3.2.2.27: uracil-DNA glycosylase
This is an abbreviated version!
For detailed information about uracil-DNA glycosylase, go to the full flat file.
Word Map on EC 3.2.2.27
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3.2.2.27
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deamination
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cytosine
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glycosylases
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endonuclease
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thymine
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abasic
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misincorporation
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ung2
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uracil-containing
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duplex
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hypermutation
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dump
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deoxyuridine
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activation-induced
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excises
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mispairs
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base-excision
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dutpase
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8-oxoguanine
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apyrimidinic
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5-methylcytosine
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5-hydroxymethyluracil
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g-quadruplexes
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transversions
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ape1
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thymine-dna
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formamidopyrimidine
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5-hydroxyuracil
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short-patch
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xrcc1
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apurinic
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class-switching
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3,n4-ethenocytosine
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translesion
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post-replicative
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ap-endonuclease
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aid-induced
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apobec3g
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drug development
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molecular biology
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analysis
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medicine
- 3.2.2.27
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deamination
- cytosine
- glycosylases
- endonuclease
- thymine
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abasic
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misincorporation
- ung2
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uracil-containing
- duplex
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hypermutation
- dump
- deoxyuridine
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activation-induced
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excises
- mispairs
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base-excision
- dutpase
- 8-oxoguanine
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apyrimidinic
- 5-methylcytosine
- 5-hydroxymethyluracil
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g-quadruplexes
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transversions
- ape1
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thymine-dna
- formamidopyrimidine
- 5-hydroxyuracil
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short-patch
- xrcc1
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apurinic
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class-switching
- 3,n4-ethenocytosine
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translesion
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post-replicative
- ap-endonuclease
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aid-induced
- apobec3g
- drug development
- molecular biology
- analysis
- medicine
Reaction
Hydrolyses single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil =
Synonyms
5-formyluracil-DNA glycosylase, AFUDG, Afung protein, Blr0248, DNA N-glycosylase, dr0689, DR_0968, endonuclease VIII, family 1 uracil N-glycosylase, family 4 UDGa, family 4 uracil-DNA glycosylase, HMUDG, mismatch-specific uracil-DNA glycosylase, MjUDG, More, MtuNei1, MUG, Pa-UDG, PF1385, PfuUDG, single-strand selective monofunctional uracil-DNA glycosylase, single-strand selective uracil DNA glycosylase, single-strand-selective mono-functional uracil-DNA glycosylase, single-strand-selective monofunctional uracil DNA glycosylase, single-strand-selective monofunctional uracil-DNA glycosylase, single-stranded monofunctional uracil DNA N-glycosylase, SMUG1, SMUG1-like glycosylase, STK_22380, Ta0477, TD12-encoded protein, Thd1p, Thp1p, TMUDG, type 1 UDG, UDG, UDG1, UDGa, UdgB, UDGIV, UDGV, UL114, UL2, UNG, UNG-1, Ung-type uracil glycosylase, UNG1, UNG2, Unga, uracil DNA glycosylase, uracil DNA glycosylase 2, uracil DNA-glycosylase, uracil DNA-glycosylase 2, uracil-DNA glycosylase, uracil-DNA glycosylase 2, uracil-DNA glycosylase a, uracil-DNA N-glycosylase, uracil-N-glycosylase 2
