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Information on EC 1.14.11.33 - DNA oxidative demethylase and Organism(s) Homo sapiens
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1.14.11.33 DNA oxidative demethylaseIUBMB Comments
Contains iron; activity is slightly stimulated by ascorbate. Catalyses oxidative demethylation of the DNA base lesions N1-methyladenine, N3-methylcytosine, N1-methylguanine, and N3-methylthymine. It works better on single-stranded DNA (ssDNA) and is capable of repairing damaged bases in RNA.
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Word Map
- 1.14.11.33
-
demethylation
- 3-methylcytosine
-
wobble
- 1,n6-ethenoadenine
-
alkbhs
-
2-oxoglutarate-dependent
-
dealkylation
-
writer
-
etheno
-
epitranscriptomic
-
5-methoxycarbonylmethyluridine
- n1-methyladenosine
- n6-methyladenine
- analysis
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
DNA-base-CH3
+
+
=
DNA-base
+
+
+
Synonyms
alkbh3, alkbh2, alkbh8, alkb homolog 1, alkylated dna repair protein, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ABH1
ABH2
ABH3
AlkB
ALKBH2
ALKBH3
alkylated DNA repair protein
-
-
-
-
alpha-ketoglutarate-dependent dioxygenase ABH1
-
-
-
-
AlkB
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidative demethylation
SYSTEMATIC NAME
IUBMB Comments
methyl DNA-base, 2-oxoglutarate:oxygen oxidoreductase (formaldehyde-forming)
Contains iron; activity is slightly stimulated by ascorbate. Catalyses oxidative demethylation of the DNA base lesions N1-methyladenine, N3-methylcytosine, N1-methylguanine, and N3-methylthymine. It works better on single-stranded DNA (ssDNA) and is capable of repairing damaged bases in RNA.
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
1-ethyladenine + O2 + 2-oxoglutarate
adenine + CO2 + acetaldehyde + succinate + H+
-
-
-
-
?
1-methyl-adenine in 5'-dAAAA-1MeA-YYAAA + 2-oxoglutarate + O2
5'-dAAAAAYYAAA + formaldehyde + succinate + CO2
-
-
-
-
?
1-methyl-dAMP + 2-oxoglutarate + O2
dAMP + formaldehyde + succinate + CO2
-
low activity
-
-
?
1-methyl-dATP + 2-oxoglutarate + O2
dATP + formaldehyde + succinate + CO2
-
low activity
-
-
?
1-methyladenine + O2 + 2-oxoglutarate
adenine + CO2 + formaldehyde + succinate + H+
-
-
-
-
?
2'-deoxy-1-methyl-adenosine 3'-phosphate + 2-oxoglutarate + O2
2'-deoxyadenosine 3'-phosphate + formaldehyde + succinate + CO2
-
low activity
-
-
?
3-methylcytosine + O2 + 2-oxoglutarate
cytosine + CO2 + formaldehyde + succinate + H+
-
-
-
-
?
d(Tpm1A) + 2-oxoglutarate + O2
d(TpA) + formaldehyde + succinate + CO2
-
low activity
-
-
?
d(Tpm1ApT) + 2-oxoglutarate + O2
d(TpApT) + formaldehyde + succinate + CO2
-
low activity
-
-
?
DNA-1-ethyladenine + 2-oxoglutarate + O2
DNA-adenine + acetaldehyde + succinate + CO2
-
-
-
ir
DNA-1-methyldeoxyadenine + 2-oxoglutarate + O2
DNA-deoxyadenine + formaldehyde + succinate + CO2
-
-
-
-
?
DNA-base-CH3 + 2-oxoglutarate + O2
DNA-base + formaldehyde + succinate + CO2
-
-
-
-
?
methylated double-stranded bacteriophage lambda + 2-oxoglutarate + O2
double-stranded bacteriophage lambda + formaldehyde + succinate + CO2
-
-
-
?
methylated luciferase-mRNA + 2-oxoglutarate + O2
luciferase-mRNA + formaldehyde + succinate + CO2
-
-
-
-
?
methylated poly(deoxyadenine) + 2-oxoglutarate + O2
poly(deoxyadenine) + formaldehyde + succinate + CO2
-
-
-
ir
methylated poly(deoxycytosine) + 2-oxoglutarate + O2
poly(deoxycytosine) + formaldehyde + succinate + CO2
-
-
-
ir
methylated poly(deoxythymine) + 2-oxoglutarate + O2
poly(deoxythymine) + formaldehyde + succinate + CO2
-
-
-
-
?
methylated RNA bacteriophage MS2 + 2-oxoglutarate + O2
RNA bacteriophage MS2 + formaldehyde + succinate + CO2
isoform ABH3 reactivates methylated single-stranded RNA bacteriophage MS2
-
-
?
methylated tRNA-Phe + 2-oxoglutarate + O2
tRNAPhe + formaldehyde + succinate + CO2
-
-
-
-
?
