Information on EC 1.14.11.33 - DNA oxidative demethylase and Organism(s) Escherichia coli and UniProt Accession P05050

-

716332, 743860

-

?

DNA-1,N6-ethenoadenine + 2-oxoglutarate + O2

DNA-adenine + formaldehyde + succinate + CO2

-

742741

-

?

DNA-1-(2-hydroxypropyl)-adenine + 2-oxoglutarate + O2

?

-

-

?

DNA-1-ethanoadenine + 2-oxoglutarate + O2

?

-

-

?

DNA-1-ethenoadenine + 2-oxoglutarate + O2

?

-

-

?

DNA-1-ethyladenine + 2-oxoglutarate + O2

DNA-adenine + acetaldehyde + succinate + CO2

-

-

ir

DNA-1-hydroxyethyladenine + 2-oxoglutarate + O2

?

-

-

?

DNA-1-methyladenine + 2-oxoglutarate + O2

DNA-adenine + formaldehyde + succinate + CO2

DNA-1-methylguanine + 2-oxoglutarate + O2

DNA-guanine + formaldehyde + succinate + CO2

weak substrate

-

ir

DNA-2-furfurylguanosine + 2-oxoglutarate + O2

?

-

-

?

DNA-2-methylguanosine + 2-oxoglutarate + O2

DNA-guanosine + formaldehyde + succinate + CO2

-

-

?

DNA-3,N4-ethenocytosine + 2-oxoglutarate + O2

?

-

-

?

DNA-3-methylcytosine + 2-oxoglutarate + O2

?

-

-

?

DNA-3-methylcytosine + 2-oxoglutarate + O2

DNA-cytosine + formaldehyde + succinate + CO2

3 entries

DNA-3-methylthymine + 2-oxoglutarate + O2

DNA-thymine + formaldehyde + succinate + CO2

DNA-4-methylcytosine + 2-oxoglutarate + O2

?

-

-

?

DNA-base-CH3 + 2-oxoglutarate + O2

DNA-base + formaldehyde + succinate + CO2

-

-

?

DNA-N1-methyladenine + 2-oxoglutarate + O2

DNA-adenine + formaldehyde + succinate + CO2

highest activity

-

?

DNA-tetrahydro-2-furfurylguanosine + 2-oxoglutarate + O2

?

-

-

?

methylated poly(deoxyadenine) + 2-oxoglutarate + O2

poly(deoxyadenine) + formaldehyde + succinate + CO2

-

-

ir

methylated poly(deoxycytosine) + 2-oxoglutarate + O2

poly(deoxycytosine) + formaldehyde + succinate + CO2

-

-

ir

1-methyl-dAMP + 2-oxoglutarate + O2

dAMP + formaldehyde + succinate + CO2

-

-

?

1-methyl-dATP + 2-oxoglutarate + O2

dATP + formaldehyde + succinate + CO2

-

-

?

2'-deoxy-1-methyl-adenosine 3'-phosphate + 2-oxoglutarate + O2

2'-deoxyadenosine 3'-phosphate + formaldehyde + succinate + CO2

-

-

?

d(Tpm1A) + 2-oxoglutarate + O2

d(TpA) + formaldehyde + succinate + CO2

-

-

?

d(Tpm1ApT) + 2-oxoglutarate + O2

d(TpApT) + formaldehyde + succinate + CO2

-

-

?

DNA-1,6-ethenoadenine + O2

DNA-adenine + glyoxal

-

713602

-

?

DNA-1,N6-ethenoadenine + 2-oxoglutarate + O2

?

-

-

?

DNA-1-methyladenine + 2-oxoglutarate + O2

DNA-adenine + formaldehyde + succinate + CO2

4 entries

DNA-1-methylguanine + 2-oxoglutarate + O2

DNA-guanine + formaldehyde + succinate + CO2

DNA-3,N4-ethenocytosine + 2-oxoglutarate + O2

?

-

-

?

DNA-3-methylcytosine + 2-oxoglutarate + O2

DNA-cytosine + formaldehyde + succinate + CO2

4 entries

DNA-3-methylthymine + 2-oxoglutarate + O2

DNA-thymine + formaldehyde + succinate + CO2

3 entries

DNA-base-CH3 + 2-oxoglutarate + O2

DNA-base + formaldehyde + succinate + CO2

-

715241, 724819

-

?

