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3,N4-ethenocytosine-mismatched double-stranded DNA + H2O
3,N4-ethenocytosine + double-stranded DNA with abasic site
3,N4-ethenocytosine-mismatched single-stranded DNA + H2O
3,N4-ethenocytosine + single-stranded DNA with abasic site
-
-
-
?
5-fluorouracil-mismatched double-stranded DNA + H2O
5-fluorouracil + double-stranded DNA with abasic site
5-formyluracil-mismatched double-stranded DNA + H2O
5-formyluracil + double-stranded DNA with abasic site
5-formyluracil-mismatched single-stranded DNA + H2O
5-formyluracil + single-stranded DNA with abasic site
-
-
-
?
5-hydroxymethyl-uracil-mismatched double-stranded DNA + H2O
5-hydroxymethyl-uracil + double-stranded DNA with abasic site
the preferred substrate of UDGb is hydroxymethyl-uracil mispaired with guanine, followed by G-U and A-U, UDGb is active on ethenocytosine-G and 5-fluorouracil-G pairs, and UDGb also performs processing of uracil and hydroxymethyluracil from single-stranded DNA, but highly prefers double-stranded DNA substrates
-
-
?
5-hydroxymethyl-uracil-mismatched single-stranded DNA + H2O
5-hydroxymethyl-uracil + single-stranded DNA with abasic site
the preferred substrate of UDGb is hydroxymethyl-uracil mispaired with guanine, followed by G-U and A-U, UDGb is active on ethenocytosine-G and 5-fluorouracil-G pairs, and UDGb also performs processing of uracil and hydroxymethyluracil from single-stranded DNA, but highly prefers double-stranded DNA substrates
-
-
?
5-hydroxymethyluracil-mismatched double-stranded DNA + H2O
5-hydroxymethyluracil + double-stranded DNA with abasic site
5-hydroxymethyluracil-mismatched double-stranded DNA with U-A mismatch + H2O
5-hydroxymethyluracil + double-stranded DNA with abasic site
-
-
-
?
5-hydroxymethyluracil-mismatched double-stranded DNA with U-G mismatch + H2O
5-hydroxymethyluracil + double-stranded DNA with abasic site
-
-
-
?
5-hydroxymethyluracil-mismatched single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
5-hydroxyuracil-mismatched double-stranded DNA + H2O
5-hydroxyuracil + double-stranded DNA with abasic site
5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
5-methylcytosine-mismatched double-stranded DNA + H2O
5-methylcytosine + double-stranded DNA with abasic site
-
-
-
?
8-oxoguanine-mismatched double-stranded DNA + H2O
8-oxoguanine + double-stranded DNA with abasic site
8-oxoguanine-mismatched single-stranded DNA + H2O
8-oxoguanine + single-stranded DNA with abasic site
deoxyuracil-containing single-stranded DNA + H2O
deoxyuracil + single-stranded DNA with abasic site
deoxyuracil-containing single-stranded RNA + H2O
deoxyuracil + single-stranded RNA
deoxyuracil-mismatched double-stranded DNA + H2O
deoxyuracil + double-stranded DNA with abasic site
double stranded DNA containing G-U mismatch + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
dUMP DNA + H2O
dUMP + DNA
dUMP-labeled calf thymus DNA + H2O
uracil + ?
ethenocytosine-mismatched double-stranded DNA + H2O
3,N4-ethenocytosine + double-stranded DNA with abasic site
UDGb is active on ethenocytosine-G
-
-
?
fU-containing 10 nucleotide DNA sequence 5'-GGAGAfUCTCC-3' with opposing C, T, A, or G + H2O
?
-
-
-
-
?
hydroxymethyluracil-containing single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
hypoxanthine-mismatched double-stranded DNA + H2O
hypoxanthine + double-stranded DNA with abasic site
the UDGb from Pyrobaculum aerophilum, belonging to a fifth UDG family, catalyzes the removal of uracil as well as of hypoxanthine from DNA by cleavage of e.g. hypoxanthine-thymine pairs, possessing an active site, that lacks the polar amino acid residue, see also EC 3.2.2.15, substrate specificity and active site structure, overview
-
-
?
M6-FAM-labeled single stranded oligonucleotide + H2O
uracil + ?
thymine-mismatched double-stranded DNA + H2O
thymine + double-stranded DNA with abasic site
uracil-containing calf thymus DNA + H2O
uracil + calf thymus DNA with abasic site
uracil-containing DNA + H2O
uracil + DNA with abasic site
uracil-containing double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
the rate of catalytic turnover (kcat), is higher with double-stranded substrate compared to single-stranded substrate (20/min versus 11/min), respectively. Catalytic efficiency is 3.5fold higher for single-stranded DNA due to the smaller Km-value
-
-
?
uracil-containing single stranded DNA + H2O
uracil + single stranded DNA with abasic site
-
duplex single stranded DNAs with sequences 5'-TGCACUUAAGAAUUTC-3'/5'-GAAATTCTTAAGTGCAGTGATAGTCTTCCGTCC-(CH2)7-methylene blue-3' and 5'-GAAATTCTTAAGTGCAGTGATAGTCTTCCGTCC-(CH2)7-methylene blue-3'/5'-TGGGGGTGCACTTAAGAATTTC-3'
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
uracil-guanine-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched 13 nt bubbled double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
low activity
-
-
?
uracil-mismatched 16 nt double-stranded DNA + H2O
uracil + 16 nt double-stranded DNA with abasic site
uracil-mismatched 19 nt bubbled double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
second best substrate
-
-
?
uracil-mismatched 19 nt shift bubbled double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
low activity
-
-
?
uracil-mismatched 7 nt bubbled double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
low activity
-
-
?
uracil-mismatched DNA + H2O
uracil + DNA with abasic site
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
uracil-mismatched double-stranded DNA with A-U mismatch + H2O
uracil + double-stranded DNA with abasic site
uracil-mismatched double-stranded DNA with U-A mismatch + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA with U-G mismatch + H2O
uracil + double-stranded DNA with abasic site
uracil-mismatched double-stranded oligonucleotide + H2O
uracil + double-stranded oligonucleotide with abasic site
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
uracil-mismatched single-stranded oligonucleotide + H2O
uracil + single-stranded oligonucleotide with abasic site
-
-
-
?
xanthine-containing single-stranded DNA + H2O
xanthine + single-stranded DNA with abasic site
-
-
-
?
additional information
?
-
3,N4-ethenocytosine-mismatched double-stranded DNA + H2O
3,N4-ethenocytosine + double-stranded DNA with abasic site
-
-
-
?
