Information on EC 3.2.2.21 - DNA-3-methyladenine glycosylase II

Information on EC 3.2.2.21 - DNA-3-methyladenine glycosylase II:

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EC NUMBER	COMMENTARY
3.2.2.21	-

RECOMMENDED NAME	GeneOntology No.
DNA-3-methyladenine glycosylase II	GO:0052822

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine		involved in the removal of alkylated bases from DNA in Escherichia coli (cf. EC 2.1.1.63 methylated-DNA-[protein]-cysteine S-methyltransferase)	-	-	-

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
hydrolysis of N-glycosyl bond	-	-	-	-

PATHWAY	KEGG Link	MetaCyc Link
No entries in this field

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).

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
3-methyladenine DNA glycosylase II	Escherichia coli	-	-	668383, 669235, 714251
3-methyladenine-DNA glycosidase II	-	-	-	-
3-methyladenine-DNA glycosylase II	-	-	-	-
AAG	Mus musculus	-	-	646885
AAG	Homo sapiens	-	-	646885, 668249
ALK	Escherichia coli	-	-	646878
AlkA	-	-	-	-
AlkA	Escherichia coli	-	-	668383, 669235, 714251, 715554
AlkA protein	Escherichia coli	-	-	646878, 646880, 646883, 646884, 646886
AlkD	Bacillus cereus	-	-	670318, 699549
alkylpurine-DNA-N-glycosylase	Homo sapiens	-	-	646890
ANPG	Homo sapiens	-	-	646890, 668249
deoxyribonucleate 3-methyladenine glycosidase II	-	-	-	-
DNA glycosylase	Bacillus cereus	-	-	699549
DNA-3-methyladenine glycosidase II	-	-	-	-
helix-hairpin-helix DNA glycosylase	Escherichia coli	-	-	646886
m3A DNA glycosylase II	Escherichia coli	-	-	646846
MAG	Saccharomyces cerevisiae	-	-	646885
Mag1 protein	Schizosaccharomyces pombe	-	-	670427
MPG	Archaeoglobus fulgidus	-	-	646888
MPG	Mus musculus	-	-	646887, 646889
MPG	Homo sapiens	-	-	646887, 646893, 668249, 701054
N-methylpurine-DNA glycosylase	Homo sapiens	-	-	701054
TagII	-	-	-	-

CAS REGISTRY NUMBER	COMMENTARY
89287-38-7	-

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Arabidopsis thaliana	-	646885	-	-
Archaeoglobus fulgidus	-	646888, 679498	-	-
Bacillus cereus	-	670318	-	-
Bacillus cereus	strain ATCC 14579	699549	-	-
Escherichia coli	-	646845, 646851, 646855, 646872, 646873, 646874, 646876, 646877, 646880, 646885, 646888, 646891, 668383, 669235, 714251	-	-
Escherichia coli	-	646886, 715554	P04395	UniProt
Escherichia coli	AB1157	646884	-	-
Escherichia coli	JM105	646878	-	-
Escherichia coli	K12 derivatives	646848	-	-
Escherichia coli	MV1161	646883, 646892	-	-
Escherichia coli	strain BW 9062	646847	-	-
Escherichia coli	tagA mutant BK2114	646846	-	-
Escherichia coli AB1157	AB1157	646884	-	-
Escherichia coli BW 9062	strain BW 9062	646847	-	-
Escherichia coli JM105	JM105	646878	-	-
Escherichia coli MV1161	MV1161	646883, 646892	-	-
Homo sapiens	-	668214, 668249, 701054	-	-
Homo sapiens	-	682910	P29372	Uniprot
Homo sapiens	human	646879, 646880, 646885, 646887, 646890	-	-
Homo sapiens	human; MDA-MB231	646893	-	-
Micrococcus luteus	-	646851	-	-
Mus musculus	mouse	646882, 646885, 646887, 646889	-	-
Mus musculus	mouse; transgenic mouse lines SVT125, 127 and 248, expressing the SV40 large T-antigen gene	646881	-	-
Mus musculus	recombinant enzyme	680691	-	-
no activity in Escherichia coli	alk mutants	646846	-	-
Rattus norvegicus	-	680028	-	-
Rattus norvegicus	rat	646880, 646885	-	-
Saccharomyces cerevisiae	yeast	646885	-	-
Schizosaccharomyces pombe	-	670427	-	-
Schizosaccharomyces pombe	fission yeast	646885	-	-