N1-methyl-ATP + 2-oxoglutarate + O2
ATP + formaldehyde + succinate + CO2
-
low activity
-
-
?
N3-methylcytosine + 2-oxoglutarate + O2
cytosine + formaldehyde + succinate + CO2
-
-
-
-
?
poly(dm1A) + 2-oxoglutarate + O2
poly(dA) + formaldehyde + succinate + CO2
-
low activity
-
-
?
RNA-1-methyladenine + 2-oxoglutarate + O2
RNA-adenine + formaldehyde + succinate + CO2
-
-
-
-
?
RNA-3-methylcytosine + 2-oxoglutarate + O2
RNA-cytosine + formaldehyde + succinate + CO2
-
-
-
-
?
tRNA-1-methylguanine + 2-oxoglutarate + O2
tRNA-guanine + formaldehyde + succinate + CO2
-
-
-
-
?
DNA-1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
-
-
-
-
?
DNA-1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
-
-
-
?
DNA-1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
-
-
-
-
?
DNA-1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
-
-
-
?
DNA-1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
good substrate
-
-
ir
DNA-1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
-
DNA-1-methyladenine is demethylated by isoforms ABH2 and ABH3
-
-
?
DNA-1-methylguanine + 2-oxoglutarate + O2
DNA-guanine + formaldehyde + succinate + CO2
weak substrate
-
-
ir
DNA-1-methylguanine + 2-oxoglutarate + O2
DNA-guanine + formaldehyde + succinate + CO2
-
DNA-1-methylguanine is also repaired by AlkB, but less efficiently as DNA-1-methyladenine or DNA-3-methylcytosine
-
-
?
DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
-
-
-
?
DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
-
-
?
DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
-
-
-
?
DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
-
-
?
DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
good substrate
-
-
ir
DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
DNA-1-methylcytosine is demethylated by isoforms ABH2 and ABH3. Isoform ABH1 exclusively repairs DNA-3-methylcytosine in single-stranded DNA with low activity
-
-
?
DNA-3-methylthymine + 2-oxoglutarate + O2
DNA-thymine + formaldehyde + succinate + CO2
-
-
-
-
?
DNA-3-methylthymine + 2-oxoglutarate + O2
DNA-thymine + formaldehyde + succinate + CO2
weak substrate
-
-
ir
DNA-3-methylthymine + 2-oxoglutarate + O2
DNA-thymine + formaldehyde + succinate + CO2
-
3-methylthymine residues in DNA is repaired inefficiently in vivo. The ABH3 protein repairs 3-methylthymine in both single-stranded and double-stranded polydeoxynucleotides, whereas the ABH2 protein prefers a duplex substrate
-
-
?
DNA-3-methylthymine + 2-oxoglutarate + O2
DNA-thymine + formaldehyde + succinate + CO2
-
DNA-3-methylthymine is also repaired by AlkB, but less efficiently as DNA-1-methyladenine or DNA-3-methylcytosine. Isoform FTO repairs DNA-3-methylthymine
-
-
?
additional information
?
-
-
isoform ABH2 does not reactivate methylated RNA bacteriophage MS2 or methylated double-stranded bacteriophage lambda
-
-
?
additional information
?
-
isoform ABH2 does not reactivate methylated RNA bacteriophage MS2 or methylated double-stranded bacteriophage lambda
-
-
?
additional information
?
-
-
ABH3 prefers single-stranded DNA and RNA substrates, whereas ABH2 can repair damage in both single- and double-stranded DNA. Isoform ABH1 does not show any DNA repair activity
-
-
?
additional information
?
-
-
ABH2 does not repair RNA. ABH2 acts more efficiently on double-stranded DNA
-
-
?
additional information
?
-
ABH2 does not repair RNA. ABH2 acts more efficiently on double-stranded DNA
-
-
?
additional information
?
-
-
ABH3 also repairs RNA. ABH3 prefers single-stranded nucleic acids
-
-
?
additional information
?
-
ABH3 also repairs RNA. ABH3 prefers single-stranded nucleic acids
-
-
?
additional information
?
-
-
isoform ABH2 prefers double-stranded DNA while isoforms ABH3 and ABH1 work better on single-stranded substrates
-
-
?
additional information
?