3,N4-ethenocytosine-mismatched double-stranded DNA + H2O
3,N4-ethenocytosine + double-stranded DNA with abasic site
-
-
-
?
5-fluorouracil-mismatched double-stranded DNA + H2O
5-fluorouracil + double-stranded DNA with abasic site
-
-
-
?
5-fluorouracil-mismatched double-stranded DNA + H2O
5-fluorouracil + double-stranded DNA with abasic site
UDGb is active on 5-fluorouracil-G pairs
-
-
?
5-fluorouracil-mismatched double-stranded DNA + H2O
5-fluorouracil + double-stranded DNA with abasic site
-
-
-
?
5-formyluracil-mismatched double-stranded DNA + H2O
5-formyluracil + double-stranded DNA with abasic site
-
-
-
?
5-formyluracil-mismatched double-stranded DNA + H2O
5-formyluracil + double-stranded DNA with abasic site
-
-
-
-
?
5-hydroxymethyluracil-mismatched double-stranded DNA + H2O
5-hydroxymethyluracil + double-stranded DNA with abasic site
-
-
-
?
5-hydroxymethyluracil-mismatched double-stranded DNA + H2O
5-hydroxymethyluracil + double-stranded DNA with abasic site
-
-
-
-
?
5-hydroxymethyluracil-mismatched single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
-
-
-
?
5-hydroxymethyluracil-mismatched single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
-
-
-
?
5-hydroxymethyluracil-mismatched single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
-
-
-
?
5-hydroxyuracil-mismatched double-stranded DNA + H2O
5-hydroxyuracil + double-stranded DNA with abasic site
-
-
-
?
5-hydroxyuracil-mismatched double-stranded DNA + H2O
5-hydroxyuracil + double-stranded DNA with abasic site
-
-
-
-
?
5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
DNA of Bacillus subtilis phage SPO1
-
-
?
5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
-
-
-
?
5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
-
-
-
?
5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
-
-
-
?
8-oxoguanine-mismatched double-stranded DNA + H2O
8-oxoguanine + double-stranded DNA with abasic site
the enzyme effciently removes uracil from both single- and double-stranded DNA. Activity with oligonucleotide duplexes containing 8-oxoguanine is 5fold lower than that of oligonucleotide duplex containing U:T
-
-
?
8-oxoguanine-mismatched double-stranded DNA + H2O
8-oxoguanine + double-stranded DNA with abasic site
the enzyme effciently removes uracil from both single- and double-stranded DNA. Activity with oligonucleotide duplexes containing 8-oxoguanine is 5fold lower than that of oligonucleotide duplex containing U:T
-
-
?
8-oxoguanine-mismatched single-stranded DNA + H2O
8-oxoguanine + single-stranded DNA with abasic site
the enzyme effciently removes uracil from both single- and double-stranded DNA
-
-
?
8-oxoguanine-mismatched single-stranded DNA + H2O
8-oxoguanine + single-stranded DNA with abasic site
the enzyme effciently removes uracil from both single- and double-stranded DNA
-
-
?
deoxyuracil-containing single-stranded DNA + H2O
deoxyuracil + single-stranded DNA with abasic site
-
-
-
-
?
deoxyuracil-containing single-stranded DNA + H2O
deoxyuracil + single-stranded DNA with abasic site
-
-
-
-
?
deoxyuracil-containing single-stranded RNA + H2O
deoxyuracil + single-stranded RNA
-
-
-
-
?
deoxyuracil-containing single-stranded RNA + H2O
deoxyuracil + single-stranded RNA
-
-
-
-
?
deoxyuracil-mismatched double-stranded DNA + H2O
deoxyuracil + double-stranded DNA with abasic site
-
isoform UDGIV removes deoxyuracil from double-stranded DNA in the following order of efficiency C/U = G/U > T/U > A/U. The preference order of double stranded DNA is G/U > C/U = T/U = A/U for isoform UDGV
-
-
?
deoxyuracil-mismatched double-stranded DNA + H2O
deoxyuracil + double-stranded DNA with abasic site
-
isoform UDGIV removes deoxyuracil from double-stranded DNA in the following order of efficiency C/U = G/U > T/U > A/U. The preference order of double stranded DNA is G/U > C/U = T/U = A/U for isoform UDGV
-
-
?
dUMP DNA + H2O
dUMP + DNA
-
-
-
-
?
dUMP DNA + H2O
dUMP + DNA
-
-
-
?
dUMP-labeled calf thymus DNA + H2O
uracil + ?
-
-
-
?
dUMP-labeled calf thymus DNA + H2O
uracil + ?
-
-
-
-
?
hydroxymethyluracil-containing single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
-
-
-
?
hydroxymethyluracil-containing single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
-
-
-
?
M6-FAM-labeled single stranded oligonucleotide + H2O
uracil + ?
T12-AGUA-T12
-
-
?
M6-FAM-labeled single stranded oligonucleotide + H2O
uracil + ?
-
T12-AGUA-T12
-
-
?
thymine-mismatched double-stranded DNA + H2O
thymine + double-stranded DNA with abasic site
-
-
-
?
thymine-mismatched double-stranded DNA + H2O
thymine + double-stranded DNA with abasic site
G-T mismatch is only a poor substrate for Thd1p
-
-
?
uracil-containing calf thymus DNA + H2O
uracil + calf thymus DNA with abasic site
-
-
-
-
?
uracil-containing calf thymus DNA + H2O
uracil + calf thymus DNA with abasic site
-
-
-
?
uracil-containing DNA + H2O
uracil + DNA with abasic site
-
uracil-containing DNA substrates with two uracil sites spaced 10, 40 or 80 bp apart
-
-
?
uracil-containing DNA + H2O
uracil + DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
the rate of catalytic turnover (kcat), is higher with double-stranded substrate compared to single-stranded substrate (20/min versus 11/min), respectively. Catalytic efficiency is 3.5fold higher for single-stranded DNA due to the smaller Km-value
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
isoform UNG1, which in contrast to isoform UNG2 lacks a PCNA-binding motif, may be specialized to act on single stranded DNA (ssDNA) through its ability to bind ssDNA-binding protein RPA
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
best substrate
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
isoform UNG1, which in contrast to isoform UNG2 lacks a PCNA-binding motif, may be specialized to act on single stranded DNA (ssDNA) through its ability to bind ssDNA-binding protein RPA
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched 16 nt double-stranded DNA + H2O
uracil + 16 nt double-stranded DNA with abasic site
5'-CCTGTCCAUGTCTCCG-3'
-
-
?