ECTree
3.2.2.27 uracil-DNA glycosylaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.2.2.27 - uracil-DNA glycosylase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C101A
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absence of a fully coordinated [4Fe-4S]2+ cluster, loses considerable activity after incubation in assay buffer for two min, with about 20% of the original level of activity remaining
C85A
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absence of a fully coordinated [4Fe-4S]2+ cluster, loses considerable activity after incubation in assay buffer for two min, with about 20% of the original level of activity remaining
K100A
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absence of a fully coordinated [4Fe-4S]2+ cluster, 3fold and 2fold increase in catalytic efficiency (kcat/Km) for the mutant over wild-type enzyme for double-stranded and single-stranded substrates, respectively
A59Y
A205S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D77N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H200Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
A205S
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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D77N
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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H200Q
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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D64N
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site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
H187Q
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site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
N123A
the mutation substantially dramatically reduces enzyme activity on A/U base pairs and other double-stranded uracil-containing base pairs
N123D/L191A
the mutation generates an enzyme that excises cytosine and distinguishes between cytosine and methylcytosine
Y66H
the mutant shows 170fold reduced uracil excision activity compared to the wild-type enzyme, but like the wild-type protein, it is susceptible to inhibition by uracil and AP-DNA
Y66W
the mutant shows 7fold reduced uracil excision activity compared to the wild-type enzyme, and lacks TDG activity. The Y66W protein is moderately compromised and attenuated in binding to AP-DNA. The Y66W mutant maintains strict specificity for uracil excision from DNA, but it is recalcitrant to inhibition by uracil and AP-DNA
D64N
Escherichia coli B / ATCC 11303
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site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
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H187Q
Escherichia coli B / ATCC 11303
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site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
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G183D
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the mutation causes a reduction in the enzyme activity but no increase in stability
G183D/R302K
A214R
site-directed mutagenesis, the mutant shows altered substrate specificity for cleavage of uracil-DNA base pairs in comparison to the wild-type enzyme, overview
G60Y
site-directed mutagenesis, the mutation completely abolishes XDG and UDG activity, which is consistent with a modeled structure in which G60Y blocks the entry of either xanthine or uracil to the base binding pocket
G63P
site-directed mutagenesis, the proline substitution at the G63 position switches the SMUG1 enzyme to an exclusive UDG with equal activity for all uracil-DNA base pairs
H210G
site-directed mutagenesis, the mutant shows altered substrate specificity for cleavage of uracil-DNA base pairs in comparison to the wild-type enzyme, overview
H210M
site-directed mutagenesis, the mutant shows altered substrate specificity for cleavage of uracil-DNA base pairs in comparison to the wild-type enzyme, overview
H210N
site-directed mutagenesis, the mutant shows altered substrate specificity for cleavage of uracil-DNA base pairs in comparison to the wild-type enzyme, overview
M57L
site-directed mutagenesis, the mutation increases the flexibility of the motif 2 loop region and specifically A214, the mutant shows reduced catalytic activity and altered substrate specificity for cleavage of uracil-DNA base pairs in comparison to the wild-type enzyme, overview
G63P
Geobacter metallireducens GS-15 / ATCC 53774 / DSM 7210
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site-directed mutagenesis, the proline substitution at the G63 position switches the SMUG1 enzyme to an exclusive UDG with equal activity for all uracil-DNA base pairs
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H210G
Geobacter metallireducens GS-15 / ATCC 53774 / DSM 7210
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site-directed mutagenesis, the mutant shows altered substrate specificity for cleavage of uracil-DNA base pairs in comparison to the wild-type enzyme, overview
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H210M
Geobacter metallireducens GS-15 / ATCC 53774 / DSM 7210
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site-directed mutagenesis, the mutant shows altered substrate specificity for cleavage of uracil-DNA base pairs in comparison to the wild-type enzyme, overview
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H210N
Geobacter metallireducens GS-15 / ATCC 53774 / DSM 7210
