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Information on EC 3.2.2.20 - DNA-3-methyladenine glycosylase I and Organism(s) Escherichia coli and UniProt Accession P05100
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3.2.2.20 DNA-3-methyladenine glycosylase IIUBMB Comments
Involved in the removal of alkylated bases from DNA in Escherichia coli (cf. EC 2.1.1.63 methylated-DNA---[protein]-cysteine S-methyltransferase).
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Word Map
- 3.2.2.20
- glycosylases
-
abasic
-
excises
-
self-labeling
- 1,n6-ethenoadenine
-
snap-tagged
- 3-methylguanine
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
protein tag, 3-methyladenine dna glycosylase, 3-methyladenine dna glycosylase i, 3mea dna glycosylase, mag1 3-methyladenine dna glycosylase, mag1p, mag2p, taga protein, 3-mea dna glycosylase i, aag 3mea dna glycosylase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-methyladenine DNA glycosylase I
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-
-
-
deoxyribonucleate 3-methyladenine DNA glycosidase I
-
-
-
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DNA-3-methyladenine DNA glycosidase I
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-
-
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TAG
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
alkylated-DNA glycohydrolase (releasing methyladenine and methylguanine)
Involved in the removal of alkylated bases from DNA in Escherichia coli (cf. EC 2.1.1.63 methylated-DNA---[protein]-cysteine S-methyltransferase).
CAS REGISTRY NUMBER
COMMENTARY
89287-37-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-methyladenine residues in alkylated DNA + H2O
3-methyladenine + ?
-
-
-
-
?
alkylated DNA + H2O
3-methyladenine + ?
smallest member of the helix-hairpin-helix HhH superfamily of DNA glycosylases
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
-
releases 3-methyladenine and 3-ethyladenine
?
alkylated DNA + H2O
3-methyladenine + ?
-
-
also releases a minmal amount of 3-methylguanine
?
alkylated DNA + H2O
3-methyladenine + ?
-
-
also releases a minmal amount of 3-methylguanine
?
alkylated DNA + H2O
3-methyladenine + ?
-
double-stranded DNA is an effective substrate, enzyme is less efficient in excision of base damage from single-stranded regions transiently formed in DNA during transcription and replication
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
double-stranded DNA is an effective substrate, enzyme is less efficient in excision of base damage from single-stranded regions transiently formed in DNA during transcription and replication
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
reaction of the enzyme with alkylated DNA leads to introduction of apurinic sites but no chain breaks
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
primarily removes N3-methyladenine but also N3-methylguanine from DNA by glycosylic cleavage in the first step of the base excision repair
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
constitutive 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 + ?
-
constitutive 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 + ?
-
constititively expressed
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
constititively expressed
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
constititively expressed
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
constititively expressed
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
constititively expressed
-
?
alkylated DNA + H2O
3-methyladenine + ?
constititively expressed
-
?
additional information
?
-
-
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
?
-
-
no detectable endonuclease activity on native, depurinated or alkylated plasmid DNA
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-
?
additional information
?
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-
does not liberate 7-methylguanine, O6-methylguanine, 7-methyladenine, 7-ethylguanine, O6-ethylguanine, and arylalkylated purine derivatives obtained by treatment of DNA with 7-bromomethyl-12-methylbenz[alpha]anthracene, no detectable nuclease activity with native DNA, depurinated DNA, ultraviolet-irradiated DNA, or X-irradiated DNA as potential substrates, enzyme does not release hypoxanthine or xanthine in free form from by nitrous acid treatment partly demainated DNA
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alkylated DNA + H2O
3-methyladenine + ?
smallest member of the helix-hairpin-helix HhH superfamily of DNA glycosylases
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
double-stranded DNA is an effective substrate, enzyme is less efficient in excision of base damage from single-stranded regions transiently formed in DNA during transcription and replication
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
double-stranded DNA is an effective substrate, enzyme is less efficient in excision of base damage from single-stranded regions transiently formed in DNA during transcription and replication
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
reaction of the enzyme with alkylated DNA leads to introduction of apurinic sites but no chain breaks
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
primarily removes N3-methyladenine but also N3-methylguanine from DNA by glycosylic cleavage in the first step of the base excision repair
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
constitutive 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 + ?
-
constitutive 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 + ?
-
constititively expressed
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
constititively expressed
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
constititively expressed
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
constititively expressed
-
?
alkylated DNA + H2O
3-methyladenine + ?