uracil-mismatched 16 nt double-stranded DNA + H2O
uracil + 16 nt double-stranded DNA with abasic site
5'-CCTGTCCAUGTCTCCG-3'
-
-
?
uracil-mismatched DNA + H2O
uracil + DNA with abasic site
-
-
-
-
?
uracil-mismatched DNA + H2O
uracil + DNA with abasic site
-
-
-
?
uracil-mismatched DNA + H2O
uracil + DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
removing uracil from double-stranded DNA containing either a U-A or U-G base pair
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
is capable of removing uracil from double-stranded DNA containing either a U/A or U/G base pair
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
the enzyme exhibits opposite base-dependent excision of uracil in order of decreasing efficiency: uridine, U:T, U:C, U:G, U:A
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
the enzyme is the principal and probably only glycosylase in Aeroglobus fulgidus that removes uracil incorporated opposite adenine in DNA during replication. The enzyme excises uracil more efficiently when it is opposite guanine than when it is opposite adenine
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
duplex DNA with A/U mismatch, substrate specificity, the base opposite to uracil in double strand DNAs affects uracil removal efficiencies in descending order U/-, U/T, U/C, U/G, U/A. Free uracil and abasic sites inhibit the reaction. Amino acids D77, H200, and A205 are important for the catalytic activity of UDG
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
duplex DNA with A/U mismatch, substrate specificity, the base opposite to uracil in double strand DNAs affects uracil removal efficiencies in descending order U/-, U/T, U/C, U/G, U/A. Free uracil and abasic sites inhibit the reaction. Amino acids D77, H200, and A205 are important for the catalytic activity of UDG
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
the enzyme removes uracil from DNA, which can occur by misincorporation of dUMP in place of dTMP during DNA synthesis or by deamination of cytosine, resulting in U-A or U-G mispairs
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-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
30-bp dsDNA oligonucleotide substrates containing G-C, G-U, G-T, and A-U base pairs. Determination of kinetics using commercially available nick-translated calf thymus DNA with deoxy[5-3H]uridine 5'-triphosphate as substrate. To perform efficient glycoside bond cleavage, drMUG must stabilize the mismatched uracil in the specificity pocket, nucleotide stabilization by Tyr46, substrate binding mechanism, overview. Binding of thymine in the activity pocket is probably prevented by Ser36 and Ser39 in MUG, binding of cytosine is prevented by Asp84
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-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
drUNG is able to excise uracil from both U-A and U-G double-stranded DNA and single-stranded DNA, substrate is commercially available nick-translated calf thymus DNA with deoxy[5-3H]uridine 5'-triphosphate: DNA binding, the active-site environment, and uracil specificity, structure-activity relationship, overview
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-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
substrate specificity, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
the enzyme initiates repair of uracil-DNA is achieved in a base-excision pathway
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
the enzyme hydrolyses the N-glycosidic bond connecting the base to the deoxyribose sugar of the DNA backbone, releasing free uracil base and DNA containing an abasic site, as its products, substrate recognition by family-1 UDG, modelling, detailed overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
Ung can utilize both double- and single-stranded substrates, preferring the latter
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
family 2 mismatch-specific uracil DNA glycosylase (MUG) is known to exhibit glycosylase activity on three mismatched base pairs, T/U, G/U and C/U. Family 1 uracil N-glycosylase (UNG) is an extremely efficient enzyme that can remove uracil from any uracil-containing base pairs including the A/U base pair
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
substrate specificity, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
substrate specificity: the enzyme excises uracil bases from DNA, it has a 2fold higher activity for single-stranded DNA than for double-stranded DNA, the substrate dUMP DNA is prepared by nick-translation and PCR of single-stranded calf-thymus DNA
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
the enzyme initiates repair of uracil-DNA is achieved in a base-excision pathway
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
substrate recognition by family-1 UDG, no activity against G-T mismatches or any of a range of other possible substrates, modelling, detailed overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
uracil detection and nucleotide flipping by UDG, pinchpushpull uracil detection mechanism, DNA binding structure, modelling, overview. The UDG shows preference for U-G mispairs compaired to U-A mispairs
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
the enzyme initiates repair of uracil-DNA is achieved in a base-excision pathway
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
substrate recognition by family-1 UDG, modelling, detailed overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
low activity
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
cytosine bases can be deaminated spontaneously to uracil, causing DNA damage. Uracil-DNA glycosylase repairs this kind of DNA damage
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
the enzyme effciently removes uracil from both single- and double-stranded DNA. Insignificant differences in activity level on the mismatched duplex substrates U:T, U:C, U:G and U:A. oligonucleotide substrates containing 3-mA, 7-mG and an apurinic/apyrimidinic site are not hydrolyzed by the enzyme
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
cytosine bases can be deaminated spontaneously to uracil, causing DNA damage. Uracil-DNA glycosylase repairs this kind of DNA damage
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
the enzyme effciently removes uracil from both single- and double-stranded DNA. Insignificant differences in activity level on the mismatched duplex substrates U:T, U:C, U:G and U:A. oligonucleotide substrates containing 3-mA, 7-mG and an apurinic/apyrimidinic site are not hydrolyzed by the enzyme
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
under physiological conditions of 60 mM NaCl, pH 7.5, increasing amounts of viral UNG cleave both 45mer U-G and PS-U oligonucleotides. Monkeypox virus, which occurs naturally in Africa, can cause a smallpoxlike disease in humans. The DNA repair protein uracil-DNA glycosylase, UNG, is one of the viral enzymes important for poxvirus pathogenesis, thus inhibition of UNG is a therapeutic strategy, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