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Mus musculus	-	-	646881, 646882, 646885, 646887, 646889	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Escherichia coli	-	-	646845, 646846, 646847, 646848, 646851, 646855, 646872, 646873, 646874, 646876, 646877, 646878, 646880, 646883, 646884, 646885	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Escherichia coli	P04395	-	646886	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Escherichia coli	-	-	646888, 646891, 646892	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Homo sapiens	-	-	646879, 646880, 646885, 646887, 646890, 646893	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Rattus norvegicus	-	-	646880, 646885	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Saccharomyces cerevisiae, Arabidopsis thaliana, Schizosaccharomyces pombe	-	-	646885	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Micrococcus luteus	-	-	646851	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Archaeoglobus fulgidus	-	-	646888	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Escherichia coli	-	calf thymus DNA	646876	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Micrococcus luteus	-	cellular repair of alkylated DNA base modifications	646851	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Escherichia coli	-	DNA repair enzyme, inducible base excision repair pathway of DNA alkylation damage	646873, 646874, 646884	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Escherichia coli	P04395	DNA repair enzyme, inducible base excision repair pathway of DNA alkylation damage	646886	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Escherichia coli	-	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	646855	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Homo sapiens	-	short-patch base excision repair pathway, repair of alkylation and oxidative DNA damage	646893	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Mus musculus	-	binds mismatch base-pairs in DNA	646889	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Escherichia coli	-	inducible pathway for repair of DNA damaged by simple alkylating agents such as methylmethanesulfonate and N-methyl-N'-nitro-N-nitrosoguanidine	646848, 646883	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + 7-methyladenine + DNA		Escherichia coli	-	-	646847	-	-	?
alkylated DNA + H2O	3-methyladenine + 3-methylguanine + 7-methyladenine + 7-methylguanine + DNA		Micrococcus luteus	-	-	646851	-	-	?
alkylated DNA + H2O	3-methyladenine + 3-methylguanine + 7-methyladenine + 7-methylguanine + DNA		Archaeoglobus fulgidus	-	-	646888	-	-	?
alkylated DNA + H2O	3-methyladenine + 3-methylguanine + 7-methylguanine + 7-methyladenine + ?		Escherichia coli	-	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	669235	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + 3-methylguanine		Bacillus cereus	-	AlkD has high activity towards 7-methylguanine but removes 3-methylguanine more slowly as compared with Escherichia coli AlkA	670318	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + ?		Homo sapiens	-	-	668249	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	?		Schizosaccharomyces pombe	-	the efficiency of 3-methyladenine and 3-methylguanine removal was 5�10 times slower for Mag1 than for Escherichia coli AlkA whereas the rate of 7-methylguanine removal is similar to the two enzymes	670427	-	-	?
alkylated DNA + H2O	3-methyladenine + N3-methylcytosine + 1,N6-ethenoadenine + DNA		Archaeoglobus fulgidus	-	-	679498	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	3-methyladenine + 7-methylguanine + DNA		Bacillus cereus	-	-	699549	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + hypoxanthine + DNA		Homo sapiens	-	-	701054	-	-	?
alkylated DNA + H2O	3-methyl-2'-deoxyadenosine + 3-deaza-3-methyl-2'-deoxyadenosine + DNA		Escherichia coli	-	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	715554	-	-	?
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + 1,N6-ethenoadenine + hypoxanthine + DNA		Escherichia coli	-	-	715554	-	-	?
DNA treated with beta-[3H]propiolactone + H2O	N1-(carboxyethyl)adenine + N7-(carboxymethyl)guanine		Escherichia coli	-	-	646847	-	-	?
duplex oligonucleotide substrate containing ethenoadenine + H2O	ethenoadenine + oligonucleotide		Homo sapiens	P29372	-	682910	-	-	?
duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine + H2O	ethenoadenine + hypoxanthine + oligonucleotide		Mus musculus	-	-	680691	-	-	?
synthetic oligosaccharide + H2O	?		Escherichia coli	-	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	668383	-	-	?
duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine + H2O	ethenoadenine + hypoxanthine + oligonucleotide		Escherichia coli	-	-	714251	-	-	?
additional information	?	-	Escherichia coli	-	-	646851, 646888	-	-	-
additional information	?	-	Micrococcus luteus	-	no activity on O2-methylcytosine, O2-methylthymine, O4-methylthymine or O6-methylguanine	646851	-	-	-
additional information	?	-	Saccharomyces cerevisiae	-	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	646885	-	-	-
additional information	?	-	Escherichia coli	-	removes alkylation damage from duplex and single stranded DNA	646891	-	-	-
additional information	?	-	Escherichia coli	-	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	646885	-	-	-
additional information	?	-	Escherichia coli	-	excises N7 guanine adducts completely, also capable of removing normal base residues from DNA	646880	-	-	-
additional information	?	-	Escherichia coli	-	also capable to relase xanthine and oxanine, guanine lesions induced by nitrosation	646892	-	-	-
additional information	?	-	Homo sapiens	-	removes N-alkylpurine damage, unrepaired DNA damage leads to carcinogenesis, cell death, and aging, also releases 1,N6-ethenoadenine	646879, 646890	-	-	-
additional information	?	-	Escherichia coli	-	with sulfur mustard treated DNA as substrate enzyme releases 7-hydroxyethylthioethyl guanine and 3-hydroxyethylthioethyl adenine, can also release carboxyethylate purines from DNA	646876	-	-	-
additional information	?	-	Mus musculus	-	removes also N-alkylpurines and cyclic ethenoadducta of adenine, guanine and cytosine	646882	-	-	-
additional information	?	-	Homo sapiens, Rattus norvegicus	-	fails to excise N7 guanine adducts	646880	-	-	-
additional information	?	-	Escherichia coli	-	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	646878	-	-	-
additional information	?	-	Homo sapiens	-	removes also hypoxanthine and 1,N6-ethenoadenine	646893	-	-	-
additional information	?	-	Escherichia coli	-	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	646847	-	-	-
additional information	?	-	Escherichia coli	-	enzyme also excises thymine residues oxidized in the methyl group like 5-formyluracil and 5-hydroxymethyluracil	646873	-	-	-
additional information	?	-	Archaeoglobus fulgidus	-	excises alkylated bases only	646888	-	-	-
additional information	?	-	Escherichia coli	-	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	646883, 646884	-	-	-
additional information	?	-	Bacillus cereus	-	AlkD is involved exclusively in the repair of alkylation damage	670318	-	-	-
additional information	?	-	Homo sapiens	-	enzyme is involved in DNA excision repair	668214	-	-	-
additional information	?	-	Escherichia coli	-	the enzyme is induced in response to DNA alkylation, and it protects cells from alkylated nucleobases by catalyzing their excision	669235	-	-	-
additional information	?	-	Bacillus cereus	-	no detectable affinity for hypoxanthine, 1,N6-ethenoadenine, 8-oxoguanine and 5-formyluracil	670318	-	-	-
additional information	?	-	Schizosaccharomyces pombe	-	no significant activity is found towards deamination products, ethenoadducts or oxidation products	670427	-	-	-
additional information	?	-	Bacillus cereus	-	AlkD does not excise 1,N6-ethenoadenine	699549	-	-	-
additional information	?	-	Escherichia coli	-	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	714251	-	-	-
additional information	?	-	Escherichia coli	-	the enzyme has little activity on correctly base-paired adenine. N3-deazaadenine is not substantially cleaved opposite cytosine or thymidine	715554	-	-	-

