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Information on EC 1.14.11.33 - DNA oxidative demethylase
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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
- glycosylase
-
alkbhs
-
writer
-
dealkylation
- demethylases
- 1,n6-ethenoadenine
-
2-oxoglutarate-dependent
-
epitranscriptomic
-
5-methoxycarbonylmethyluridine
- n1-methyladenosine
-
etheno
- analysis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
DNA-base-CH3
+
+
=
DNA-base
+
+
+
Synonyms
alkbh3, alkbh2, alkbh8, alkb homolog 1, alkylated dna repair protein, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-methyladenine-DNA dioxygenase
ABH1
ABH2
ABH3
AlkB
ALKBH2
ALKBH3
ALKBH8
AlkB
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA-base-CH3 + 2-oxoglutarate + O2 = DNA-base + formaldehyde + succinate + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
demethylation
oxidative demethylation
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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.
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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-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
3-methylcytosine + O2 + 2-oxoglutarate
cytosine + CO2 + formaldehyde + succinate + H+
-
-
-
?
DNA-1,N6-ethenoadenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
-
-
?
DNA-1-methylcytosine-CH3 + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
DNA-1-methyldeoxyadenine + 2-oxoglutarate + O2
DNA-deoxyadenine + formaldehyde + succinate + CO2
-
-
-
?
DNA-2-methylguanosine + 2-oxoglutarate + O2
DNA-guanosine + formaldehyde + succinate + CO2
-
-
?
DNA-N1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
highest activity
-
?
double-stranded DNA-1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
-
major substrate, AlkB demethylates DNA-1-methyladenine and DNA-3-methylcytosine with comparable efficiencies and has only a modest preference for a single-stranded DNA substrate over its double-stranded DNA counterpart
-
?
double-stranded DNA-1-methyladenine + 2-oxoglutarate + O2
double-stranded DNA-adenine + formaldehyde + succinate + CO2
-
major substrate, AlkB demethylates DNA-1-methyladenine and DNA-3-methylcytosine with comparable efficiencies and has only a modest preference for a single-stranded DNA substrate over its double-stranded DNA counterpart
-
?
double-stranded DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
major substrate, AlkB demethylates DNA-1-methyladenine and DNA-3-methylcytosine with comparable efficiencies and has only a modest preference for a single-stranded DNA substrate over its double-stranded DNA counterpart
-
?
double-stranded DNA-3-methylcytosine + 2-oxoglutarate + O2
double-stranded DNA-cytosine + formaldehyde + succinate + CO2
-
major substrate, AlkB demethylates DNA-1-methyladenine and DNA-3-methylcytosine with comparable efficiencies and has only a modest preference for a single-stranded DNA substrate over its double-stranded DNA counterpart
-
?
methylated DNA bacteriophage M13mp18 + 2-oxoglutarate + O2
DNA bacteriophage M13mp18 + 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
methylated poly(deoxycytosine) + 2-oxoglutarate + O2
poly(deoxycytosine) + formaldehyde + succinate + CO2
methylated poly(deoxythymine) + 2-oxoglutarate + O2
poly(deoxythymine) + formaldehyde + succinate + CO2
methylated RNA bacteriophage MS2 + 2-oxoglutarate + O2
RNA bacteriophage MS2 + formaldehyde + succinate + CO2
methylated single-stranded poly(deoxyadenosine) + 2-oxoglutarate + O2
single-stranded poly(deoxyadenosine) + formaldehyde + succinate + CO2
methylated tRNA-Phe + 2-oxoglutarate + O2
tRNA-Phe + formaldehyde + succinate + CO2
-
-
-
?
methylated tRNA-Phe + 2-oxoglutarate + O2
tRNAPhe + formaldehyde + succinate + CO2
-
-
-
?
N1-methyladenine in DNA + 2-oxoglutarate + O2
adenine in DNA + formaldehyde + succinate + CO2
-
strong substrate in ss-DNA
-
?
N1-methylguanine in DNA + 2-oxoglutarate + O2
guanine in DNA + formaldehyde + succinate + CO2
-
weak substrate in ds-DNA
-
?
N3-methylcytosine in DNA + 2-oxoglutarate + O2
cytosine in DNA + formaldehyde + succinate + CO2
-
strong substrate in ss-DNA
-
?
N3-methylthymine in DNA + 2-oxoglutarate + O2
thymine in DNA + formaldehyde + succinate + CO2
-
weak substrate in ds-DNA
-
?
N6-methyladenine + 2-oxoglutarate + O2
adenine + formaldehyde + succinate + CO2
-
via 6-hydroxymethyl adenine derivative
-
?
single-stranded DNA-1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
-
major substrate, AlkB demethylates DNA-1-methyladenine and DNA-3-methylcytosine with comparable efficiencies and has only a modest preference for a single-stranded DNA substrate over its double-stranded DNA counterpart
-
?
single-stranded DNA-1-methyladenine + 2-oxoglutarate + O2
single-stranded DNA-adenine + formaldehyde + succinate + CO2
-
major substrate, AlkB demethylates DNA-1-methyladenine and DNA-3-methylcytosine with comparable efficiencies and has only a modest preference for a single-stranded DNA substrate over its double-stranded DNA counterpart
-
?
single-stranded DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
major substrate, AlkB demethylates DNA-1-methyladenine and DNA-3-methylcytosine with comparable efficiencies and has only a modest preference for a single-stranded DNA substrate over its double-stranded DNA counterpart
-
?
single-stranded DNA-3-methylcytosine + 2-oxoglutarate + O2
single-stranded DNA-cytosine + formaldehyde + succinate + CO2
-
major substrate, AlkB demethylates DNA-1-methyladenine and DNA-3-methylcytosine with comparable efficiencies and has only a modest preference for a single-stranded DNA substrate over its double-stranded DNA counterpart
-
?