cleavage of a duplex oligonucleotide containing a single lesion at a defined position. The viral mpUNG protein excises uracil and prefers the U-G pair over the U-A pair and does not excise oxidized bases
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
under physiological conditions of 60 mM NaCl, pH 7.5, increasing amounts of viral UNG cleave both 45mer U-G and PS-U oligonucleotides. Monkeypox virus, which occurs naturally in Africa, can cause a smallpoxlike disease in humans. The DNA repair protein uracil-DNA glycosylase, UNG, is one of the viral enzymes important for poxvirus pathogenesis, thus inhibition of UNG is a therapeutic strategy, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
cleavage of a duplex oligonucleotide containing a single lesion at a defined position. The viral mpUNG protein excises uracil and prefers the U-G pair over the U-A pair and does not excise oxidized bases
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
the highly preferred substrate of UDGa is uracil mispaired with guanine, followed by A-U pairs, no activity with hydroxymethyl-uracil mispaired with guanine, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
UDGs of the four UDG families catalyze the removal of uracil from DNA by flipping it out of the double helix into their binding pockets, where the glycosidic bond is hydrolyzed by a water molecule activated by an aromatic amino acid, while the UDGb from Pyrobaculum aerophilum, belonging to a fifth UDG family, catalyzes the removal of uracil, possessing an active site, that lacks the polar amino acid residue, see also EC 3.2.2.15, substrate specificity and active site structure, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
UDGs of the four UDG families, uracil-DNA glycosylase including Pyrobaculum aerophilum UDGa, catalyze the removal of uracil from DNA by flipping it out of the double helix into their binding pockets, where the glycosidic bond is hydrolyzed by a water molecule activated by an aromatic amino acid, while the UDGb from Pyrobaculum aerophilum, belonging to a fifth UDG family, also catalyzes the removal of hypoxanthine from DNA possessing an active site, that lacks the polar amino acid residue, substrate specificity and active site structure, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
uracil residues in G/U mispairs, in A/U pairs. Preference for G/U substrate over A/U substrate and uracil in single-stranded DNA
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
uracil residues in G/U mispairs, in A/U pairs. Preference for G/U substrate over A/U substrate and uracil in single-stranded DNA
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
the formation of archaeal chromatin is highly repressive to UDG1 activity, mechanistic basis for coupling UDG1 to the replication fork, modelling, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
UDG1 shows a marked preference for substrates containing a G-U base pair over either A-U or single-stranded uracil-containing DNA substrates, and it interacts with a single subunit of the heterotrimeric sliding clamp proliferating cell nuclear antigen, PCNA, in a PIP motif-dependent manner, a conserved C-terminal consensus interaction motif, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
UDG is a DNA repair enzyme removing uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP, and it is the primary activity in the DNA base excision repair pathway, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
TMUDG removes uracil from double-stranded oligonucleotides containing either a U-G or a U-A base pair, e.g. from a 30mer ds oligonucleotide, DNA containing 3H-labeled uracil substrate preparation by nick translation of calf thymus DNA, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
UDG is a DNA repair enzyme removing uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP, and it is the primary activity in the DNA base excision repair pathway, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
TMUDG removes uracil from double-stranded oligonucleotides containing either a U-G or a U-A base pair, e.g. from a 30mer ds oligonucleotide, DNA containing 3H-labeled uracil substrate preparation by nick translation of calf thymus DNA, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
Q7WYV4
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
Q7WYV4
UDG removes uracil from DNA to initiate DNA base excision repair, Thermus thermophilus UDG processes both single-stranded and double-stranded DNA containing uracil, regardless of opposing base, but does not process G-T mismatched DNA, nor does it possess AP endonuclease activity, uracil bases in U-A mismatches are excised less efficiently, due to the stability of that particular base-pair. The UDG possesses a [4Fe-4S] cluster, distant from the active site, which interacts with loop structures and is unessential to the activity but necessary for stabilizing the loop structures. Uracil recognition mechanism, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
Q7WYV4
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
Q7WYV4
UDG removes uracil from DNA to initiate DNA base excision repair, Thermus thermophilus UDG processes both single-stranded and double-stranded DNA containing uracil, regardless of opposing base, but does not process G-T mismatched DNA, nor does it possess AP endonuclease activity, uracil bases in U-A mismatches are excised less efficiently, due to the stability of that particular base-pair. The UDG possesses a [4Fe-4S] cluster, distant from the active site, which interacts with loop structures and is unessential to the activity but necessary for stabilizing the loop structures. Uracil recognition mechanism, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
the DNA repair protein uracil-DNA glycosylase is one of the viral enzymes important for poxvirus pathogenesis, it is part of the base excision repair pathway, BER
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
UDG catalyzes excision of uracil from DNA. The viral UDG plays an essential role in viral replication as a component of the DNA polymerase processivity factor. It adopts a catalysis-independent role in DNA replication that involves interaction with a viral protein, A20, to form the processivity factor. UDG-A20 association is essential for assembling of the processive DNA polymerase complex, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
UNG excises uracil from DNA, preferentially when it is opposite to cytosine
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA with A-U mismatch + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA with A-U mismatch + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA with U-G mismatch + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA with U-G mismatch + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA with U-G mismatch + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded oligonucleotide + H2O
uracil + double-stranded oligonucleotide with abasic site
oligonucleotide duplex containing a U:T mispair
-
-
?
uracil-mismatched double-stranded oligonucleotide + H2O
uracil + double-stranded oligonucleotide with abasic site
oligonucleotide duplex containing a U:T mispair
-
-
?