-
isoform ABH2 shows some preference for methylated poly(dA) over methylated poly(dC) and also prefers a double-stranded substrate. not ABH2 cannot demethylate 1-methyladenine in RNA
-
-
?
additional information
?
-
isoform ABH2 shows some preference for methylated poly(dA) over methylated poly(dC) and also prefers a double-stranded substrate. not ABH2 cannot demethylate 1-methyladenine in RNA
-
-
?
additional information
?
-
isoform ABH2 shows some preference for methylated poly(dC) over methylated poly(dA) and also prefers a single-stranded substrate. Isoform ABH3 can also demethylate 1-methyladenine in RNA
-
-
?
additional information
?
-
isoform ABH2 shows some preference for methylated poly(dC) over methylated poly(dA) and also prefers a single-stranded substrate. Isoform ABH3 can also demethylate 1-methyladenine in RNA
-
-
?
additional information
?
-
-
isoform ABH3 prefers single-stranded DNA (also under magnesium-free conditions) and RNA, while isoform ABH2 prefers double-stranded DNA (only in the presence of magnesium) and RNA
-
-
?
additional information
?
-
-
repair of alkylated poly(A) by ABH3 is almost as efficient as repair of poly(dA), and repair of poly(C) is substantially more efficient than repair of poly(dA), although not as good as repair of poly(dC) and single-stranded bacteriophage M13 DNA
-
-
?
additional information
?
-
repair of alkylated poly(A) by ABH3 is almost as efficient as repair of poly(dA), and repair of poly(C) is substantially more efficient than repair of poly(dA), although not as good as repair of poly(dC) and single-stranded bacteriophage M13 DNA
-
-
?
additional information
?
-
-
the enzyme does not demethylate 3-methyladenine, 7-methyladenine, 7-methylguanine, thymine (5-methyluracil), and 5-methylcytosine
-
-
?
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
DNA-base-CH3 + 2-oxoglutarate + O2
DNA-base + formaldehyde + succinate + CO2
-
-
-
-
?
methylated double-stranded bacteriophage lambda + 2-oxoglutarate + O2
double-stranded bacteriophage lambda + formaldehyde + succinate + CO2
-
-
-
?
methylated RNA bacteriophage MS2 + 2-oxoglutarate + O2
RNA bacteriophage MS2 + formaldehyde + succinate + CO2
isoform ABH3 reactivates methylated single-stranded RNA bacteriophage MS2
-
-
?
N3-methylcytosine + 2-oxoglutarate + O2
cytosine + formaldehyde + succinate + CO2
-
-
-
-
?
DNA-1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
-
-
-
-
?
DNA-1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
-
-
-
?
DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
-
-
-
?
DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
-
-
?
additional information
?
-
-
isoform ABH2 does not reactivate methylated RNA bacteriophage MS2 or methylated double-stranded bacteriophage lambda
-
-
?
additional information
?
-
isoform ABH2 does not reactivate methylated RNA bacteriophage MS2 or methylated double-stranded bacteriophage lambda
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Mg2+
-
the double-stranded DNA preference of isoform ABH2 is observed only in the presence of magnesium, the presence of magnesium stimulates the activity of isoform ABH2 on double-stranded DNA, but inhibits its activity on single-stranded DNA (maximal effect is observed in the presence of 10 mM MgCl2)
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0004
1-methyl-adenine in 5'-dAAAA-1MeA-YYAAA
-
pH not specified in the publication, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
1-methyl-adenine in 5'-dAAAA-1MeA-YYAAA
-
pH not specified in the publication, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
D-2-hydroxyglutarate
Homo sapiens
-
isoform ALKBH2, pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
repair of DNA-3-methylthymine by ABH3 is optimal at pH 6.5, but inefficient
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
actinomycin D treatment resulted in nuclear localization of ABH2. DNAse I treatment results in a loss of ABH2 nucleolar localization. ABH2 nucleolar localization is dependent on its association with both DNA and RNA
-
-
nucleolar localization sequence RKRPRR at aa38-aa43 of ABH2, mutation of RKR to AAA within this sequence impaired the nuclear and nucleolar localization of ABH2 in HeLa cells. ABH2 associates with nucleolar proteins NCL, NPM1, and UBF
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
ABH2 knockdown impairs rDNA transcription and leads to increased single-stranded and double-stranded DNA breaks that are more pronounced in the rDNA genes, whereas ABH2 overexpression protects cells from methyl-methanesulfonate-induced DNA damage and inhibition of rDNA transcription
physiological function
additional information
-
ABH2 associates with DNA repair proteins Ku70/Ku80, overview
physiological function
-