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site-directed mutagenesis, the mutant shows altered substrate specificity for cleavage of uracil-DNA base pairs in comparison to the wild-type enzyme, overview
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M57L
Geobacter metallireducens GS-15 / ATCC 53774 / DSM 7210
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site-directed mutagenesis, the mutation increases the flexibility of the motif 2 loop region and specifically A214, the mutant shows reduced catalytic activity and altered substrate specificity for cleavage of uracil-DNA base pairs in comparison to the wild-type enzyme, overview
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D183G
D183G/K302R
F98H
site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme
F98L
site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme
G87A
site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme
H239L
site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme
H239N
site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme
N163D
site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme
N85A
site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme
Q152L/D154E
a siRNA-insensitive, inactive UNG2 mutant, overexpression in UNG2-depleted MAGI-CCR5 producer cells fails to restore viral infectivity
R276X
mutations at Arg276 transform uracil-DNA glycosylase into a single-stranded DNA-specific uracil-DNA glycosylase. The kcat of the R276 mutants is comparable to wild-type UNG on single-stranded DNA and differentially affected by NaCl, however, kcat on double-stranded DNA substrate is reduced 4-12-fold and decreases sharply at NaCl concentrations as low as 20 mM, the mutant proteins exhibit a 2.6 to 7.7fold reduction in affinity for a doubled-stranded oligonucleotide containing a pseudouracil residue opposite 2-aminopurine compared to the wild-type UNG
W231A/F234G
site-directed mutagenesis, the mutation impairs the association of UNG2 with viral protein Vpr UNG2-depleted MAGI-CCR5 producer cells and viral infectivity
D88N
S67M/S68N
the mutant shows reduced activity compared to the wild type enzyme
S68N
the mutant shows reduced activity compared to the wild type enzyme
D150E
D150W
E132K
Y152E
Y152N
D150E
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displays reduced activity of about 70% of the wild type value
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E132K
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mutation converts the enzyme into a bifunctional glycosylase/AP lyase capable of both removing uracil at a glycosylic bond and cleaving the phosphodiester backbone at an apurinic/apyrimidinic site. The mutant catalyzes a beta-elimination reaction at the apurinic/apyrimidinic site via uracil excision and forms a Schiff base intermediate in the form of a protein-DNA complex
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Y152E
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retains unchanged levels of uracil-DNA glycosylase activity
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Y152N
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retains unchanged levels of uracil-DNA glycosylase activity
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D145N
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the mutant shows increased class switch recombination efficiency and reduced uracil removal activity compared to the wild type enzyme
DELTA90/W231A
H239L
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a SMUG1 mutant, the mutation affects the stabilization of transition state
H268L
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the mutant shows increased class switch recombination efficiency and reduced deoxyuracil removal activity compared to the wild type enzyme
C17S
the mutant enzyme has a brown color similar to that of the wild type protein
C17S/C20S
colorless mutant enzyme, loss of the Fe-S cluster, decrease in activity
C20S
the mutant enzyme has a brown color similar to that of the wild type protein
D75A
the D75A mutant shows low enzymatic activity for the removal of uracil from U-G or thymine from T-G. However, the mutant can distinguish between the C5-hydrogen and the C5-methyl group
E41A/G42D
the mutant shows severely reduced activity compared to the wild type enzyme
E41Q
the mutant shows 888fold reduced activity compared to the wild type enzyme
E41Q/G42D
the mutant shows 5.3fold reduced activity compared to the wild type enzyme
E47A
the mutant shows severely reduced activity compared to the wild type enzyme
F54A
the mutant shows severely reduced activity compared to the wild type enzyme
G42D
the mutant shows 89fold reduced activity compared to the wild type enzyme
H155S
the mutant shows reduced activity compared to the wild type enzyme
N80A
the mutant shows severely reduced activity compared to the wild type enzyme
N89A
the mutant shows reduced activity compared to the wild type enzyme
D75A
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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the D75A mutant shows low enzymatic activity for the removal of uracil from U-G or thymine from T-G. However, the mutant can distinguish between the C5-hydrogen and the C5-methyl group
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G179R
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structure modelling of the temperature-sensitive mutant Dts30, overview
L110F
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structure modelling of the temperature-sensitive mutant Dts27, overview