uracil-mismatched double-stranded oligonucleotide + H2O
uracil + double-stranded oligonucleotide with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
removing uracil from single-stranded DNA containing either a U-A or U-G base pair
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
single-stranded 26-mer uracil-containing 2'-deoxyribose oligonucleotide
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
single-stranded DNA containing uracil labeled with fluorescein in the 5'-end, sequence overview. Determination of kinetics using commercially available nick-translated calf thymus DNA with deoxy[5-3H]uridine 5'-triphosphate as substrate. To perform efficient glycoside bond cleavage, drMUG must stabilize the mismatched uracil in the specificity pocket, nucleotide stabilization by Tyr46, substrate binding mechanism, overview. Binding of thymine in the activity pocket is probably prevented by Ser36 and Ser39 in MUG, binding of cytosine is prevented by Asp84
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
Ung catalyzes the removal of uracil from Ura-Cyt pairs in single-stranded long DNA consisting of identical repeated lesion-containing oligonucleotide units, constructed by ligation. Ung can utilize both double- and single-stranded substrates, preferring the latter
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
family 2 mismatch-specific uracil DNA glycosylase (MUG) is known to exhibit glycosylase activity on three mismatched base pairs, T/U, G/U and C/U. Family 1 uracil N-glycosylase (UNG) is an extremely efficient enzyme that can remove uracil from any uracil-containing base pairs including the A/U base pair
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
substrate specificity: the enzyme excises uracil bases from DNA, it has a 2fold higher activity for single-stranded DNA than for double-stranded DNA, the substrate dUMP DNA is prepared by nick-translation and PCR of single-stranded calf-thymus DNA
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
single-stranded 26-mer uracil-containing 2'-deoxyribose oligonucleotide
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
SMUG1 is specific for ssDNA substrates, substrate recognition by family-3 SMUG, modelling, detailed overview
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
the enzyme effciently removes uracil from both single- and double-stranded DNA
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
the enzyme effciently removes uracil from both single- and double-stranded DNA
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
Monkeypox virus, which occurs naturally in Africa, can cause a smallpox-like disease in humans. The DNA repair protein uracil-DNA glycosylase, UNG, is one of the viral enzymes important for poxvirus pathogenesis, thus inhibition of UNG is a therapeutic strategy, overview
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
cleavage of a single-stranded oligonucleotide containing a single lesion at a defined position, usage of single-stranded DNA oligonucleotide labeled with a 5'-fluorescein and a 3'-dabsyl. The viral mpUNG protein excises uracil preferentially from single-stranded DNA and does not excise oxidized bases
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
Monkeypox virus, which occurs naturally in Africa, can cause a smallpox-like disease in humans. The DNA repair protein uracil-DNA glycosylase, UNG, is one of the viral enzymes important for poxvirus pathogenesis, thus inhibition of UNG is a therapeutic strategy, overview
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
cleavage of a single-stranded oligonucleotide containing a single lesion at a defined position, usage of single-stranded DNA oligonucleotide labeled with a 5'-fluorescein and a 3'-dabsyl. The viral mpUNG protein excises uracil preferentially from single-stranded DNA and does not excise oxidized bases
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
UDGs of the four UDG families catalyze the removal of uracil from DNA by flipping it out of the double helix into their binding pockets, where the glycosidic bond is hydrolyzed by a water molecule activated by an aromatic amino acid, while the UDGb from Pyrobaculum aerophilum, belonging to a fifth UDG family, catalyzes the removal of uracil, possessing an active site, that lacks the polar amino acid residue, see also EC 3.2.2.15, substrate specificity and active site structure, overview
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
Q7WYV4
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
Q7WYV4
UDG removes uracil from DNA to initiate DNA base excision repair, Thermus thermophilus UDG processes both single-stranded and double-stranded DNA containing uracil, regardless of opposing base, but does not process G-T mismatched DNA, nor does it possess AP endonuclease activity, uracil bases in U-A mismatches are excised less efficiently, due to the stability of that particular base-pair. The UDG possesses a [4Fe-4S] cluster, distant from the active site, which interacts with loop structures and is unessential to the activity but necessary for stabilizing the loop structures. Uracil recognition mechanism, overview
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
Q7WYV4
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
Q7WYV4
UDG removes uracil from DNA to initiate DNA base excision repair, Thermus thermophilus UDG processes both single-stranded and double-stranded DNA containing uracil, regardless of opposing base, but does not process G-T mismatched DNA, nor does it possess AP endonuclease activity, uracil bases in U-A mismatches are excised less efficiently, due to the stability of that particular base-pair. The UDG possesses a [4Fe-4S] cluster, distant from the active site, which interacts with loop structures and is unessential to the activity but necessary for stabilizing the loop structures. Uracil recognition mechanism, overview
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
The viral UDG enzyme is highly specific for uracil and preferentially excises uracil when present in single stranded DNA, the reaction mechanism of the viral enzyme is different from the human host enzyme, active site structure and motifs, modelling, overview
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
additional information
?
-
-
AtUNG is the major UDG activity in Arabidopsis thaliana AtUNG excises uracil in vivo but generates toxic AP sites when processing abundant U:A pairs in dTTP-depleted cells
-
-
?
additional information
?
-
-
AtUNG exhibits the narrow substrate specificity and single-stranded DNA preference, it is active on 5'-labeled 51mer oligonucleotide duplex containing a U:G mispair. AtUNG is significantly more active on U:G mispairs than on U:A pairs. The activity on U:T and U:C mispairs is slightly lower than on U:G, but higher than on U:A pairs
-
-
?
additional information
?
-
the protein is devoid of methyl purine and formamidopyrimidine DNA glycosylase activity, respectively
-
-
?
additional information
?
-
-
the protein is devoid of methyl purine and formamidopyrimidine DNA glycosylase activity, respectively
-
-
?
additional information
?
-
UDG specifically and selectively removes uracil bases from DNA, substrate specificity, overview
-
-
?
additional information
?
-
-
UDG specifically and selectively removes uracil bases from DNA, substrate specificity, overview
-
-
?
additional information
?
-
UDG specifically and selectively removes uracil bases from DNA, substrate specificity, overview
-
-
?
additional information
?
-
the enzyme does not utilize DNA oligomer containing inosine or thymine in single stranded DNA or double stranded DNA
-
-
?
additional information
?
-
-
the enzyme does not utilize DNA oligomer containing inosine or thymine in single stranded DNA or double stranded DNA
-
-
?
additional information
?
-
the enzyme prefers single stranded DNA
-
-
?
additional information
?
-
-
the enzyme prefers single stranded DNA
-
-
?
additional information
?
-
the enzyme does not utilize DNA oligomer containing inosine or thymine in single stranded DNA or double stranded DNA
-
-
?
additional information
?
-
the enzyme prefers single stranded DNA
-
-
?
additional information
?
-
-
UNG-1 removes uracil from both U-G and U-A base pairs in DNA. It also removes uracil from single-stranded oligonucleotide substrate less efficiently than double-stranded oligonucleotide. The active site A is present between residues 116-137, active site B at residues 247-253. Aromatic residues Tyr125, Phe136 and His247 are involved in the stacking interaction with uracil
-
-
?
additional information
?
-
-
the enzyme shows activity on double-stranded as well as single-stranded DNAs, the assay uses a 19mer oligodeoxyribonucleotide substrate containing a single uracil residue (5'-CATAAAGTGUAAAGCCTGG-3') and a guanine or adenine residue opposite uracil
-
-
?
additional information
?
-
-
UNG-1 removes uracil from both U-G and U-A base pairs in DNA. It also removes uracil from single-stranded oligonucleotide substrate less efficiently than double-stranded oligonucleotide. The active site A is present between residues 116-137, active site B at residues 247-253. Aromatic residues Tyr125, Phe136 and His247 are involved in the stacking interaction with uracil
-
-
?
additional information
?