1-methyl-dAMP + 2-oxoglutarate + O2
dAMP + 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
-
-
-
?
1-methyl-dATP + 2-oxoglutarate + O2
dATP + formaldehyde + succinate + CO2
-
low activity
-
?
2'-deoxy-1-methyl-adenosine 3'-phosphate + 2-oxoglutarate + O2
2'-deoxyadenosine 3'-phosphate + formaldehyde + succinate + CO2
-
-
-
?
2'-deoxy-1-methyl-adenosine 3'-phosphate + 2-oxoglutarate + O2
2'-deoxyadenosine 3'-phosphate + formaldehyde + succinate + CO2
-
low activity
-
?
d(Tpm1A) + 2-oxoglutarate + O2
d(TpA) + formaldehyde + succinate + CO2
-
-
-
?
d(Tpm1A) + 2-oxoglutarate + O2
d(TpA) + formaldehyde + succinate + CO2
-
low activity
-
?
d(Tpm1ApT) + 2-oxoglutarate + O2
d(TpApT) + formaldehyde + succinate + CO2
-
-
-
?
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-ethyladenine + 2-oxoglutarate + O2
DNA-adenine + acetaldehyde + succinate + CO2
-
-
ir
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
-
best substrate for AlkB
-
?
DNA-1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
-
purified AlkB repairs the cytotoxic lesion 1-methyladenine in single- and double-stranded DNA
-
?
DNA-1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
-
this reaction occurs on both single- and double-stranded DNA
-
?
DNA-1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
Escherichia coli W3110 / ATCC 27325
-
-
-
?
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
-
-
?
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-methylcytosine-CH3 + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
-
-
?
DNA-1-methylcytosine-CH3 + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
-
-
?
DNA-1-methylcytosine-CH3 + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
Agrobacterium tumefaciens C58 / ATCC 33970
-
-
-
?
DNA-1-methylcytosine-CH3 + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
-
-
?
DNA-1-methylcytosine-CH3 + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
-
-
?
DNA-1-methylcytosine-CH3 + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
-
?
DNA-1-methylcytosine-CH3 + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
-
?
DNA-1-methylcytosine-CH3 + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
-
-
?
DNA-1-methylcytosine-CH3 + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
-
-
?
DNA-1-methylguanine + 2-oxoglutarate + O2
DNA-guanine + formaldehyde + succinate + CO2
-
-
-
?
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-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,N4-ethenocytosine + 2-oxoglutarate + O2
?
-
high activity
-
?
DNA-3,N4-ethenocytosine + 2-oxoglutarate + O2
?
-
high activity
-
?
DNA-3,N4-ethenocytosine + 2-oxoglutarate + O2
?
Agrobacterium tumefaciens C58 / ATCC 33970
-
high activity
-
?
DNA-3,N4-ethenocytosine + 2-oxoglutarate + O2
?
high activity
-
?
DNA-3,N4-ethenocytosine + 2-oxoglutarate + O2
?
high activity
-
?
DNA-3,N4-ethenocytosine + 2-oxoglutarate + O2
?
-
high activity
-
?
DNA-3,N4-ethenocytosine + 2-oxoglutarate + O2
?
-
high activity
-
?
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
-
best substrate for AlkB
-
?
DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
preferred substrate of AlkB
-
?
DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
purified AlkB repairs the cytotoxic lesion 3-methylcytosine in single- and double-stranded DNA
-
?
DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
this reaction occurs on both single- and double-stranded DNA
-
?
DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
Escherichia coli W3110 / ATCC 27325
-
-
-
?
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
-
-
?
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
-
-
?
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 AlkB protein repairs 3-methylthymine in both single-stranded and double-stranded polydeoxynucleotidese
-
?
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
-
?
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
-
?
DNA-base-CH3 + 2-oxoglutarate + O2
DNA-base + formaldehyde + succinate + CO2
-
-
-
?
DNA-base-CH3 + 2-oxoglutarate + O2
DNA-base + formaldehyde + succinate + CO2
-
-
?
DNA-base-CH3 + 2-oxoglutarate + O2
DNA-base + formaldehyde + succinate + CO2
-
-
-
?
DNA-base-CH3 + 2-oxoglutarate + O2
DNA-base + formaldehyde + succinate + CO2
-
-
-
?
methylated DNA bacteriophage M13mp18 + 2-oxoglutarate + O2
DNA bacteriophage M13mp18 + formaldehyde + succinate + CO2
-
-
-
?
methylated DNA bacteriophage M13mp18 + 2-oxoglutarate + O2
DNA bacteriophage M13mp18 + formaldehyde + succinate + CO2
-
-
-
?
methylated DNA bacteriophage M13mp18 + 2-oxoglutarate + O2
DNA bacteriophage M13mp18 + formaldehyde + succinate + CO2
-
-
-
?
methylated luciferase-mRNA + 2-oxoglutarate + O2
luciferase-mRNA + formaldehyde + succinate + CO2
-
AlkB is used at a maximal concentration of 0.00083 mM for this reaction since the luciferase-mRNA is degraded when higher AlkB concentrations are used
-
?