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Mus musculus	-	-	646881, 646882, 646885, 646887	-	-
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Escherichia coli	-	-	646845, 646846, 646847, 646851, 646872, 646876, 646877, 646878, 646880, 646885, 646888, 646891, 646892	-	-
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Homo sapiens	-	-	646879, 646880, 646885, 646887, 646890	-	-
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Rattus norvegicus	-	-	646880, 646885	-	-
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Saccharomyces cerevisiae, Arabidopsis thaliana, Schizosaccharomyces pombe	-	-	646885	-	-
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Archaeoglobus fulgidus	-	-	646888	-	-
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Micrococcus luteus	-	cellular repair of alkylated DNA base modifications	646851	-	-
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Escherichia coli	-	DNA repair enzyme, inducible base excision repair pathway of DNA alkylation damage	646873, 646874, 646884	-	-
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Escherichia coli	P04395	DNA repair enzyme, inducible base excision repair pathway of DNA alkylation damage	646886	-	-
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Escherichia coli	-	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	646855	-	-
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Homo sapiens	-	short-patch base excision repair pathway, repair of alkylation and oxidative DNA damage	646893	-	-
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Mus musculus	-	binds mismatch base-pairs in DNA	646889	-	-
alkylated DNA + H2O	3-methyladenine + 7-methylguanine + O2-methylthymine + O2-methylcytosine + DNA		Escherichia coli	-	inducible pathway for repair of DNA damaged by simple alkylating agents such as methylmethanesulfonate and N-methyl-N'-nitro-N-nitrosoguanidine	646848, 646883	-	-
additional information	?	-	Bacillus cereus	-	AlkD is involved exclusively in the repair of alkylation damage	670318	-	-
additional information	?	-	Homo sapiens	-	enzyme is involved in DNA excision repair	668214	-	-
additional information	?	-	Escherichia coli	-	the enzyme is induced in response to DNA alkylation, and it protects cells from alkylated nucleobases by catalyzing their excision	669235	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
additional information	Micrococcus luteus	-	no absolute cofactor requirement	646851	-

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Ca2+	Archaeoglobus fulgidus	-	2 mM CaCl2, enzyme activity 103%	646888
Cd2+	Homo sapiens	P29372	inhibitory above 0.05 mM. Reduced catalytic activity in presence of Zn2+ is not due to altered binding of substrate	682910
K+	Homo sapiens	-	optimal activity at pH 7.5 and 100 mM KCl	701054
Mg2+	Escherichia coli	-	stimulated by 1 mM	646847
Mg2+	Escherichia coli	-	stimulated by 1.5 mM MgCl2	646851
Mg2+	Micrococcus luteus	-	no obligatory requirement, but addition of 1.5 mM MgCl2 causes stimulation in the catalytic activity 2fold	646851
Mg2+	Archaeoglobus fulgidus	-	2 mM MgSO4, enzyme activity 112%	646888
Mg2+	Escherichia coli	-	-	646888
Mg2+	Mus musculus	-	at low concentration, Mg2+ stimulates enzyme activity with substrate hypoxanthine, but not with ethenoadenine. At high concentrations, inhibitory	680691
Mn2+	Archaeoglobus fulgidus	-	2 mM MnCl2, enzyme activity 102%	646888
Ni2+	Homo sapiens	P29372	inhibitory above 0.05 mM, but to lesser extent than Cd2+ or Zn2+. Reduced catalytic activity in presence of Zn2+ is not due to altered binding of substrate	682910
Zn2+	Archaeoglobus fulgidus	-	0.1 mM ZnSO4, enzyme activity 114%	646888
Zn2+	Homo sapiens	P29372	enzyme active site has a potential binding site for Zn2+. Reduced catalytic activity in presence of Zn2+ is not due to altered binding of substrate	682910