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enzyme substrate is uracil-labeled calf thymus DNA prepared by nick translation with dUTP
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additional information
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enzyme substrate is uracil-labeled calf thymus DNA prepared by nick translation with dUTP
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5-methylcytosine and thymine derivatives are processed with an appreciable efficiency only by the human and the Drosophila enzymes
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additional information
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5-methylcytosine and thymine derivatives are processed with an appreciable efficiency only by the human and the Drosophila enzymes
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additional information
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the enzyme shows a broad and species-specific substrate spectrum, substrate binding structure, overview. The common most efficiently processed substrates of all are uracil and 3,N4-ethenocytosine opposite guanine and 5-fluorouracil in any double-stranded DNA context, the enzyme is able to hydrolyze a non-damaged 5'-methylcytosine opposite G, and the double strand and mismatch dependency of the enzymes varies with the substrate
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additional information
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the enzyme shows a broad and species-specific substrate spectrum, substrate binding structure, overview. The common most efficiently processed substrates of all are uracil and 3,N4-ethenocytosine opposite guanine and 5-fluorouracil in any double-stranded DNA context, the enzyme is able to hydrolyze a non-damaged 5'-methylcytosine opposite G, and the double strand and mismatch dependency of the enzymes varies with the substrate
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additional information
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family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by base-sampling probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. Although structures are not yet available for family-3/SMUG and family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family
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additional information
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Ung catalyzes the removal of uracil from Ura-Cyt pairs in single-stranded long DNA consisting of identical repeated lesion-containing oligonucleotide units, constructed by ligation. Ung can utilize both double- and single-stranded substrates, preferring the latter
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additional information
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UNG removes uracil from DNA, substrate recognition and catalytic reaction mechanism, short-range sliding is vital for extrahelical uracil trapping, intramolecular transfer mechanisms of the enzyme, detailed overview
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additional information
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uracil-DNA glycosylases are ubiquitously found enzymes that hydrolyze the N-glycosidic bond of deoxyuridine, generating from deamination of cytosine, in DNA, UNG enzymes specifically excise Ura bases from both double-stranded and single-stranded DNA with a slight preference for the latter substrate, and shows no activity against normal DNA bases or against uracil in RNA. As potentially mutagenic and deleterious for cell regulation, uracil must be removed from DNA
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additional information
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preparation of a set of model nucleosome substrates, of 154mer DNA, in which single thymidine residues are replaced with uracil at specific locations and a second set of nucleosomes in which uracils are randomly substituted for all thymidines. UDG efficiently removes uracil from internal locations in the nucleosome where the DNA backbone is oriented away from the surface of the histone octamer, without significant disruption of histone-DNA interactions. However, uracils at sites oriented toward the histone octamer surface are excised at much slower rates, consistent with a mechanism requiring spontaneous DNA unwrapping from the nucleosome. In contrast to the nucleosome core, UDG activity on DNA outside the core DNA region is similar to that of naked DNA, overview
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additional information
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UNG hydrolyzes the N-glycosidic bond of deoxyuridine in DNA. It binds with appreciable affinity to any DNA, mainly due to the interactions with the charged backbone. Search for the lesion by UNG involves random sliding along DNA alternating with dissociation-association events and partial eversion of undamaged bases for initial sampling. DNA in the complex with UNG is highly distorted to allow the extrahelical recognition of uracil, mechanism of uracil search and recognition by UNG, overview
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additional information
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Ung shows strict specificity for uracil excision activity
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additional information
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SMUG1 is an uracil-DNA glycosylase, that also shows xanthine-DNA glycosylase activity, XDG, EC 3.2.2.15, but is not active in excising hypoxanthine and oxanine from DNA
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additional information
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SMUG1 is an uracil-DNA glycosylase, that also shows xanthine-DNA glycosylase activity, XDG, EC 3.2.2.15, but is not active in excising hypoxanthine and oxanine from DNA
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additional information
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SMUG1 is an uracil-DNA glycosylase, that also shows xanthine-DNA glycosylase activity, XDG, EC 3.2.2.15, but is not active in excising hypoxanthine and oxanine from DNA
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additional information
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substrate specificity, overview
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additional information
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substrate specificity, overview
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additional information
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dual role of hSMUG1 as a backup enzyme for UNG and a primary repair enzyme for a subset of oxidized pyrimidines such as 5-formyluracil, 5-hydroxymethyluracil, and 5-hydroxyuracil
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additional information
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dual role of hSMUG1 as a backup enzyme for UNG and a primary repair enzyme for a subset of oxidized pyrimidines such as 5-formyluracil, 5-hydroxymethyluracil, and 5-hydroxyuracil
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additional information
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family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by base-sampling probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. Although structures are not yet available for family-3/SMUG and family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family
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additional information
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hSMUG1 removes uracil from both double- and single-stranded DNA in nuclear chromatin, hSMUG1 has a broad substrate specificity, including 5-hydroxymethyluracil, and 3,N4-ethenocytosine. hSMUG1 acts as a broad specificity backup and is the major 5-hydroxymethyluracil-DNA glycosylase in nuclear cell extracts, overview
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additional information
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hSMUG1 removes uracil from both double- and single-stranded DNA in nuclear chromatin, hSMUG1 has a broad substrate specificity, including 5-hydroxymethyluracil, and 3,N4-ethenocytosine. hSMUG1 acts as a broad specificity backup and is the major 5-hydroxymethyluracil-DNA glycosylase in nuclear cell extracts, overview
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additional information
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hSMUG1 removes uracil from both double- and single-stranded DNA, including 5-hydroxy-2'-deoxyuridine and 5-carboxy-2'-deoxyuridine, substrate selectivity mechanism, overview
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additional information
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hSMUG1 removes uracil from both double- and single-stranded DNA, including 5-hydroxy-2'-deoxyuridine and 5-carboxy-2'-deoxyuridine, substrate selectivity mechanism, overview
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additional information
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hUNG2 removes uracil from both double- and single-stranded DNA in nuclear chromatin. hUNG2 in nuclear extracts initiates base excision repair of plasmids containing either U-A and U-G in vitro. hUNG2 is responsible for both prereplicative removal of deaminated cytosine and postreplicative removal of misincorporated uracil at the replication fork, it is the major enzyme for removal of deaminated cytosine outside of replication foci, overview
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additional information