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(deoxyadenine) + 2-oxoglutarate + O2
poly(deoxyadenine) + formaldehyde + succinate + CO2
-
0.1 pmol AlkB protein removes 1.7 pmol 1-methyladenine from methylated poly(deoxyadenine) in 15 min
-
?
methylated poly(deoxyadenine) + 2-oxoglutarate + O2
poly(deoxyadenine) + formaldehyde + succinate + CO2
-
the activity of AlkB on methylated poly(deoxyadenine) annealed to unmethylated poly(deoxythymine) is 3fold higher than with methylated poly(deoxyadenine) alone
-
?
methylated poly(deoxyadenine) + 2-oxoglutarate + O2
poly(deoxyadenine) + formaldehyde + succinate + CO2
-
-
ir
methylated poly(deoxycytosine) + 2-oxoglutarate + O2
poly(deoxycytosine) + formaldehyde + succinate + CO2
-
-
-
?
methylated poly(deoxycytosine) + 2-oxoglutarate + O2
poly(deoxycytosine) + 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 poly(deoxythymine) + 2-oxoglutarate + O2
poly(deoxythymine) + formaldehyde + succinate + CO2
-
-
-
?
methylated RNA bacteriophage MS2 + 2-oxoglutarate + O2
RNA bacteriophage MS2 + formaldehyde + succinate + CO2
-
-
-
?
methylated RNA bacteriophage MS2 + 2-oxoglutarate + O2
RNA bacteriophage MS2 + formaldehyde + succinate + CO2
-
-
-
?
methylated RNA bacteriophage MS2 + 2-oxoglutarate + O2
RNA bacteriophage MS2 + 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 single-stranded poly(deoxyadenosine) + 2-oxoglutarate + O2
single-stranded poly(deoxyadenosine) + formaldehyde + succinate + CO2
-
-
-
?
methylated single-stranded poly(deoxyadenosine) + 2-oxoglutarate + O2
single-stranded poly(deoxyadenosine) + formaldehyde + succinate + CO2
Escherichia coli W3110 / ATCC 27325
-
-
-
?
N1-methyl-ATP + 2-oxoglutarate + O2
ATP + formaldehyde + succinate + CO2
-
-
-
?
N1-methyl-ATP + 2-oxoglutarate + O2
ATP + formaldehyde + succinate + CO2
-
low activity
-
?
N1-methyladenine + 2-oxoglutarate + O2
adenine + formaldehyde + succinate + CO2
-
-
-
?
N1-methyladenine + 2-oxoglutarate + O2
adenine + formaldehyde + succinate + CO2
-
-
-
?
N3-methylcytosine + 2-oxoglutarate + O2
cytosine + formaldehyde + succinate + CO2
-
-
-
?
N3-methylcytosine + 2-oxoglutarate + O2
cytosine + formaldehyde + succinate + CO2
-
-
-
?
N3-methylcytosine + 2-oxoglutarate + O2
cytosine + formaldehyde + succinate + CO2
-
-
-
?
poly(dm1A) + 2-oxoglutarate + O2
poly(dA) + 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-1-methyladenine + 2-oxoglutarate + O2
RNA-adenine + formaldehyde + succinate + CO2
-
-
-
?
RNA-1-methyladenine + 2-oxoglutarate + O2
RNA-adenine + formaldehyde + succinate + CO2
-
-
-
?
RNA-1-methyladenine + 2-oxoglutarate + O2
RNA-adenine + formaldehyde + succinate + CO2
-
-
-
?
RNA-1-methyladenine + 2-oxoglutarate + O2
RNA-adenine + formaldehyde + succinate + CO2
-
-
-
?
RNA-3-methylcytosine + 2-oxoglutarate + O2
RNA-cytosine + formaldehyde + succinate + CO2
-
-
-
?
RNA-3-methylcytosine + 2-oxoglutarate + O2
RNA-cytosine + formaldehyde + succinate + CO2
-
-
-
?
RNA-3-methylcytosine + 2-oxoglutarate + O2
RNA-cytosine + formaldehyde + succinate + CO2
-
-
-
?
RNA-3-methylcytosine + 2-oxoglutarate + O2
RNA-cytosine + formaldehyde + succinate + CO2
-
-
-
?
RNA-3-methylcytosine + 2-oxoglutarate + O2
RNA-cytosine + formaldehyde + succinate + CO2
-
-
-
?
RNA-base-CH3 + 2-oxoglutarate + O2
RNA-base + formaldehyde + succinate + CO2
-
-
-
?
RNA-base-CH3 + 2-oxoglutarate + O2
RNA-base + formaldehyde + succinate + CO2
-
-
-
?
tRNA-1-methylguanine + 2-oxoglutarate + O2
tRNA-guanine + formaldehyde + succinate + CO2
-
-
-
?
tRNA-1-methylguanine + 2-oxoglutarate + O2
tRNA-guanine + formaldehyde + succinate + CO2
-
-
-
?
additional information
?
-
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
?
additional information
?
-
-
no activity with DNA-1-methyladenine-CH3
-
?
additional information
?
-
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
?
additional information
?
-
-
no activity with DNA-1-methyladenine-CH3
-
?
additional information
?
-
Agrobacterium tumefaciens C58 / ATCC 33970
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
?
additional information
?
-
Agrobacterium tumefaciens C58 / ATCC 33970
-
no activity with DNA-1-methyladenine-CH3
-
?
additional information
?
-
-
the viral AlkB protein prefers single-stranded RNA over single-stranded DNA substrates (10fold)
-
?
additional information
?