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 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

716220

-

?

methylated poly(deoxyadenine) + 2-oxoglutarate + O2

poly(deoxyadenine) + formaldehyde + succinate + CO2

methylated poly(deoxycytosine) + 2-oxoglutarate + O2

poly(deoxycytosine) + formaldehyde + succinate + CO2

-

716323

-

?

methylated poly(deoxythymine) + 2-oxoglutarate + O2

poly(deoxythymine) + 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

-

716220

-

?

N1-methyl-ATP + 2-oxoglutarate + O2

ATP + formaldehyde + succinate + CO2

-

-

?

N1-methyladenine + 2-oxoglutarate + O2

adenine + formaldehyde + succinate + CO2

-

724819, 725207

-

?

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 + 2-oxoglutarate + O2

cytosine + formaldehyde + succinate + CO2

-

-

?

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

-

?

poly(dm1A) + 2-oxoglutarate + O2

poly(dA) + formaldehyde + succinate + CO2

-

-

?

RNA-1-methyladenine + 2-oxoglutarate + O2

RNA-adenine + formaldehyde + succinate + CO2

-

716363, 716364, 716368

-

?

RNA-3-methylcytosine + 2-oxoglutarate + O2

RNA-cytosine + formaldehyde + succinate + CO2

-

716363, 716364, 716368

-

?

RNA-base-CH3 + 2-oxoglutarate + O2

RNA-base + formaldehyde + succinate + CO2

-

-

?

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

-

?

tRNA-1-methylguanine + 2-oxoglutarate + O2

tRNA-guanine + formaldehyde + succinate + CO2

-

716364

-

?

additional information

?

-

12 entries

DNA-1,N6-ethenoadenine + 2-oxoglutarate + O2

?

-

-

?

DNA-1,N6-ethenoadenine + 2-oxoglutarate + O2

DNA-adenine + formaldehyde + succinate + CO2

-

742741

-

?

DNA-1-(2-hydroxypropyl)-adenine + 2-oxoglutarate + O2

?

-

-

?

DNA-1-ethanoadenine + 2-oxoglutarate + O2

?

-

-

?

DNA-1-ethenoadenine + 2-oxoglutarate + O2

?

-

-

?

DNA-1-hydroxyethyladenine + 2-oxoglutarate + O2

?

-

-

?

DNA-1-methyladenine + 2-oxoglutarate + O2

DNA-adenine + formaldehyde + succinate + CO2

-

-

?

DNA-2-furfurylguanosine + 2-oxoglutarate + O2

?

-

-

?

DNA-2-methylguanosine + 2-oxoglutarate + O2

DNA-guanosine + formaldehyde + succinate + CO2

-

-

?

DNA-3,N4-ethenocytosine + 2-oxoglutarate + O2

?

-

-

?

DNA-3-methylcytosine + 2-oxoglutarate + O2

?

-

-

?

DNA-3-methylcytosine + 2-oxoglutarate + O2

DNA-cytosine + formaldehyde + succinate + CO2

-

-

?

DNA-4-methylcytosine + 2-oxoglutarate + O2

?

-

-

?

DNA-base-CH3 + 2-oxoglutarate + O2

DNA-base + formaldehyde + succinate + CO2

-

-

?

DNA-tetrahydro-2-furfurylguanosine + 2-oxoglutarate + O2

?

-

-

?

DNA-1,N6-ethenoadenine + 2-oxoglutarate + O2

?

-

-

?

DNA-1-methylguanine + 2-oxoglutarate + O2

DNA-guanine + formaldehyde + succinate + CO2

-

-

?

DNA-3,N4-ethenocytosine + 2-oxoglutarate + O2

?

-

-

?

DNA-3-methylthymine + 2-oxoglutarate + O2

DNA-thymine + formaldehyde + succinate + CO2

-

-

?

DNA-base-CH3 + 2-oxoglutarate + O2

DNA-base + formaldehyde + succinate + CO2

-

715241, 724819

-

?

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

-

?

N1-methyladenine + 2-oxoglutarate + O2

adenine + formaldehyde + succinate + CO2

-

724819, 725207

-

?

N3-methylcytosine + 2-oxoglutarate + O2

cytosine + formaldehyde + succinate + CO2

-

-

?

N6-methyladenine + 2-oxoglutarate + O2

adenine + formaldehyde + succinate + CO2

-

via 6-hydroxymethyl adenine derivative

-

?