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
2'-deoxy-2'-fluoro-7-methylguanosine	Escherichia coli	-	-	715554	-
abasic-containing DNA	Escherichia coli	-	potent inhibitor	714251	-
apurinic-DNA	Escherichia coli	-	-	646847	-
CaCl2	Micrococcus luteus	-	-	646851	2D-image
DNA containing 1-azaribose	Escherichia coli	-	-	646886	-
Double-stranded DNA	Escherichia coli	-	-	646847	2D-image
N-ethylmaleimide	Escherichia coli	-	1 mM, 24% inhibition	646847	2D-image
N-ethylmaleimide	Escherichia coli, Micrococcus luteus	-	-	646851	2D-image
NaCl	Escherichia coli	-	-	646847, 646851	2D-image
Ni2+	Homo sapiens	-	0.001 mM	668214	2D-image
p-hydroxymercuribenzoate	Archaeoglobus fulgidus	-	-	646888	2D-image
p-mercuribenzoate	Micrococcus luteus	-	-	646851	2D-image
Pyrrolidine-containing oligonucleotide	Escherichia coli	-	-	646874	-
ZnSO4	Archaeoglobus fulgidus	-	2 mM, enzyme activity 23%	646888	2D-image
Mg2+	Mus musculus	-	significant inhibition depending on its concentration, but independent of substrate type. Mg2+ at high but physiologic concentrations decreases the amount of active enzyme. Inhibition affects the Km value, but not Vmax, and is due to inhibition in substrate binding and can be reversed by EDTA. At low concentration, Mg2+ stimulates enzyme activity with substrate hypoxanthine, but not with ethenoadenine	680691	2D-image
additional information	Escherichia coli	-	prior complex formation between mismatch repair protein MutS and a heteroduplex containing an 5-formyluracil-guanine mispair inhibits the activity of AlkA to 5-formyluracil	646884	-
additional information	Archaeoglobus fulgidus	-	resistant to product inhibition by free 3-methyladenine	646888	-
additional information	Escherichia coli	-	resistant to product inhibition by free 3-methyladenine	646846, 646847, 646851, 646888	-

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
3-Methyladenine	Archaeoglobus fulgidus	-	5 mM, enzyme activity 110%	646888	2D-image
3-Methylguanine	Archaeoglobus fulgidus	-	5 mM, enzyme activity 120%	646888	2D-image
N-methyl-N'-nitro-N-nitrosoguanidine	Escherichia coli	-	-	646845	2D-image
N-methyl-N'-nitro-N-nitrosoguanidine	Escherichia coli	-	MNNG, good inducer of the enzyme, methylmethanesulfonate is less effective and 4-nitroquinoline-1-oxide has no effect	646846	2D-image
spermidine	Escherichia coli	-	stimulates activity	646847, 646851	2D-image
spermine	Escherichia coli	-	stimulates activity	646851	2D-image

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
2.4e-05	-	1,N6-ethenoadenine residues in alkylated DNA	Homo sapiens	-	pH 7.5, 37�C, excision of 1, N6-ethenoadenine	646890	-
4e-05	0.001	1,N6-ethenoadenine residues in alkylated DNA	Mus musculus	-	pH 8.3, 37�C, release of 1,N6-ethenoadenine, wild type enzyme	646882	-
6e-05	0.0013	1,N6-ethenoadenine residues in alkylated DNA	Mus musculus	-	pH 8.3, 37�C, release of 1,N6-ethenoadenine, truncated mutant N-DELTA100C-DELTA18	646882	-
9.2e-06	-	3-methyladenine residues in alkylated DNA	Escherichia coli	-	pH 8.0, 37�C, release of 3-methyladenine	646847	-
1.1e-05	-	7-methylguanine residues in alkylated DNA	Escherichia coli	-	pH 8.0, 37�C, release of 7-methylguanine	646847	-
1.4e-07	-	Alkylated DNA	Escherichia coli	-	pH 7.5, 37�C, excision of 5-hydroxymethyluracil, denatured DNA	646873	2D-image
4.4e-06	-	Alkylated DNA	Escherichia coli	-	pH 7.5, 37�C, excision of 5-hydroxymethyluracil	646873	2D-image
1.08e-05	-	Alkylated DNA	Escherichia coli	-	pH 7.5, 37�C, excision of 3-methyladenine	646873	2D-image
2.1e-05	-	Alkylated DNA	Escherichia coli	-	pH 8.0, 37�C, excision of 5-formyluracil	646883	2D-image
3e-05	-	Alkylated DNA	Escherichia coli	-	pH 8.0, 37�C, excision of 7-methylguanine	646883	2D-image
3.1e-05	-	alkylated DNA, treated with N-methyl-N'-nitro-N-nitrosoguanidine	Escherichia coli	-	pH 7.5, 37�C, excision of 7-methylguanine	646892	-
5.3e-05	-	alkylated DNA, treated with N-methyl-N'-nitro-N-nitrosoguanidine	Escherichia coli	-	pH 7.5, 37�C, excision of xanthine	646892	-
3.54e-05	-	duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine	Mus musculus	-	37�C, pH 7.9	680691	-
4.48e-05	-	duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine	Mus musculus	-	37�C, pH 7.9, presence of 250 mM Mg2+	680691	-
5.48e-05	-	duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine	Mus musculus	-	37�C, pH 7.9, presence of 500 mM Mg2+	680691	-
0.042	-	duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine	Escherichia coli	-	at 37�C, in 50 mM Na-MES buffer (pH 6.1)	714251	-
5.3e-06	-	hypoxanthine	Homo sapiens	-	at 37�C	701054	2D-image