-
-
the viral AlkB protein prefers single-stranded RNA over single-stranded DNA substrates (10fold)
-
?
additional information
?
-
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
?
additional information
?
-
-
no activity with DNA-1-methyladenine-CH3
-
?
additional information
?
-
-
adenosine, deoxythymine, 3-methyldeoxythymidine, guanosine, 1-methylguanosine, 1-methylguanine and 3-methylthymine do not stimulate AlkB-mediated decarboxylation of 2-oxoglutarate
-
?
additional information
?
-
-
AlkB also repairs RNA. AlkB prefers single-stranded nucleic acids.
-
?
additional information
?
-
AlkB binds to single-stranded DNA, but less efficiently to double-stranded DNA
-
?
additional information
?
-
-
AlkB can repair damage in both single- and double-stranded DNA
-
?
additional information
?
-
-
AlkB has no detectable nuclease, DNA glycosylase or methyltransferase activity
-
?
additional information
?
-
-
AlkB preferentially binds and reactivates methylated single-stranded DNA
-
?
additional information
?
-
-
although the lesions targeted by AlkB are introduced primarily into single-stranded DNA, AlkB is also capable of removing lesions from double-stranded DNA
-
?
additional information
?
-
-
Escherichia coli AlkB is approximately 10fold more active on single-stranded DNA compared to single-stranded RNA, Eschichia coli AlkB displays a somewhat lower activity on double-stranded RNA substrates than on single-stranded RNA substrates
-
?
additional information
?
-
-
the enzyme does not demethylate 3-methyladenine, 7-methyladenine, 7-methylguanine, thymine (5-methyluracil), and 5-methylcytosine
-
?
additional information
?
-
-
exocyclic carbons adjacent to the N6 of adenine are targets for oxidation by the Escherichia coli adaptive response protein AlkB
-
?
additional information
?
-
-
AlkB prefers to repair N1-methylguanine and N3-methylthymine lesions in ds-DNA over ss-DNA. The enzyme is able to repair the lesion when the adduct is present in a mismatched base pair
-
?
additional information
?
-
Escherichia coli W3110 / ATCC 27325
-
although the lesions targeted by AlkB are introduced primarily into single-stranded DNA, AlkB is also capable of removing lesions from double-stranded DNA
-
?
additional information
?
-
-
the viral AlkB protein prefers single-stranded RNA over single-stranded DNA substrates (10fold)
-
?
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
-
?
additional information
?
-
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
?
additional information
?
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
?
additional information
?
-
no activity with DNA-1-methyladenine-CH3
-
?
additional information
?
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
?
additional information
?
-
no activity with DNA-1-methyladenine-CH3
-
?
additional information
?
-
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
?
additional information
?
-
-
no activity with DNA-1-methyladenine-CH3
-
?
additional information
?
-
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
?
additional information
?
-
-
no activity with DNA-1-methyladenine-CH3
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-1,N6-ethenoadenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
-
-
-
?
DNA-1-methylguanine + 2-oxoglutarate + O2
DNA-guanine + formaldehyde + succinate + CO2
-
-
-
-
?
DNA-2-methylguanosine + 2-oxoglutarate + O2
DNA-guanosine + formaldehyde + succinate + CO2
-
-
-
?
DNA-3-methylthymine + 2-oxoglutarate + O2
DNA-thymine + formaldehyde + succinate + CO2
-
-
-
-
?
double-stranded DNA-1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
-
major substrate, AlkB demethylates DNA-1-methyladenine and DNA-3-methylcytosine with comparable efficiencies and has only a modest preference for a single-stranded DNA substrate over its double-stranded DNA counterpart
-
-
?
double-stranded DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
major substrate, AlkB demethylates DNA-1-methyladenine and DNA-3-methylcytosine with comparable efficiencies and has only a modest preference for a single-stranded DNA substrate over its double-stranded DNA counterpart
-
-
?
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
-
-
?
N6-methyladenine + 2-oxoglutarate + O2
adenine + formaldehyde + succinate + CO2
-
via 6-hydroxymethyl adenine derivative
-
-
?
single-stranded DNA-1-methyladenine + 2-oxoglutarate + O2
DNA-adenine + formaldehyde + succinate + CO2
-
major substrate, AlkB demethylates DNA-1-methyladenine and DNA-3-methylcytosine with comparable efficiencies and has only a modest preference for a single-stranded DNA substrate over its double-stranded DNA counterpart
-
-
?
single-stranded DNA-3-methylcytosine + 2-oxoglutarate + O2
DNA-cytosine + formaldehyde + succinate + CO2
-
major substrate, AlkB demethylates DNA-1-methyladenine and DNA-3-methylcytosine with comparable efficiencies and has only a modest preference for a single-stranded DNA substrate over its double-stranded DNA counterpart
-
-
?
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-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-base-CH3 + 2-oxoglutarate + O2
DNA-base + formaldehyde + succinate + CO2
-
-
-
-
?
DNA-base-CH3 + 2-oxoglutarate + O2
DNA-base + formaldehyde + succinate + CO2
-
-
-
?
DNA-base-CH3 + 2-oxoglutarate + O2
DNA-base + formaldehyde + succinate + CO2
-
-
-
-
?
DNA-base-CH3 + 2-oxoglutarate + O2
DNA-base + formaldehyde + succinate + CO2
-
-
-
-
?
N1-methyladenine + 2-oxoglutarate + O2
adenine + formaldehyde + succinate + CO2
-
-
-
-
?