RNA-base-CH3 + 2-oxoglutarate + O2

RNA-base + formaldehyde + succinate + CO2

-

-

?

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

-

?

additional information

?

-

-

exocyclic carbons adjacent to the N6 of adenine are targets for oxidation by the Escherichia coli adaptive response protein AlkB

-

?

2-oxoglutarate

-

2-oxoglutarate

-

713602, 715241, 715464, 715470, 716220, 716323, 716324, 716325, 716362, 716363, 716364, 716367, 716368, 716972

Fe2+

Fe2+

EDTA

-

ascorbate

2 m ascorbate is used in assay conditions

0.002

DNA-N1-methyladenine

wild type enzyme, pH and 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

0.0044 - 0.05

d(Tpm1A)

0.0028

d(Tpm1ApT)

-

apparent value, at 37°C, pH 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

-

0.1235

DNA-N1-methyladenine

wild type enzyme, pH and temperature not specified in the publication

-

0.07

1-methyl-dAMP

-

at 37°C, pH not specified in the publication

0.033

1-methyl-dATP

-

at 37°C, pH not specified in the publication

0.012

2'-deoxy-1-methyl-adenosine 3'-phosphate

-

at 37°C, pH not specified in the publication

0.06

d(Tpm1A)

-

at 37°C, pH not specified in the publication

0.12

d(Tpm1ApT)

-

at 37°C, pH 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

-

0.02

N1-methyl-ATP

-

at 37°C, pH not specified in the publication

0.2

poly(dm1A)

-

at 37°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

-

61.8

DNA-N1-methyladenine

wild type enzyme, pH and temperature not specified in the publication

-

1.7

1-methyl-ATP

-

at 37°C, pH not specified in the publication

35

1-methyl-dAMP

-

at 37°C, pH not specified in the publication

11.7

1-methyl-dATP

-

at 37°C, pH not specified in the publication

3.3

2'-deoxy-1-methyl-adenosine 3'-phosphate

-

at 37°C, pH not specified in the publication

43

d(Tpm1ApT)

-

at 37°C, pH 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

-

143

poly(dm1A)

-

at 37°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

-

6

-

repair of DNA-3-methylthymine by AlkB is optimal at pH 6.0, but inefficient

7

-

assay at

7.6 - 8

-

DNA-3-methylcytosine is repaired optimally at pH 7.5-8.0

8

-

assay at

37

-

assay at

724819, 725207

-

716107, 716332, 741601, 742741, 743860

UniProt

malfunction

physiological function

8 entries

additional information

-

the recombinant AlkB expressed is less active than the natural endogenous form

5 entries

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

D135A

the mutant displays about 5-15% of wild type activity towards 1-methyladenine at pH 7.0

716332

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

716332

E136L

the mutant shows increased activity with RNA-N6-methyladenine and reduced activity with DNA-N1-methyladenine compared to the wild type enzyme

D133C

-

the mutant contains no iron and shows indistinguishable chromatographic behavior from that of 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

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

-

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

Ni-NTA column chromatography and Mono-Q column chromatography

-

-

DEAE-cellulose column chromatography, S-Sepharose column chromatography, Ni-NTA column chromatography, and Mono-S cation exchange column chromatography

-

716362

DEAE-cellulose column chromatography, SP Sepharose cation exchange column chromatography, and Mono-S cation exchange column chromatography

-

GSTrap 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

-

716325

expressed in Escherichia coli BL21(DE3) cells

716107, 716332

AlkB is expressed in Escherichia coli BL21(DE3) cells

-

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 coli B834lambda (DE3) cells

-

742862

expressed in Escherichia coli BL21 Star(DE3)pLysS cells

-

expressed in Escherichia coli BL21(DE3) cells

-

715241, 716220, 716325, 716362, 716367

713602

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

19852088

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

15612731

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

12944387

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

15269201

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)

16793366

716220

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

15469826

716323

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

12226667

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

12226668

716325

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)

12594517

716332

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)

21068844

716362

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

15004242

716363

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

15229293

716364

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

15576352

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

18003660

716368

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

Blackberry virus Y, blueberry scorch virus, Escherichia coli, grapevine virus A

18718927

716972

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

12517444

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

23276627

Li, D.; Delaney, J.C.; Page, C.M.; Yang, X.; Chen, A.S.; Wong, C.; Drennan, C.L.; Essigmann, J.M.

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