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.000833	-	1,N6-ethenoadenine residues in alkylated DNA	Homo sapiens	-	pH 7.5, 37�C, excision of1, N6-ethenoadenine	646890	-
0.01	-	1,N6-ethenoadenine residues in alkylated DNA	Mus musculus	-	pH 8.3, 37�C, release of 1,N6-ethenoadenine, truncated mutant N-DELTA100C-DELTA18	646882	-
0.0167	-	1,N6-ethenoadenine residues in alkylated DNA	Mus musculus	-	pH 8.3, 37�C, release of 1,N6-ethenoadenine, wild-type	646882	-
0.00125	-	duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine	Escherichia coli	-	at 37�C, in 50 mM Na-MES buffer (pH 6.1)	714251	-
0.0033	-	hypoxanthine	Homo sapiens	-	at 37�C	701054	2D-image

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
30	-	duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine	Escherichia coli	-	at 37�C, in 50 mM Na-MES buffer (pH 6.1)	714251	0

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
8e-08	-	Mus musculus	-	mutant Asn-152, expressed in Escherichia coli	646887
5e-06	-	Mus musculus	-	mutant Asn-252, expressed in Escherichia coli	646887
7e-06	-	Mus musculus	-	mutant Asn-255 and Asn-231, expressed in Escherichia coli	646887
9e-06	-	Mus musculus	-	mutant Asn-259, expressed in Escherichia coli	646887
1e-05	-	Mus musculus	-	mutant Asn-260, expressed in Escherichia coli	646887
1.3e-05	-	Mus musculus	-	mutant Asn-112, expressed in Escherichia coli	646887
1.4e-05	-	Mus musculus	-	wild-type Ndelta100Cdelta18, expressed in Escherichia coli	646887
1.8e-05	-	Mus musculus	-	mutant Asn-310, expressed in Escherichia coli	646887
0.000375	-	Micrococcus luteus	-	-	646851
0.0247	-	Escherichia coli	-	-	646873
additional information	-	Archaeoglobus fulgidus	-	specific activity 1100 pmol of 3-methyladenine released/mg of protein, 6.7 mg protein/4 ml	646888
additional information	-	Homo sapiens	-	the crude extract shows a specific activity of 80 IU/mg, the 125fold purified enzyme displays a specific activity of 10000 IU/mg, one international unit (IU) is defined as the activity, which cleaves 50% of 0.5 pmole of double stranded DNA oligo substrate containing a hypoxanthine lesion in 10 min at 37�C	701054

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
5.2	-	Archaeoglobus fulgidus	-	-	646888
6.1	-	Escherichia coli	-	-	714251
7	9	Escherichia coli	-	-	646847
7.5	-	Homo sapiens	-	-	701054

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
65	75	Archaeoglobus fulgidus	-	-	646888

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
20	80	Archaeoglobus fulgidus	-	-	646888

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
7.3	7.4	Escherichia coli	-	isoelectric focusing	646847
9.65	-	Homo sapiens	-	isoelectric focusing	701054

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
brain	Mus musculus	-	-	646881
epithelial cell	Homo sapiens	-	normal, malignant and immortalized breast cells	646879
heart	Mus musculus	-	-	646881
kidney	Mus musculus	-	-	646881
lung	Mus musculus	-	-	646881
lymphocyte	Homo sapiens	-	-	668214
MCF-7 cell	Homo sapiens	-	-	646879
MCF10A cell	Homo sapiens	-	immortalized, non-transformed breast epithelial cell line	646879
MDA-MB-231 cell	Homo sapiens	-	-	646879, 646893
muscle	Mus musculus	-	-	646881
ovary	Mus musculus	-	-	646881
stomach	Mus musculus	-	-	646881
T47D cell	Homo sapiens	-	-	646879
thymus	Mus musculus	-	thymic carcinoma	646881

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
mitochondrion	Homo sapiens	-	-	5739	646893

PDB	SCOP	CATH	ORGANISM
2jhj, download	SCOP (2jhj)	CATH (2jhj)	Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
2jhn, download	SCOP (2jhn)	CATH (2jhn)	Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
1diz, download	SCOP (1diz)	CATH (1diz)	Escherichia coli (strain K12)
1mpg, download	SCOP (1mpg)	CATH (1mpg)	Escherichia coli (strain K12)
1pvs, download	SCOP (1pvs)	CATH (1pvs)	Escherichia coli (strain K12)
3cvs, download	SCOP (3cvs)	CATH (3cvs)	Escherichia coli (strain K12)
3cvt, download	SCOP (3cvt)	CATH (3cvt)	Escherichia coli (strain K12)
3cw7, download	SCOP (3cw7)	CATH (3cw7)	Escherichia coli (strain K12)
3cwa, download	SCOP (3cwa)	CATH (3cwa)	Escherichia coli (strain K12)
3cws, download	SCOP (3cws)	CATH (3cws)	Escherichia coli (strain K12)
3cwt, download	SCOP (3cwt)	CATH (3cwt)	Escherichia coli (strain K12)
3cwu, download	SCOP (3cwu)	CATH (3cwu)	Escherichia coli (strain K12)
3d4v, download	SCOP (3d4v)	CATH (3d4v)	Escherichia coli (strain K12)
3ogd, download	SCOP (3ogd)	CATH (3ogd)	Escherichia coli (strain K12)
3oh6, download	SCOP (3oh6)	CATH (3oh6)	Escherichia coli (strain K12)
3oh9, download	SCOP (3oh9)	CATH (3oh9)	Escherichia coli (strain K12)
1bnk, download	SCOP (1bnk)	CATH (1bnk)	Homo sapiens
1ewn, download	SCOP (1ewn)	CATH (1ewn)	Homo sapiens
3qi5, download	SCOP (3qi5)	CATH (3qi5)	Homo sapiens
3uby, download	SCOP (3uby)	CATH (3uby)	Homo sapiens
3s6i, download	SCOP (3s6i)	CATH (3s6i)	Schizosaccharomyces pombe (strain 972 / ATCC 24843)
4b21, download	SCOP (4b21)	CATH (4b21)	Schizosaccharomyces pombe (strain 972 / ATCC 24843)
4b22, download	SCOP (4b22)	CATH (4b22)	Schizosaccharomyces pombe (strain 972 / ATCC 24843)
4b23, download	SCOP (4b23)	CATH (4b23)	Schizosaccharomyces pombe (strain 972 / ATCC 24843)
4b24, download	SCOP (4b24)	CATH (4b24)	Schizosaccharomyces pombe (strain 972 / ATCC 24843)
4hsb, download	SCOP (4hsb)	CATH (4hsb)	Schizosaccharomyces pombe (strain 972 / ATCC 24843)