ABH3 restores the biological function of mRNA and tRNA inactivated by chemical methylation. A methylation-induced block in translation of an mRNA can be readily relieved by treatment with ABH3 prior to translation. Chemical methylation of tRNA-Phe inhibits aminoacylation and translation, but the inhibition can be reversed by ABH3
physiological function
-
AlkB corrects some of the unwanted methylations of DNA bases by a unique oxidative demethylation in which the methyl carbon is liberated as formaldehyde. The enzyme also repairs exocyclic DNA lesions
physiological function
isoform ABH2 repairs DNA close to the replication forks, is more active on double-stranded than on single-stranded DNA and is present in different subnuclear compartments at different stages of the cell cycle
physiological function
the nuclear localization of ABH3 and the clear preference for single-stranded DNA and RNA suggest that ABH3 has a role in maintenance of nuclear single-stranded DNA and RNA, with genes undergoing transcription potentially being its main targets
physiological function
-
critical role of ABH2 in maintaining rDNA gene integrity and transcription, the DNA alkylation repair enzyme ABH2/ALKBH2 is highly enriched in the nucleolus. ABH2 overexpression protects cells from methyl-methanesulfonate-induced DNA damage and inhibition of rDNA transcription. In response to massive alkylation damage, ABH2 rapidly redistributes from the nucleolus to nucleoplasm. ABH2 interacts with DNA repair proteins Ku70 and Ku80 as well as nucleolar proteins nucleolin, nucleophosmin 1, and upstream binding factor. ABH2 associates with and promotes rDNA transcription through its DNA repair activity. The physical association between ABH2 and Ku70/Ku80 may help mobilize ABH2 to DSBs to remove alkylation damage and thus facilitate the DNA repair process, or the physical association between ABH2 and Ku70/Ku80 may allow Ku70/Ku80 to sense the potential sites of DSBs through recognition of alkylation damages by ABH2
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ALKB1_HUMAN
389
0
43832
Swiss-Prot
other Location (Reliability: 5)
ALKB2_HUMAN
261
0
29322
Swiss-Prot
other Location (Reliability: 2)
ALKB3_HUMAN
286
0
33375
Swiss-Prot
Mitochondrion (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D173A
-
site-directed mutagenesis, the mutant maintains nucleolar localization, but is not able to enhance transcription from the rDNA luciferase reporter. eÉctopic expression of wild-type ABH2 leads to a 2.5fold increase of pre-rRNA, whereas ectopic expression of D173A mutant only leads to a marginal increase of pre-rRNA
H131C
-
the mutant slightly prefers single-stranded DNA substrates over any double-stranded DNA
H171C
-
the ABH2 mutant shows indistinguishable chromatographic behaviors from those of the wild type proteins and cross-links efficiently with the single-stranded DNA-1 and DNA3-6
H191C
-
the ABH3 mutant shows indistinguishable chromatographic behaviors from those of the wild type proteins and cross-links to DNA-1 much more efficiently than the wild type protein after a 20 h incubation
H231C
-
the ABH1 mutant shows indistinguishable chromatographic behaviors from those of the wild type proteins, no cross-link between the mutant protein and the single-stranded and double-stranded DNA probes is observed
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose column chromatography, S-Sepharose column chromatography, Ni-NTA column chromatography, and Mono-S cation exchange column chromatography
-
His-tagged enzyme is purified by Ni-NTA agarose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells and in Sf9 insect cells
expressed in Escherichia coli BL21(DE3) cells and in Sf9 insect cells. ABH3 expressed in insect cells contains no posttranslational modifications but is nevertheless found to be 5fold more active than ABH3 purified from Escherichia coli, suggesting ABH3 may not be correctly folded when purified from Escherichia coli
-
expression of GFP-tagged enzyme in HeLa cells, localization in nucleoli due to the genuine nucleolar localization signal sequence. Ectopic expression of wild-type ABH2 leads to a 2.5fold increase of pre-rRNA, whereas ectopic expression of D173A mutant only leads to a marginal increase of pre-rRNA
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
development of a fluorogenic probe design (MAQ) that is directly responsive to ALKBH3 repair activity. MAQ uses the fluorescence-quenching properties of 1-methyladenine, removal of the alkyl group results in an more than 10fold light-up signal. The probe is specific for ALKBH3 over its related homologue ALKBH2 and can be used to identify and measure the effectiveness of enzyme inhibitors. The probe functions efficiently in cells, allowing imaging and quantitation of ALKBH3 activity by microscopy and flow cytometry
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yi, C.; Yang, C.G.; He, C.