H194R
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
V90R
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
additional information
A59Y
the mutation leads to a decrease in its activity on xanthine, and 5-hydroxymethyluracil containing single stranded DNAs but not on uracil containing single stranded DNA
A59Y
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the mutation leads to a decrease in its activity on xanthine, and 5-hydroxymethyluracil containing single stranded DNAs but not on uracil containing single stranded DNA
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G183D/R302K
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the mutation causes a reduction in the enzyme activity but no increase in stability
G183D/R302K
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the mutations cause a reduction in the enzyme activity but no increase in stability
D183G
the mutant shows a slight increase in stability with concomitant reduction in the enzyme activity
D183G
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the mutant shows a slight increase in stability with concomitant reduction in the enzyme activity
D183G/K302R
the mutant shows a slight increase in stability with concomitant reduction in the enzyme activity
D183G/K302R
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the mutant shows a slight increase in stability with concomitant reduction in the enzyme activity
D88N
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site-directed mutagenesis of the active site Asp88, catalytically inactive mutant, analysis of substrate binding , overview
D88N
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site-directed mutagenesis of the active site Asp88, catalytically inactive mutant, analysis of substrate binding , overview
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D150E
displays reduced activity of about 70% of the wild type value
D150W
site-directed mutagenesis, the mutant shows 70% of wild-type enzyme activity
E132K
site-directed mutagenesis, a mutation in the HhH motif with a lysine residue equivalent to Lys120 in endonuclease III leading to conversion of the enzyme into a bifunctional glycosylase/AP lyase capable of both removing uracil at a glycosylic bond and cleaving the phosphodiester backbone at an AP site. Mutant E132K catalyzes a beta-elimination reaction at the AP site via uracil excision and forms a Schiff base intermediate in the form of a protein-DNA complex
E132K
mutation converts the enzyme into a bifunctional glycosylase/AP lyase capable of both removing uracil at a glycosylic bond and cleaving the phosphodiester backbone at an apurinic/apyrimidinic site. The mutant catalyzes a beta-elimination reaction at the apurinic/apyrimidinic site via uracil excision and forms a Schiff base intermediate in the form of a protein-DNA complex
Y152E
site-directed mutagenesis, the mutant shows unaltered enzyme activity compared to the wild-type enzyme
Y152E
retains unchanged levels of uracil-DNA glycosylase activity
Y152N
site-directed mutagenesis, the mutant shows unaltered enzyme activity compared to the wild-type enzyme
Y152N
retains unchanged levels of uracil-DNA glycosylase activity
DELTA90/W231A
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the mutant shows reduced class switch recombination efficiency and reduced deoxyuracil removal activity compared to the wild type enzyme
additional information
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the Arabidopsis mutant line GK-440E07 harbors a T-DNA insertion in the AtUNG gene. AtUNG-deficient plants do not display any apparent phenotype, but show increased resistance to 5-fluorouracil. The resistance of atung-/- mutants to 5-FU is accompanied by the accumulation of uracil residues in DNA
additional information
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a Ung-1 defective mutant strain TM2862 shows no uracil excision activity, but the mutation in the ung-1 gene does not affect development, fertility and lifespan in Caenorhanditis elegans, suggesting the existence of backup enzyme
additional information
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an ung-1 mutant has reduced ability to repair uracil-containing DNA. Ung-1 mutants show altered levels of apoptotic cell corpses formed in response to DNA damaging agents and increased apoptosis in response to ionizing radiation. The phenotype is a consequence of compensatory transcriptomic shifts that modulate oxidative stress responses in the mutant and not an effect of reduced DNA damage signaling, overview. Attenuation of paraquat-induced apoptosis in ung-1 mutant results from modulation of stress-induced signaling pathways, overview
additional information
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a Ung-1 defective mutant strain TM2862 shows no uracil excision activity, but the mutation in the ung-1 gene does not affect development, fertility and lifespan in Caenorhanditis elegans, suggesting the existence of backup enzyme
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additional information
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construction of infectious SVV mutants defective in either dUTPase or UDG activity or both using recA assisted restriction endonuclease cleavage and a cosmid recombination system. The mutant lose their viral dUTPase and UDG enzymatic activity in infected CV-1 cells
additional information