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
22000	-	Micrococcus luteus	-	gel filtration, Svedberg equation	646851
27000	-	Escherichia coli	-	gel filtration	646846, 646847
31000	-	Escherichia coli	-	SDS-PAGE	646876
31400	-	Escherichia coli	-	-	646855, 646872
32000	-	Homo sapiens	-	SDS-PAGE	646879
33000	-	Homo sapiens	-	SDS-PAGE	701054
34250	-	Archaeoglobus fulgidus	-	predicted from nucleotide sequence	646888
40000	-	Archaeoglobus fulgidus	-	recombinant protein, expressed in Escherichia coli, SDS-PAGE	646888

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
?	Bacillus cereus	-	x * 25000, AlkD, SDS-PAGE	670318

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
at 1.8 A resolution. Structure contains two sodium ions in octahedral coordination	Archaeoglobus fulgidus	-	679498
sitting drop vapour diffusion method, with 85 mM HEPES (pH 7.5), 15% (w/v) PEG 4000, and 17% (v/v) glycerol, at 21�C	Bacillus cereus	-	699549
-	Escherichia coli	-	646885
2.5 A crystal structure colmplexed to DNA, crystals belong to space group P3(1)21, cell dimensions a = B = 82.4 A and c = 199.7 A	Escherichia coli	-	646886
AlkA in complex with undamaged DNA, sitting drop vapor diffusion method, using 25-29% (w/v) polyethylene glycol 3350, 100 mM bis-Tris, pH 6.0-6.6, 200 mM Li2S04, and 3% (w/v) 6-aminocaproic acid, at 25�C	Escherichia coli	-	715554
crystal structure of AlkA solved with the multiple isomorphous replacement method, crystals grown with sitting-drop vapor-diffusion technique, space group P2(1), cell dimensions a = 58.61 A, b = 76.93 A, c = 62.27 A	Escherichia coli	-	646877
hanging drop vapor difusion crystallization, space group P2(1), unit-cell parameters are a = 58.17, b = 76.27, c = 61.69, alpha = gamma = 90�, beta = 109.98�	Escherichia coli	-	646891
sitting drop method of vapour diffusion, monoclinic space group C2, a = 58.6 A, b = 76.8 A, c = 62.2 A	Escherichia coli	-	646872
AAG complexed to DNA	Homo sapiens	-	646885
expression in Saccharomyces cerevisiae	Homo sapiens	-	668249

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
45	-	Archaeoglobus fulgidus	-	activity reduced by 50%	646888
48	-	Escherichia coli	-	relatively heat resistant	646846
48	-	Escherichia coli	-	50% inactivation requires 65 min	646847
50	-	Escherichia coli	-	65 min time for 50% inactivation	646851
50	-	Micrococcus luteus	-	3.5 min, 50% inactivation	646851
50	-	Homo sapiens	-	the purified full-length MPG is stable at high temperature, at 50 �C 30 min of incubation inactivate the protein by 30%	701054
60	-	Micrococcus luteus	-	heat stable, retains 40% of its original activity after 2 min incubation	646851
90	-	Archaeoglobus fulgidus	-	60% enzyme activity retains after incubation for 1 h	646888

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
very unstable	Micrococcus luteus	-	646851

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-70�C, purified enzyme remains stable for more than 4 years when stored in 20% glycerol,	Escherichia coli	-	646873
-20�C, stored in 50% glycerol, undergoes complete inactivation in 3-4 weeks	Micrococcus luteus	-	646851