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hUNG2 removes uracil from both double- and single-stranded DNA in nuclear chromatin. hUNG2 in nuclear extracts initiates base excision repair of plasmids containing either U-A and U-G in vitro. hUNG2 is responsible for both prereplicative removal of deaminated cytosine and postreplicative removal of misincorporated uracil at the replication fork, it is the major enzyme for removal of deaminated cytosine outside of replication foci, overview
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additional information
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UDG initiates DNA base excision repair, BER, by hydrolyzing the uracil base from the deoxyribose. BER repairs a wide range of base lesions through the use of many different DNA glycosylases specific for distinct types of DNA damage, UDG activity is cell-cycle dependent and generally higher in proliferating cells than in non-cycling cells, overview
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additional information
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UNG2 is an important enzyme in the base excision repair pathway, interaction with Ugene is involved in the phenotype of colon cancer, Ugene interacts with the base excision repair pathway, overview
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additional information
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uracil DNA glycosylase acts in removing uracil from the sugar backbone of DNA, leaving abasic sites and initiating the uracil base-excision-repair pathway, BER. The human UNG2 enzyme, but not UNG1, is packaged and incorporated into HIV-1 virions via specific interaction with the integrase domain of the Gag-Pol precursor, the virally Vpr protein might also able to mediate the incorporation of UNG2, packaged UNG2 can process uracil from DNA, indicating that HIV-1 has the ability to control dUTP misincorporation in viral DNA, the enzyme is essential to the HIV-1 life cycle. HIV-1 RT and UNG2 recombinant proteins can process uracil from primer-template substrate, molecular mechanism
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additional information
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preference of hSMUG1 for mispaired uracil over uracil paired with adenine, substrate selectivity with oligonucleotide 24-mers containing uracil with different 5-substituents, overview
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additional information
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preference of hSMUG1 for mispaired uracil over uracil paired with adenine, substrate selectivity with oligonucleotide 24-mers containing uracil with different 5-substituents, overview
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additional information
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SMUG1 is a monofunctional DNA glycosylase specific for uracil residues, and has appreciable selectivity for single-stranded rather than double-stranded DNA substrates, overview
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additional information
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SMUG1 is a monofunctional DNA glycosylase specific for uracil residues, and has appreciable selectivity for single-stranded rather than double-stranded DNA substrates, overview
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additional information
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SMUG1 is an uracil-DNA glycosylase, that also shows xanthine-DNA glycosylase activity, XDG, EC 3.2.2.15
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additional information
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SMUG1 is an uracil-DNA glycosylase, that also shows xanthine-DNA glycosylase activity, XDG, EC 3.2.2.15
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additional information
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specific excision and removal of dUTP from dsDNA and ssDNA, cleavage of for U-A and U-G pairs. UNG2 binds to Ugene, a nuclear protein overexpressed in colon cancer, Ugene-p binds to the NH2-terminus of UNG2, which does not directly alter UNG2 enzymatic activity or localization, interaction analysis, overview
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additional information
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substrate specificity of SMUG, activity of hSMUG1 against uracil containing single- and double-stranded DNA containing matched and mismatched uracil, overview
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additional information
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substrate specificity of SMUG, activity of hSMUG1 against uracil containing single- and double-stranded DNA containing matched and mismatched uracil, overview
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additional information
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substrate specificity, overview. hSMUG1 removes damaged bases from Fenton-oxidized calf thymus DNA, generating abasic sites
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additional information
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substrate specificity, overview. hSMUG1 removes damaged bases from Fenton-oxidized calf thymus DNA, generating abasic sites
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additional information
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substrate specificity, the enzyme is not active with other oxidized pyrimidines such as 5-hydroxycytosine, 5-formylcytosine and thymine glycol, and intact pyrimidines such as thymine and cytosine. Mutational analysis of the catalytic and damage-recognition mechanism of hSMUG1, overview
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additional information
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substrate specificity, the enzyme is not active with other oxidized pyrimidines such as 5-hydroxycytosine, 5-formylcytosine and thymine glycol, and intact pyrimidines such as thymine and cytosine. Mutational analysis of the catalytic and damage-recognition mechanism of hSMUG1, overview
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additional information
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hSMUG1 shows excision activity for 5-formyluracil, a major thymine lesion formed by ionizing radiation, opposite all normal bases in DNA
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additional information
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UNG2 of the human host is required by HIV-1 strain R5, but not by X4HIV, during the early stage of infection
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additional information
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uracil DNA glycosylase does not show any activity on G:IU, i.e. iodouridine, or A:IU mispairs
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additional information
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uracil in single-stranded DNA, resulting from incorporation of dUMP during replication and from spontaneous or enzymatic deamination of cytosine, causing U:A pairs or U:G mismatches, respectively, has to be removed by the enzyme. Nuclear UNG2 is apparently the sole contributor to the post-replicative repair of U:A lesions and to the removal of uracil from U:G contexts in immunoglobulin genes as part of somatic hypermutation and class-switch recombination processes in adaptive immunity. UNG2 and SMUG1 contribute to U:G repair. UNG2 is highly specific for uracil, SMUG1 also efficiently removes 5-hydroxymethyluracil
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additional information
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uracil-DNA glycosylases are ubiquitously found enzymes that hydrolyze the N-glycosidic bond of deoxyuridine, generating from deamination of cytosine, in DNA, UNG enzymes specifically excise Ura bases from both double-stranded and single-stranded DNA with a slight preference for the latter substrate, and shows no activity against normal DNA bases or against uracil in RNA. As potentially mutagenic and deleterious for cell regulation, uracil must be removed from DNA
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additional information
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excision of 5-formyluracil, fU, from fU-containing 10 nucleotide DNA sequence 5'-GGAGAfUCTCC-3'. Substrate-binding pocket of hSMUG1 and its interactions with uracil and fU, base-pairing properties of fU residues in DNA, structures, overview
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additional information
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SMUG1 binds tightly to AP sites and inhibits cleavage by AP-endonucleases
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additional information
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UNG hydrolyzes the N-glycosidic bond of deoxyuridine in DNA. It binds with appreciable affinity to any DNA, mainly due to the interactions with the charged backbone. Search for the lesion by UNG involves random sliding along DNA alternating with dissociation-association events and partial eversion of undamaged bases for initial sampling. DNA in the complex with UNG is highly distorted to allow the extrahelical recognition of uracil, mechanism of uracil search and recognition by UNG, structure-function relationship, overview
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additional information
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the enzyme primarily interacts with the phosphate backbone on the single strand of DNA. The enzyme does not require a continuous polyanion DNA strand
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additional information
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family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by base-sampling probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. Although structures are not yet available for family-3/SMUG and family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family