N1-methyladenine + 2-oxoglutarate + O2
adenine + formaldehyde + succinate + CO2
-
-
-
-
?
N3-methylcytosine + 2-oxoglutarate + O2
cytosine + formaldehyde + succinate + CO2
-
-
-
-
?
N3-methylcytosine + 2-oxoglutarate + O2
cytosine + formaldehyde + succinate + CO2
-
-
-
-
?
N3-methylcytosine + 2-oxoglutarate + O2
cytosine + formaldehyde + succinate + CO2
-
-
-
-
?
RNA-base-CH3 + 2-oxoglutarate + O2
RNA-base + formaldehyde + succinate + CO2
-
-
-
-
?
RNA-base-CH3 + 2-oxoglutarate + O2
RNA-base + formaldehyde + succinate + CO2
-
-
-
-
?
additional information
?
-
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
-
?
additional information
?
-
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
-
?
additional information
?
-
Agrobacterium tumefaciens C58 / ATCC 33970
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
-
?
additional information
?
-
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
-
?
additional information
?
-
-
exocyclic carbons adjacent to the N6 of adenine are targets for oxidation by the Escherichia coli adaptive response protein AlkB
-
-
?
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
?
-
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
-
?
additional information
?
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
-
?
additional information
?
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
-
?
additional information
?
-
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
-
?
additional information
?
-
-
the enzyme displays both DNA repair activity and wobble uridine modification of tRNA
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
Fe2+
-
required for activity
Fe2+
-
required for activity, AlkB is a member of the non-heme iron (II) 2-oxoglutarate-dependent dioxygenase superfamily
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
CpG promoter methylation of the ALKBH3 alkylation repair gene in breast cancer.
Carcinogenesis
Analysis of differentially expressed genes in human rectal carcinoma using suppression subtractive hybridization.
Carcinogenesis
Fluorescence Probes for ALKBH2 Allow the Measurement of DNA Alkylation Repair and Drug Resistance Responses.
Carcinogenesis
The oxidative demethylase ALKBH3 marks hyperactive gene promoters in human cancer cells.
Carcinoma
A novel human AlkB homologue, ALKBH8, contributes to human bladder cancer progression.
Carcinoma
ALKBH2, a novel AlkB homologue, contributes to human bladder cancer progression by regulating MUC1 expression.
Carcinoma
ALKBH3 Contributes to Survival and Angiogenesis of Human Urothelial Carcinoma Cells through NADPH Oxidase and Tweak/Fn14/VEGF Signals.
Carcinoma in Situ
A novel human AlkB homologue, ALKBH8, contributes to human bladder cancer progression.
Carcinoma in Situ
ALKBH2, a novel AlkB homologue, contributes to human bladder cancer progression by regulating MUC1 expression.
Carcinoma, Non-Small-Cell Lung
Down-regulation of ALKBH2 increases cisplatin sensitivity in H1299 lung cancer cells.
dna oxidative demethylase deficiency
Loss of epitranscriptomic control of selenocysteine utilization engages senescence and mitochondrial reprogramming?.
Glioblastoma
The DNA repair protein ALKBH2 mediates temozolomide resistance in human glioblastoma cells.
Hodgkin Disease
Epigenetic Loss of m1A RNA Demethylase ALKBH3 in Hodgkin Lymphoma Targets Collagen Conferring Poor Clinical Outcome.
Intellectual Disability
Recessive Truncating Mutations in ALKBH8 Cause Intellectual Disability and Severe Impairment of Wobble Uridine Modification.
Lung Neoplasms
ALKBH3, a human AlkB homologue, contributes to cell survival in human non-small-cell lung cancer.
Lung Neoplasms
Down-regulation of ALKBH2 increases cisplatin sensitivity in H1299 lung cancer cells.
Lung Neoplasms
TP53 gene status is a critical determinant of phenotypes induced by ALKBH3 knockdown in non-small cell lung cancers.
Neoplasm Metastasis
Indenone derivatives as inhibitor of human DNA dealkylation repair enzyme AlkBH3.
Neoplasms
A novel human AlkB homologue, ALKBH8, contributes to human bladder cancer progression.
Neoplasms
AlkB homolog 3-mediated tRNA demethylation promotes protein synthesis in cancer cells.
Neoplasms
ALKBH overexpression in head and neck cancer: potential target for novel anticancer therapy.
Neoplasms
ALKBH2, a novel AlkB homologue, contributes to human bladder cancer progression by regulating MUC1 expression.
Neoplasms
ALKBH3 Contributes to Survival and Angiogenesis of Human Urothelial Carcinoma Cells through NADPH Oxidase and Tweak/Fn14/VEGF Signals.
Neoplasms
ALKBH8 promotes bladder cancer growth and progression through regulating the expression of survivin.
Neoplasms
Anti-Tumor Effect of AlkB Homolog 3 Knockdown in Hormone- Independent Prostate Cancer Cells.
Neoplasms
Association of AlkB homolog 3 expression with tumor recurrence and unfavorable prognosis in hepatocellular carcinoma.
Neoplasms
DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA alkylation repair and cancer cell proliferation.
Neoplasms
Fluorescence Monitoring of the Oxidative Repair of DNA Alkylation Damage by ALKBH3, a Prostate Cancer Marker.
Neoplasms
Fluorescence Probes for ALKBH2 Allow the Measurement of DNA Alkylation Repair and Drug Resistance Responses.
Neoplasms
Human ALKBH3-induced m1A demethylation increases the CSF-1 mRNA stability in breast and ovarian cancer cells.