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-	Archaeoglobus fulgidus	-	646888
-	Bacillus cereus	-	670318
Ni-NTA column chromatography, heparin affinity column chromatography, and gel filtration	Bacillus cereus	-	699549
-	Escherichia coli	-	646855, 646872, 646873, 646883, 646891, 714251
Mono Q column chromatography	Escherichia coli	-	715554
partially	Escherichia coli	-	646846, 646847
purified from an overproducing strain	Escherichia coli	-	646876
purified from overproducing strains DH1 and HB101, harboring plasmid pYN3070	Escherichia coli	-	646877
purified from strain JM105 harboring pAlk10 plasmid	Escherichia coli	-	646878
-	Homo sapiens	-	646879
recombinant protein, purified from Escherichia coli	Homo sapiens	-	646880
SP Sepharose column chromatography	Homo sapiens	-	701054
-	Micrococcus luteus	-	646851
recombinant protein, expressed from baculovirus	Mus musculus	-	646882
recombinant protein, expressed in Escherichia coli	Mus musculus	-	646887, 646889
recombinant protein, purified from Escherichia coli	Rattus norvegicus	-	646880
-	Schizosaccharomyces pombe	-	670427

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
gene afalkA, AF2117 ORF cloned and overexpressed in Escherichia coli, gene function suppresses the alkylation sensitivity in Escherichia coli tag alkA double mutants	Archaeoglobus fulgidus	-	646888
expressed in Escherichia coli HMS174 cells	Bacillus cereus	-	699549
expression in Escherichia coli BL21, AlkD	Bacillus cereus	-	670318
-	Escherichia coli	-	646880, 646884
alkAg+ gene cloned and sequenced	Escherichia coli	-	646848
expressed in Escherichia coli	Escherichia coli	-	714251
-	Homo sapiens	-	646880, 646890
construction of recombinant GST-MPG fusion proteins	Homo sapiens	-	646879
expressed in Escherichia coli BL21(DE3) cells	Homo sapiens	-	701054
overexpressed in MDA-MB231 breast cancer cell line	Homo sapiens	-	646893
cloned and expressed in Escherichia coli BL21(DE3)	Mus musculus	-	646887
MPG deletion mutant N-DELTA100C-DELTA18 overexpressed in Escherichia coli	Mus musculus	-	646889
truncated MPG polypeptides expressed in Escherichia coli using vector pRSET, full length MPG protein cloned in eukaryotic baculovirus expression vector pVL1393 and host Sf9 insect cells used for expression	Mus musculus	-	646882
-	Rattus norvegicus	-	646880
expression by adenoviral system and targeting of enzyme to mitochondria or nucleus of primary astrocytes	Rattus norvegicus	-	680028

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
D113N	Bacillus cereus	-	the mutation results in a 100fold decrease in the single-turnover rate of 7-methylguanine excision relative to the wild type enzyme	699549
R148A	Bacillus cereus	-	the mutation results in a 100fold decrease in the single-turnover rate of 7-methylguanine excision relative to the wild type enzyme	699549
D238N	Escherichia coli	-	site-directed mutagenesis	646877
W218A	Escherichia coli	-	site-directed mutagenesis	646877
N169A	Homo sapiens	-	ratio of 3-methyladenine/7-methylguanine is 29:1 for wild-type enzyme and 26:1 for mutant enzyme N169A, 30fold lower activity than wild-type enzyme. Expression of the N169A in Saccharomyces cerevisiae during methyl methanesulfonate exposure results in greater sensitivity, greater mutation induction following exposure to methyl methanesulfonate and more strand breaks in vivo	668249
N169D	Homo sapiens	-	ratio of 3-methyladenine/7-methylguanine is 29:1 for wild-type enzyme, 100fold lower production of 3-methyladeine and no production of 7-methylguanine is detected with mutant enzyme N169D. When expressed in Saccharomyces cerevisiae, the N169D variant provides better protection against methyl methanesulfonate toxicity than wild-type enzyme. Fewer strand breaks in vivo are seen in the presence of the N169D variant following exposure to methyl methanesulfonate	668249
N169S	Homo sapiens	-	ratio of 3-methyladenine/7-methylguanine is 29:1 for wild-type enzyme and 24:1 for mutant enzyme N169S, 30fold lower activity than wild-type enzyme. Expression of the N169S in Saccharomyces cerevisiae during methyl methanesulfonate exposure results in greater sensitivity, greater mutation induction following exposure to methyl methanesulfonate and more strand breaks in vivo	668249
D112N	Mus musculus	-	site-directed mutagenesis	646887
D152N	Mus musculus	-	site-directed mutagenesis	646887
D252N	Mus musculus	-	site-directed mutagenesis	646887
D259N	Mus musculus	-	site-directed mutagenesis	646887
D260N	Mus musculus	-	site-directed mutagenesis	646887
D310N	Mus musculus	-	site-directed mutagenesis	646887
additional information	Rattus norvegicus	-	recombinant expression of enzyme and targeting to mitochondria or nucleus of primary astrocytes. Increasing enzyme activity significantly increases base excision repair kinetics in both the mitochondria and nuclei. Increased nuclear enzyme activity results in cell death in astrocyte cultures treated with methylnitrososurea	680028

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
inhibition by Cd2+, Ni2+, or Zn2+ can be reversed by EDTA	Homo sapiens	P29372	682910

