to chemotherapeutic agents
Glia
55
1416-1425
2007
Rattus norvegicus
brenda
Adhikari, S.; Toretsky, J.A.; Yuan, L.; Roy, R.
Magnesium, essential for base excision repair enzymes, inhibits substrate binding of N-methylpurine-DNA glycosylase
J. Biol. Chem.
281
29525-29532
2006
Mus musculus
brenda
Wang, P.; Guliaev, A.B.; Hang, B.
Metal inhibition of human N-methylpurine-DNA glycosylase activity in base excision repair
Toxicol. Lett.
166
237-247
2006
Homo sapiens (P29372), Homo sapiens
brenda
Rubinson, E.H.; Metz, A.H.; OQuin, J.; Eichman, B.F.
A new protein architecture for processing alkylation damaged DNA: the crystal structure of DNA glycosylase AlkD
J. Mol. Biol.
381
13-23
2008
Bacillus cereus
brenda
Adhikari, S.; Manthena, P.V.; Uren, A.; Roy, R.
Expression, purification and characterization of codon-optimized human N-methylpurine-DNA glycosylase from Escherichia coli
Protein Expr. Purif.
58
257-262
2008
Homo sapiens
brenda
Zhao, B.; OBrien, P.J.
Kinetic mechanism for the excision of hypoxanthine by Escherichia coli AlkA and evidence for binding to DNA ends
Biochemistry
50
4350-4359
2011
Escherichia coli
brenda
Bowman, B.R.; Lee, S.; Wang, S.; Verdine, G.L.
Structure of Escherichia coli AlkA in complex with undamaged DNA
J. Biol. Chem.
285
35783-35791
2010
Escherichia coli (P04395), Escherichia coli
brenda
Moe, E.; Hall, D.R.; Leiros, I.; Monsen, V.T.; Timmins, J.; McSweeney, S.
Structure-function studies of an unusual 3-methyladenine DNA glycosylase II (AlkA) from Deinococcus radiodurans
Acta Crystallogr. Sect. D
68
703-712
2012
Deinococcus radiodurans (Q9RRB0), Deinococcus radiodurans
brenda
Admiraal, S.; O'Brien, P.
DNA-N-glycosylases process novel O-glycosidic sites in DNA
Biochemistry
52
4066-4074
2013
Escherichia coli (P04395), Escherichia coli
brenda
Michelson, A.Z.; Chen, M.; Wang, K.; Lee, J.K.
Gas-phase studies of purine 3-methyladenine DNA glycosylase II (AlkA) substrates
J. Am. Chem. Soc.
134
9622-9633
2012
Escherichia coli (P04395)
brenda
Admiraal, S.J.; O'Brien, P.J.
Base excision repair enzymes protect abasic sites in duplex DNA from interstrand cross-links
Biochemistry
54
1849-1857
2015
Escherichia coli, Homo sapiens (P29372), Homo sapiens
brenda
Lenz, S.A.P.; Wetmore, S.D.
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 (P29372), Homo sapiens
brenda
Lenz, S.A.P.; Wetmore, S.D.
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 (P29372), Homo sapiens
brenda