Neoplasms
Indenone derivatives as inhibitor of human DNA dealkylation repair enzyme AlkBH3.
Neoplasms
The interaction between ALKBH2 DNA repair enzyme and PCNA is direct, mediated by the hydrophobic pocket of PCNA and perturbed in naturally-occurring ALKBH2 variants.
Neoplasms
The oxidative demethylase ALKBH3 marks hyperactive gene promoters in human cancer cells.
Neoplasms
TP53 regulates human AlkB homologue 2 expression in glioma resistance to Photofrin-mediated photodynamic therapy.
Neoplasms
Transfer RNA demethylase ALKBH3 promotes cancer progression via induction of tRNA-derived small RNAs.
Prostatic Hyperplasia
Anti-Tumor Effect of AlkB Homolog 3 Knockdown in Hormone- Independent Prostate Cancer Cells.
Prostatic Neoplasms
ALKBH3, a human AlkB homologue, contributes to cell survival in human non-small-cell lung cancer.
Prostatic Neoplasms
Anti-Tumor Effect of AlkB Homolog 3 Knockdown in Hormone- Independent Prostate Cancer Cells.
Prostatic Neoplasms
Fluorescence Monitoring of the Oxidative Repair of DNA Alkylation Damage by ALKBH3, a Prostate Cancer Marker.
Prostatic Neoplasms
The oxidative demethylase ALKBH3 marks hyperactive gene promoters in human cancer cells.
Urinary Bladder Neoplasms
A novel human AlkB homologue, ALKBH8, contributes to human bladder cancer progression.
Urinary Bladder Neoplasms
ALKBH2, a novel AlkB homologue, contributes to human bladder cancer progression by regulating MUC1 expression.
Urinary Bladder Neoplasms
ALKBH3 Contributes to Survival and Angiogenesis of Human Urothelial Carcinoma Cells through NADPH Oxidase and Tweak/Fn14/VEGF Signals.
Urinary Bladder Neoplasms
ALKBH8 promotes bladder cancer growth and progression through regulating the expression of survivin.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.002
1-methyl-dAMP
-
apparent value, at 37°C, pH not specified in the publication
0.0055
1-methyl-dATP
-
apparent value, at 37°C, pH not specified in the publication
0.012
2'-deoxy-1-methyl-adenosine 3'-phosphate
-
apparent value, at 37°C, pH not specified in the publication
0.0028
d(Tpm1ApT)
-
apparent value, at 37°C, pH not specified in the publication
0.002
DNA-N1-methyladenine
wild type enzyme, pH and temperature not specified in the publication
-
0.0062
double-stranded DNA-1-methyladenine
-
at 25°C, pH not specified in the publication
-
0.0093
double-stranded DNA-3-methylcytosine
-
at 25°C, pH not specified in the publication
-
0.01
N1-methyl-ATP
-
apparent value, at 37°C, pH not specified in the publication
0.0014
poly(dm1A)
-
apparent value, at 37°C, pH not specified in the publication
-
0.0054
single-stranded DNA-1-methyladenine
-
at 25°C, pH not specified in the publication
-
0.0034
single-stranded DNA-3-methylcytosine
-
at 25°C, pH not specified in the publication
-
0.0044
d(Tpm1A)
-
apparent value, at 37°C, pH not specified in the publication
0.04 - 0.05
d(Tpm1A)
-
apparent value, at 37°C, pH not specified in the publication
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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
0.012
2'-deoxy-1-methyl-adenosine 3'-phosphate
-
at 37°C, pH not specified in the publication
0.1235
DNA-N1-methyladenine
wild type enzyme, pH and temperature not specified in the publication
-
0.052
double-stranded DNA-1-methyladenine
-
at 25°C, pH not specified in the publication
-
0.055
double-stranded DNA-3-methylcytosine
-
at 25°C, pH not specified in the publication
-
0.062
single-stranded DNA-1-methyladenine
-
at 25°C, pH not specified in the publication
-
0.037
single-stranded DNA-3-methylcytosine
-
at 25°C, pH not specified in the publication
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.3
2'-deoxy-1-methyl-adenosine 3'-phosphate
-
at 37°C, pH not specified in the publication
61.8
DNA-N1-methyladenine
wild type enzyme, pH and temperature not specified in the publication
-
8
double-stranded DNA-1-methyladenine
-
at 25°C, pH not specified in the publication
-
5.8
double-stranded DNA-3-methylcytosine
-
at 25°C, pH not specified in the publication
-
11.3
single-stranded DNA-1-methyladenine
-
at 25°C, pH not specified in the publication
-
10.8
single-stranded DNA-3-methylcytosine
-
at 25°C, pH not specified in the publication
-
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
-
repair of DNA-3-methylthymine by AlkB is optimal at pH 6.0, but inefficient
6.5
-
repair of DNA-3-methylthymine by ABH3 is optimal at pH 6.5, but inefficient
7.6 - 8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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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
-
brenda
-
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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
malfunction
-
Escherichia coli alkB mutants are defective in processing methylation damage generated in single-stranded DNA
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
malfunction
-
an AlkB-deficient strain accumulates N1-methyladenine at a high rate
malfunction
-
an AlkB-deficient strain accumulates N1-methyladenine at a high rate
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
-
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
-
AlkB 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 AlkB prior to translation. Chemical methylation of tRNA-Phe inhibits aminoacylation and translation, but the inhibition can be reversed by AlkB
physiological function
-
AlkB-mediated oxidative demethylation reverses DNA damage
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
-
oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage
physiological function
-
the alkB gene product protects against cell killing by SN2-alkylating agents, probably through DNA repair
physiological function
-
the AlkB protein catalyzes the direct reversal of alkylation damage to DNA, primarily 1-methyladenine and 3-methylcytosine lesions created by endogenous or environmental alkylating agents
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
-
viral AlkB proteins maintain the integrity of the viral RNA genome through repair of deleterious methylation damage
physiological function