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construction of infectious SVV mutants defective in either dUTPase or UDG activity or both using recA assisted restriction endonuclease cleavage and a cosmid recombination system. The mutant lose their viral dUTPase and UDG enzymatic activity in infected CV-1 cells
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additional information
construction of a His-tagged truncated Thd1p variant comprising residues 650M-1063N from Escherichia coli strain BL21 (DE3)
additional information
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construction of a His-tagged truncated Thd1p variant comprising residues 650M-1063N from Escherichia coli strain BL21 (DE3)
additional information
allelic exchange of ung with ung::kan, ungY66H:amp or ungY66W:amp alleles shows 5fold, 3.0fold, and 2.0fold, respectively, increase in mutation frequencies, widening of the substrate binding pocket can lead to aquirement of thymine DNA glycosylase activity, overview
additional information
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UNG mutants with the set of bonds in the conserved 143GQ144 motif optimized for recognition of Cyt or Thy instead of Ura are able to excise normal pyrimidines from DNA and confer a spontaneous mutator phenotype to overexpressing Escherichia coli cells
additional information
depletion of UNG2 in macrophages by siRNA, HIV-1 virus fails to replicate in UNG2-depleted macrophages, UNG1 cannot compensate. Depletion of UNG2 in producer MAGI-CCR5 cells generates noninfectious virus, overview. Restoration of viral infectivity of UNG2-deficient virus by transfection of dUTPase-expressing vector in UNG2-depleted producer cells
additional information
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siRNA knockdown of endogenous UNG2 in primary cells show that UNG2 is required for R5 but not X4HIV infection and that this requirement is bypassed when HIV enters the target cell via vesicular stomatitis virus envelope-glycoprotein-mediated endocytosis. siRNA knockdown of UNG2 in virus-producing primary cells leads to defective R5 HIV virions that are unable to complete viral cDNA synthesis, overview
additional information
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reconstitution of a system with purified HSV-1 and human proteins that perform all the steps of uracil DNA glycosylase-initiated base excision repair in Herpes simplex virus-1, including HSV-1 uracil DNA glycosylase, UL2, product analysis, overview
additional information
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reconstitution of a system with purified HSV-1 and human proteins that perform all the steps of uracil DNA glycosylase-initiated base excision repair in Herpes simplex virus-1, including HSV-1 uracil DNA glycosylase, UL2, product analysis, overview
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additional information
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reconstitution of a minmal system from purified components of archaeal DNA uracil repair via direct strand incision, overview
additional information
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reconstitution of a minmal system from purified components of archaeal DNA uracil repair via direct strand incision, overview
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additional information
Ung knockout mice display no increase in mutation frequency due to the second UDG activity, SMUG1
additional information
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UNG deficiency reduces CSR efficiency to one tenth, but catalytically inactive mutants of UNG are fully proficient in CSR and several mutants at noncatalytic sites loose CSR activity. CSR activity by many UNG mutants critically depends on its N-terminal domain, irrespective of their enzymatic activities
additional information
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Ung knockout, Smug1 siRNA knockdown and Ung knockout/Smug1 knockdown mouse cells show that Smug1 and Ung2 are both required for the prevention of mutations and that their functions are not redundant
additional information
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nei nth double mutants exhibit an elevated spontaneous mutation frequency. Spontaneous mutations observed in the double mutant are solely from C to T transitions due to the inability to repair oxidized cytosines, which can be efficiently prevented by MtuNei1 and MtuNei2
additional information
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nei nth double mutants exhibit an elevated spontaneous mutation frequency. Spontaneous mutations observed in the double mutant are solely from C to T transitions due to the inability to repair oxidized cytosines, which can be efficiently prevented by MtuNei1 and MtuNei2
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additional information
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generation of udgB and ung knockout mutants by allelic replacement techniques. The general mutation frequency is increased in UDG knockout strains, frequencies of A:T to G:C mutations, which may arise through adenine deamination, in the udgB knockout mutant and in the double-knockout mutant are 10fold and 31fold higher that those in the wild-type strain, respectively, overview
additional information
mutagenesis of motifs A and B strongly attenuates the enzyme activity of UDGb
additional information
mutagenesis of motifs A and B strongly attenuates the enzyme activity of UDGb
additional information
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mutagenesis of motifs A and B strongly attenuates the enzyme activity of UDGb