-
constititively expressed
-
?
alkylated DNA + H2O
3-methyladenine + ?
constititively expressed
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
free adenine, 1 methyladenine, 7-methylguanine, caffeine or uracil fails to inhibit the enzyme
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000006
3-methyladenine residues in alkylated DNA
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pH 7.6, 37°C, release of 3-methyladenine
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0.000014
3-methyladenine residues in alkylated DNA
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pH 7.8, 37°C, release of 3-methyladenine
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
-
more active in 0.07 M HEPES-KOH buffer than in 0.07 M Tris-HCl buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19000
21100
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repeated freezing and thawing does not effect any apparent loss in enzyme activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stored frozen in buffer containing 1 mg/ml bovine serum albumin, stable for more than 6 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type TAG overexpressed from pET21a(TAG) in Escherichia coli BL21(DE3)
integration and expression of the tag gene with retroviral vectors into chinese hamster V79 cells by liposome mediated transfection and into murine haemopoeitic stemm cells by cocultivation with a lipofected, virus-packaging cell line, stable transfectants are more resistant to cytotoxic effects of methylmethanesulfonate and N-methyl-nitrosourea than their parent cell lines
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Riazuddin, S.; Lindahl, T.
Properties of 3-methyladenine-DNA glycosylase from Escherichia coli
Biochemistry
17
2110-2118
1978
Escherichia coli
Evensen, G.; Seeberg, E.
Adaptation to alkylation resistance involves the induction of a DNA glycosylase
Nature
296
773-775
1982
Escherichia coli
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
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, no activity in Escherichia coli, Escherichia coli BW 9062
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
Steinum, A.L.; Seeberg, E.
Nucleotide sequence of the tag gene from Escherichia coli
Nucleic Acids Res.
14
3763-3772
1986
Escherichia coli
Bjelland, S.; Seeberg, E.
Purification and characterization of 3-methyladenine DNA glycosylase I from Escherichia coli
Nucleic Acids Res.
15
2787-2801
1987
Escherichia coli
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
Klungland, A.; Fairbairn, L.; Watson, A.J.; Margison, G.P.; Seeberg, E.
Expression of the E.coli 3-methyladenine DNA glycosylase I gene in mammalian cells reduces the toxic and mutagenic effects of methylating agents
EMBO J.
11
4439-4444
1992
Escherichia coli
Taverna, P.; Garattini, E.; Citti, L.; Damia, G.; D'Incalci, M.
Expression of E. coli tag gene encoding 3-methyladenine glycosylase I in NIH-3T3 murine fibroblasts
Biochem. Biophys. Res. Commun.
185
41-46
1992
Escherichia coli
Seeberg, E.
Physical and genetic mapping of the tag gene on the Escherichia coli chromosome
J. Bacteriol.
175
5733-5734
1993
Escherichia coli
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
Tomicic, M.; Franekic, J.
Effect of overexpression of E. coli 3-methyladenine-DNA glycosylase I (Tag) on survival and mutation induction in Salmonella typhimurium
Mutat. Res.
358
81-87
1996
Escherichia coli
Plochocka, D.; Kierzek, A.; Obtulowicz, T.; Tudek, B.; Zielenkiewicz, P.
3-Methyladenine-DNA glycosylase I from Escherichia coli-computer modeling and supporting experimental evidence
Biochem. Biophys. Res. Commun.
268
724-727
2000
Escherichia coli
Bujnicki, J.M.; Rychlewski, L.
Fold-recognition analysis predicts that the Tag protein family shares a common domain with the helix-hairpin-helix DNA glycosylases
DNA Repair
1
391-395
2002
Escherichia coli, Homo sapiens
Drohat, A.C.; Kwon, K.; Krosky, D.J.; Stivers, J.T.
3-Methyladenine DNA glycosylase I is an unexpected helix-hairpin-helix superfamily member
Nat. Struct. Biol.
9
659-664
2002
Escherichia coli (W8TFT1), Escherichia coli, Escherichia coli B / ATCC 11303 (W8TFT1)
Cao, C.; Kwon, K.; Jiang, Y.L.; Drohat, A.C.; Stivers, J.T.
Solution structure and base perturbation studies reveal a novel mode of alkylated base recognition by 3-methyladenine DNA glycosylase I
J. Biol. Chem.
278
48012-48020
2003
Escherichia coli
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