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
medicine	Escherichia coli	-	sulfur mustard, or mustard gas, bis-(2-chloroethyl)sulfide is carcinogenic to humans, acutely toxic to the skin, repiratory tract and eyes and causes a delayed bone marrow depression, knowledge of the DNA damage caused by this agent and the cellular defenses against this damage are of fundamental importance	646876
medicine	Homo sapiens	-	MPG overexpression is paradoxically associated with increased suspectibility to DNA damage, up-regulation of this gene may suggest a functional role in breast carcinogenesis, animal models using transgenic mice overexpressing the enzyme are being developed to determine the in vivo role of MPG in breast carcinogenesis	646879
medicine	Homo sapiens	-	overexpression of MPG can result in increased kill of tumor cells using lower doses of harmful alkylating agents such as temozolomide and cross-linking agents such as cisplatin, use of lower doses of chemotherapeutic agents, which will decrease the emergence of drug-resistant tumor cells and decrease the need fro stem-cell support, leading to an increased patient response and a better quality of life for the patient	646893
medicine	Rattus norvegicus	-	recombinant expression of enzyme and targeting to mitochondria or nucleus of primary astrocytes. Increasing enzyme activity significantly increases base excision repair kinetics in both the mitochondria and nuclei. Increased nuclear enzyme activity results in cell death in astrocyte cultures treated with methylnitrososurea	680028

DISEASE	TITLE OF PUBLICATION	LINK TO PUBMED
Acquired Immunodeficiency Syndrome	-	PubMed
Adenocarcinoma	-	PubMed, PubMed
Adenoma	-	PubMed, PubMed, PubMed, PubMed, PubMed
Adenomatous Polyposis Coli	-	PubMed, PubMed
Breast Neoplasms	-	PubMed, PubMed, PubMed
Carcinoma	-	PubMed, PubMed, PubMed, PubMed, PubMed, PubMed, PubMed, PubMed, PubMed
Carcinoma, Hepatocellular	-	PubMed
Carcinoma, Non-Small-Cell Lung	-	PubMed
Cell Transformation, Neoplastic	-	PubMed
Cockayne Syndrome	-	PubMed, PubMed
Colitis	-	PubMed
Colonic Neoplasms	-	PubMed, PubMed
Colorectal Neoplasms	-	PubMed, PubMed, PubMed, PubMed, PubMed
Diabetes Mellitus	-	PubMed
Diabetes Mellitus, Type 1	-	PubMed
Diabetes Mellitus, Type 2	-	PubMed
dna-3-methyladenine glycosylase ii deficiency	-	PubMed
Glioblastoma	-	PubMed
Glioma	-	PubMed, PubMed, PubMed
Hepatitis B	-	PubMed
HIV Infections	-	PubMed
Hyperinsulinism	-	PubMed
Hypersensitivity	-	PubMed
Infection	-	PubMed
Lung Neoplasms	-	PubMed, PubMed, PubMed, PubMed, PubMed
Lymphoma, B-Cell	-	PubMed
Melanoma	-	PubMed
Multiple Myeloma	-	PubMed
Neoplasms	-	PubMed, PubMed, PubMed, PubMed, PubMed, PubMed, PubMed, PubMed, PubMed, PubMed, PubMed, PubMed, PubMed, PubMed, PubMed, PubMed
Neurodegenerative Diseases	-	PubMed
Obesity	-	PubMed
Osteosarcoma	-	PubMed
Ovarian Neoplasms	-	PubMed
Retinal Degeneration	-	PubMed
Retinoblastoma	-	PubMed
Stomach Neoplasms	-	PubMed
Thymoma	-	PubMed
Tuberculosis	-	PubMed, PubMed
Urinary Bladder Neoplasms	-	PubMed, PubMed
Uterine Cervical Neoplasms	-	PubMed
Werner Syndrome	-	PubMed, PubMed
Xeroderma Pigmentosum	-	PubMed, PubMed, PubMed

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM (UNIPROT ACCESSION NO.)	LINK TO PUBMED	SOURCE
646845	Evensen, G.; Seeberg, E.	Adaptation to alkylation resistance involves the induction of a DNA glycosylase	Nature	296	773-775	1982	Escherichia coli	PubMed
646846	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	PubMed
646847	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	PubMed
646848	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	PubMed
646851	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	PubMed
646855	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	PubMed
646872	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	PubMed
646873	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	PubMed
646874	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	-
646876	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	PubMed
646877	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	PubMed
646878	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	PubMed
646879	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	PubMed
646880	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	PubMed
646881	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	PubMed
646882	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	PubMed
646883	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	PubMed
646884	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	PubMed
646885	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, Escherichia coli, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Schizosaccharomyces pombe	PubMed
646886	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, Escherichia coli (P04395)	PubMed
646887	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	PubMed
646888	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	PubMed
646889	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	PubMed
646890	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	PubMed
646891	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	Bioconjugate Chem.	13	403-407	2002	Escherichia coli	PubMed
646892	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	PubMed
646893	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	PubMed
668214	Wozniak, K.; Blasiak, J.	Nickel impairs the repair of UV- and MNNG-damaged DNA	Cell. Mol. Biol. Lett.	9	83-94	2004	Homo sapiens	PubMed
668249	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	PubMed
668383	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	PubMed
669235	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	PubMed
670318	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	PubMed
670427	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	PubMed
679498	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	PubMed
680028	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	PubMed
680691	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	PubMed
682910	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, Homo sapiens (P29372)	PubMed
699549	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	PubMed
701054	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	PubMed
714251	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	PubMed
715554	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, Escherichia coli (P04395)	PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 3.2.2.21)

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IUBMB Enzyme Nomenclature

PROSITE Database of protein families and domains

SYSTERS

Protein Mutant Database

InterPro (database of protein families, domains and functional sites)

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