A non-heme iron-mediated chemical demethylation in DNA and RNA
Acc. Chem. Res.
42
519-529
2009
Escherichia coli, Homo sapiens
Koivisto, P.; Duncan, T.; Lindahl, T.; Sedgwick, B.
Minimal methylated substrate and extended substrate range of Escherichia coli AlkB protein, a 1-methyladenine-DNA dioxygenase
J. Biol. Chem.
278
44348-44354
2003
Escherichia coli, Homo sapiens
Koivisto, P.; Robins, P.; Lindahl, T.; Sedgwick, B.
Demethylation of 3-methylthymine in DNA by bacterial and human DNA dioxygenases
J. Biol. Chem.
279
40470-40474
2004
Escherichia coli, Homo sapiens
Sedgwick, B.; Robins, P.; Lindahl, T.
Direct removal of alkylation damage from DNA by AlkB and related DNA dioxygenases
Methods Enzymol.
408
108-120
2006
Escherichia coli (P05050), Homo sapiens (Q6NS38), Homo sapiens (Q96Q83)
Ougland, R.; Zhang, C.M.; Liiv, A.; Johansen, R.F.; Seeberg, E.; Hou, Y.M.; Remme, J.; Falnes, P.O.
AlkB restores the biological function of mRNA and tRNA inactivated by chemical methylation
Mol. Cell
16
107-116
2004
Escherichia coli, Homo sapiens
Aas, P.A.; Otterlei, M.; Falnes, P.O.; Vagbo, C.B.; Skorpen, F.; Akbari, M.; Sundheim, O.; Bjoras, M.; Slupphaug, G.; Seeberg, E.; Krokan, H.E.
Human and bacterial oxidative demethylases repair alkylation damage in both RNA and DNA
Nature
421
859-863
2003
Escherichia coli, Homo sapiens, Homo sapiens (Q96Q83)
Mishina, Y.; Lee, C.H.; He, C.
Interaction of human and bacterial AlkB proteins with DNA as probed through chemical cross-linking studies
Nucleic Acids Res.
32
1548-1554
2004
Escherichia coli, Homo sapiens
Falnes, P.O.; Bjoras, M.; Aas, P.A.; Sundheim, O.; Seeberg, E.
Substrate specificities of bacterial and human AlkB proteins
Nucleic Acids Res.
32
3456-3461
2004
Escherichia coli, Homo sapiens
Falnes, P.O.
Repair of 3-methylthymine and 1-methylguanine lesions by bacterial and human AlkB proteins
Nucleic Acids Res.
32
6260-6267
2004
Escherichia coli, Homo sapiens
Duncan, T.; Trewick, S.C.; Koivisto, P.; Bates, P.A.; Lindahl, T.; Sedgwick, B.
Reversal of DNA alkylation damage by two human dioxygenases
Proc. Natl. Acad. Sci. USA
99
16660-5
2002
Homo sapiens
Li, P.; Gao, S.; Wang, L.; Yu, F.; Li, J.; Wang, C.; Li, J.; Wong, J.
ABH2 couples regulation of ribosomal DNA transcription with DNA alkylation repair
Cell Rep.
4
817-829
2013
Homo sapiens
Beharry, A.A.; Lacoste, S.; OConnor, T.R.; Kool, E.T.
Fluorescence monitoring of the oxidative repair of DNA alkylation damage by ALKBH3, a prostate cancer marker
J. Am. Chem. Soc.
138
3647-3650
2016
Homo sapiens
Wang, P.; Wu, J.; Ma, S.; Zhang, L.; Yao, J.; Hoadley, K.A.; Wilkerson, M.D.; Perou, C.M.; Guan, K.L.; Ye, D.; Xiong, Y.
Oncometabolite D-2-hydroxyglutarate inhibits ALKBH DNA repair enzymes and sensitizes IDH mutant cells to alkylating agents
Cell Rep.
13
2353-2361
2015
Homo sapiens
Silvestrov, P.; Mueller, T.A.; Clark, K.N.; Hausinger, R.P.; Cisneros, G.A.
Homology modeling, molecular dynamics, and site-directed mutagenesis study of AlkB human homolog 1 (ALKBH1)
J. Mol. Graph. Model.
54
123-130
2014
Homo sapiens
EXTERNAL LINKS (specific for EC-Number 1.14.11.33)
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Release 2023.1 (January 2023)
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