-
viral AlkB proteins maintain the integrity of the viral RNA genome through repair of deleterious methylation damage
physiological function
-
viral AlkB proteins maintain the integrity of the viral RNA genome through repair of deleterious methylation damage
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
physiological function
-
protein AlkB repairs cytotoxic 1-methyladenine and 3-methylcytosine lesions induced by methyl methanesulfonate in DNA and RNA in vitro and in pre-damaged DNA and RNA bacteriophages in vivo, quantification of AlkB-mediated repair of endogenous RNA and DNA in vivo, overview
physiological function
-
the DNA and RNA repair protein AlkB removes alkyl groups from nucleic acids by a unique iron- and 2-oxoglutarate-dependent oxidation strategy, role for AlkB in regulation of important cellular functions in vivo. Complete adduct restructuring of ethano-adenine, a DNA adduct formed by an important anticancer drug, BCNU, by AlkB to a form that does not hinder replication. Ethano-adenine dealkylation process requires two oxidation reactions, one at N1 and a second at N6, to achieve complete restoration of the undamaged adenine base. AlkB DNA substrate N6-methyladenine is an important epigenetic signal for DNA replication and many other cellular processes
physiological function
Escherichia coli W3110 / ATCC 27325
-
AlkB-mediated oxidative demethylation reverses DNA damage
physiological function
-
protein AlkB repairs cytotoxic 1-methyladenine and 3-methylcytosine lesions induced by methyl methanesulfonate in DNA and RNA in vitro and in pre-damaged DNA and RNA bacteriophages in vivo, quantification of AlkB-mediated repair of endogenous RNA and DNA in vivo, overview
additional information
-
ABH2 associates with DNA repair proteins Ku70/Ku80, overview
additional information
-
the recombinant AlkB expressed is less active than the natural endogenous form
additional information
-
the recombinant AlkB expressed is less active than the natural endogenous form
Show AA Sequence and Transmembrane Helices (1173 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12)
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AlkB in complex with double-stranded DNA containing 1,N6-ethenoadenine, 3-methylthymine, and 3-methylcytosine, using 100 mM NaCl, 25 mM MgCl2, 100 mM cacodylate (pH 6.5) and 20-24% (w/v) PEG 8K or 4K
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D61A
-
the mutant is unable to rescue methylated RNA phage MS2 and is unable to convert 2-oxoglutarate to succinate
H59A
-
the mutant is unable to rescue methylated RNA phage MS2 and is unable to convert 2-oxoglutarate to succinate
D133C
-
the mutant contains no iron and shows indistinguishable chromatographic behavior from that of wild type enzyme
D135A
the mutant displays about 5-15% of wild type activity towards 1-methyladenine at pH 7.0
D135I
the mutant shows increased activity with RNA-N6-methyladenine and reduced activity with DNA-N1-methyladenine compared to the wild type enzyme
D135N
D135S
the mutant displays about 5-15% of wild type activity towards 1-methyladenine at pH 7.0
E136L
the mutant shows increased activity with RNA-N6-methyladenine and reduced activity with DNA-N1-methyladenine compared to the wild type enzyme
H131C
-
the mutant contains no iron and shows indistinguishable chromatographic behavior from that of wild type enzyme
H187C
-
the mutant contains no iron and shows indistinguishable chromatographic behavior from that of wild type enzyme
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
D135N
the mutant displays about 5-15% of wild type activity towards 1-methyladenine at pH 7.0
D135N
the mutant shows increased activity with RNA-N6-methyladenine and reduced activity with DNA-N1-methyladenine compared to the wild type enzyme
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
the iron(II)-bound AlkB is reasonably stable at 4°C in the presence of 10 mM 2-mercaptoethanol at concentrations up to 2 mM
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose column chromatography, S-Sepharose column chromatography, Ni-NTA column chromatography, and Mono-S cation exchange column chromatography
DEAE-cellulose column chromatography, SP Sepharose cation exchange column chromatography, and Mono-S cation exchange column chromatography
-
His-tagged AlkB is purified by Ni-NTA agarose column chromatography, untagged Alkb is purified by DEAE-cellulose column chromatography, Sepharose column chromatography, and Mono S column chromatography
His-tagged enzyme is purified by Ni-NTA agarose column chromatography
Ni-NTA agarose column chromatography
Ni-NTA column chromatography
Ni-NTA column chromatography and SP-Sepharose cation exchange affinity column chromatography
-
Ni-NTA column chromatography and UnoS column chromatography
TALON metal affinity resin column chromatography
Talon metal affinity resincolumn chromatography
DEAE-cellulose column chromatography, S-Sepharose column chromatography, Ni-NTA column chromatography, and Mono-S cation exchange column chromatography
-
DEAE-cellulose column chromatography, S-Sepharose column chromatography, Ni-NTA column chromatography, and Mono-S cation exchange column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AlkB overexpression in Escherichia coli AlkB-deficient strains HK82 and BW25113. AlkB mutant strain HK82 is transformed with the low-copy-number expression plasmid pJB658 containing the alkB gene following a toluic acid-inducible promoter. The recombinant AlkB expressed is less active than the natural endogenous form
-
expressed in Escherichia BL21-CodonPlus(DE3)-RIPL cells
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
-
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL cells
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
-
expressed in Escherichia coli BL21(DE3) cells
-
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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
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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
brenda
Mishina, Y.; Chen, L.X.; He, C.
Preparation and characterization of the native iron(II)-containing DNA repair AlkB protein directly from Escherichia coli
J. Am. Chem. Soc.
126
16930-16936
2004
Escherichia coli
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
Trewick, S.C.; Henshaw, T.F.; Hausinger, R.P.; Lindahl, T.; Sedgwick, B.
Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage
Nature
419
174-178
2002
Escherichia coli
brenda
Falnes, P.O.; Johansen, R.F.; Seeberg, E.
AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli
Nature
419
178-182
2002
Escherichia coli, Escherichia coli W3110 / ATCC 27325
brenda
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)
brenda
Yi, C.; Jia, G.; Hou, G.; Dai, Q.; Zhang, W.; Zheng, G.; Jian, X.; Yang, C.G.; Cui, Q.; He, C.
Iron-catalysed oxidation intermediates captured in a DNA repair dioxygenase
Nature
468
330-333
2010
Escherichia coli (P05050)
brenda
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
brenda
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
brenda
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
brenda
Roy, T.W.; Bhagwat, A.S.
Kinetic studies of Escherichia coli AlkB using a new fluorescence-based assay for DNA demethylation
Nucleic Acids Res.
35
e147
2007
Escherichia coli
brenda
van den Born, E.; Omelchenko, M.V.; Bekkelund, A.; Leihne, V.; Koonin, E.V.; Dolja, V.V.; Falnes, P.?.
Viral AlkB proteins repair RNA damage by oxidative demethylation
Nucleic Acids Res.
36
5451-5461
2008
Escherichia coli, blueberry scorch virus, Blackberry virus Y, grapevine virus A
brenda
Begley, T.J.; Samson, L.D.
AlkB mystery solved: oxidative demethylation of N1-methyladenine and N3-methylcytosine adducts by a direct reversal mechanism
Trends Biochem. Sci.
28
2-5
2003
Escherichia coli
brenda
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
brenda
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
brenda
Vagbo, C.B.; Svaasand, E.K.; Aas, P.A.; Krokan, H.E.
Methylation damage to RNA induced in vivo in Escherichia coli is repaired by endogenous AlkB as part of the adaptive response
DNA Repair
12
188-195
2013
Escherichia coli, Escherichia coli AB1157
brenda
Li, D.; Delaney, J.C.; Page, C.M.; Yang, X.; Chen, A.S.; Wong, C.; Drennan, C.L.; Essigmann, J.M.
Exocyclic carbons adjacent to the N6 of adenine are targets for oxidation by the Escherichia coli adaptive response protein AlkB
J. Am. Chem. Soc.
134
8896-8901
2012
Escherichia coli
brenda
Chen, F.; Tang, Q.; Bian, K.; Humulock, Z.; Yang, X.; Jost, M.; Drennan, C.; Essigmann, J.; Li, D.
Adaptive response enzyme AlkB preferentially repairs 1-methylguanine and 3-methylthymine adducts in double-stranded DNA
Chem. Res. Toxicol.
29
687-693
2016
Escherichia coli
brenda
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
brenda
Zhu, C.; Yi, C.
Switching demethylation activities between AlkB family RNA/DNA demethylases through exchange of active-site residues
Angew. Chem. Int. Ed. Engl.
53
3659-3662
2014
Escherichia coli (P05050)
brenda
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
brenda
Wang, B.; Usharani, D.; Li, C.; Shaik, S.
Theory uncovers an unusual mechanism of DNA repair of a lesioned adenine by AlkB enzymes
J. Am. Chem. Soc.
136
13895-13901
2014
Escherichia coli (P05050)
brenda
Ergel, B.; Gill, M.L.; Brown, L.; Yu, B.; Palmer, A.G.; Hunt, J.F.
Protein dynamics control the progression and efficiency of the catalytic reaction cycle of the Escherichia coli DNA-repair enzyme AlkB
J. Biol. Chem.
289
29584-29601
2014
Escherichia coli
brenda
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
brenda
Zdzalik, D.; Vagbo, C.B.; Kirpekar, F.; Davydova, E.; Puscian, A.; Maciejewska, A.M.; Krokan, H.E.; Klungland, A.; Tudek, B.; van den Born, E.; Falnes, P.O.
Protozoan ALKBH8 oxygenases display both DNA repair and tRNA modification activities
PLoS ONE
9
e98729
2014
Agrobacterium tumefaciens, Cryptosporidium parvum, Tetrahymena thermophila, Acanthamoeba polyphaga Mimivirus, Rickettsia felis, Roseobacter denitrificans (Q16D46), Roseobacter denitrificans OCh (Q16D46), Agrobacterium tumefaciens C58 / ATCC 33970, Tetrahymena thermophila SB210
brenda
Tishinov, K.; Gillingham, D.
Synthesis of new alkylated mononucleotide analogues and their repair proficiency by the prokaryotic DNA repair protein AlkB
Synlett
26
2720-2723
2015
Escherichia coli (P05050)
-
brenda
Soll, J.M.; Sobol, R.W.; Mosammaparast, N.
Regulation of DNA alkylation damage repair lessons and therapeutic opportunities
Trends Biochem. Sci.
42
206-218
2017
Homo sapiens (Q6NS38)
brenda
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