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additional information
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UDG is responsible for the removal of uracil from DNA with U-A or U-G mismatch, UDG is active on single- or double-stranded DNA, the damage recognition step in the HSV-1 UDG reaction pathway is modulated by local DNA sequences, substrate specificity with several oligonucleotide substrate possessing U-A or U-G mispairs, overview
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additional information
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viral uracil DNA glycosylase, UL2, in conjunction with the HSV-1 DNA polymerase catalytic subunit, UL30, cellular AP endonuclease and DNA ligase IIIalpha/XRCC1, perform uracil-initiated base excision repair. UL30 exhibits apurinic/apyrimidinic and 5'-deoxyribose phosphate lyase activities. UL2 and UL30 co-localize to viral prereplicative sites. The interaction between HSV-1 proteins UL2 and Pol occurs in HSV-1 infected cells
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additional information
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cleavage of oligonucleotide PBAZ7 which contains a U at position 17
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additional information
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UDG is responsible for the removal of uracil from DNA with U-A or U-G mismatch, UDG is active on single- or double-stranded DNA, the damage recognition step in the HSV-1 UDG reaction pathway is modulated by local DNA sequences, substrate specificity with several oligonucleotide substrate possessing U-A or U-G mispairs, overview
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additional information
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UL114 and DNA polymerase catalytic subunit UL54 act in concert during base excision repair of the viral genome
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additional information
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direct UL114-UL54 interaction. The UL54 carboxyl terminus is not required for UL54-UL114 interaction, but for UL114-UL44 interaction, overview
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additional information
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no enzymatic activity is detected with double-stranded and single-stranded hypoxanthine-, xanthine-, 5-hydroxymethyluracil-, 5-hydroxyuracil-, 8-oxoguanine-, 8-oxoadenine-, 5,6-dihydroxyuracil, 5-hydroxycytosine-, thymine glycol-, N6-methyladenine-, O6-methylguanine-, and ethenoadenine-containing DNA
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additional information
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no enzymatic activity is detected with double-stranded and single-stranded hypoxanthine-, xanthine-, 5-hydroxymethyluracil-, 5-hydroxyuracil-, 8-oxoguanine-, 8-oxoadenine-, 5,6-dihydroxyuracil, 5-hydroxycytosine-, thymine glycol-, N6-methyladenine-, O6-methylguanine-, and ethenoadenine-containing DNA
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additional information
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DNA uracil repair occurs ubiquitously throughout all existant life forms. Base excision repair is triggered by a uracil DNA glycosylase, UDG. The organism uniquely initiates DNA repair by direct strand incision next to the DNA-U residue, a reaction catalyzed by the DNA uridine endonuclease Mth212, detailed mechanism, overview
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additional information
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DNA uracil repair occurs ubiquitously throughout all existant life forms. Base excision repair is triggered by a uracil DNA glycosylase, UDG. The organism uniquely initiates DNA repair by direct strand incision next to the DNA-U residue, a reaction catalyzed by the DNA uridine endonuclease Mth212, detailed mechanism, overview
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additional information
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SMUG1 is specialized for antimutational uracil excision in mammalian cells. Ung knockout mice display no increase in mutation frequency due to the second UDG activity, SMUG1
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additional information
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SMUG1 also excises the oxidation-damage product 5-hydroxymethyluracil, but like UNG is inactive against thymine, i.e. 5-methyluracil, displacement/replacement mechanism allowing SMUG1 to exclude thymine from its active site while accepting 5-hydroxymethyluracil, overview
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additional information
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deamination of cytosine in DNA leads to formation of uracil, which is removed by uracil DNA glycosylase, UNG. The N-terminus of UNG is required for class switch recombination activity, overview
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additional information
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uracil in single-stranded DNA, resulting from incorporation of dUMP during replication and from spontaneous or enzymatic deamination of cytosine, causing U:A pairs or U:G mismatches, respectively, has to be removed by the enzyme. Nuclear UNG2 is apparently the sole contributor to the post-replicative repair of U:A lesions and to the removal of uracil from U:G contexts in immunoglobulin genes as part of somatic hypermutation and class-switch recombination processes in adaptive immunity. UNG2 and SMUG1 contribute to U:G repair. UNG2 is highly specific for uracil, SMUG1 also efficiently removes 5-hydroxymethyluracil
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additional information
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uracil DNA glycosylase uses single-stranded DNA substrate, a 5'-FITC-labeled oligonucleotide of 30mer with an internal single U residue
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additional information
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MtuNei1 recognizes oxidized pyrimidines on both double-stranded and single-stranded DNA and exhibits uracil DNA glycosylase activity. MtuNei2 and MtuNei1 can prevent G to T transversions probably by removing oxidized guanine products, such as Sp and urea
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additional information
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MtuNei1 recognizes oxidized pyrimidines on both double-stranded and single-stranded DNA and exhibits uracil DNA glycosylase activity. MtuNei1 excises thymine glycol and strongly prefers the 5R isomers. GC/MS analysis of products released by MtuNei1, overview. Substrates are oligonucleotides with 7,8-dihydro-8-oxoguanine, thymine glycol, 5,6-dihydrouracil, 5,6-dihydrothymine, 5-hydroxyuracil, 5-hydroxycytosine, uracil, and furan
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additional information
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MtuNei1 recognizes oxidized pyrimidines on both double-stranded and single-stranded DNA and exhibits uracil DNA glycosylase activity. MtuNei2 and MtuNei1 can prevent G to T transversions probably by removing oxidized guanine products, such as Sp and urea
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additional information
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MtuNei1 recognizes oxidized pyrimidines on both double-stranded and single-stranded DNA and exhibits uracil DNA glycosylase activity. MtuNei1 excises thymine glycol and strongly prefers the 5R isomers. GC/MS analysis of products released by MtuNei1, overview. Substrates are oligonucleotides with 7,8-dihydro-8-oxoguanine, thymine glycol, 5,6-dihydrouracil, 5,6-dihydrothymine, 5-hydroxyuracil, 5-hydroxycytosine, uracil, and furan
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additional information
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UDG initiates uracil excision repair to safeguard the genomic integrity, mechanism, overview
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additional information
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Mycobacterium smegmatis UDG excises uracil from different loop positions of tetraloop hairpin substrates with comparable efficiencies, substrate Escherichia coli RZ1032 dut1 ung1 genomic DNA
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additional information
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UdgB removes aberrant bases uracil, from deaminated cytosine, and hypoxanthine, from deaminated adenine, and 5-fluorouracil from DNA with high efficiency
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additional information
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UDG initiates uracil excision repair to safeguard the genomic integrity, mechanism, overview
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additional information
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Mycobacterium smegmatis UDG excises uracil from different loop positions of tetraloop hairpin substrates with comparable efficiencies, substrate Escherichia coli RZ1032 dut1 ung1 genomic DNA
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additional information
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UDG specifically and selectively removes uracil bases from DNA, substrate specificity, overview
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additional information
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UDG specifically and selectively removes uracil bases from DNA, substrate specificity, overview
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additional information
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the preferred substrate of UDGb is hydroxymethyl-uracil mispaired with guanine, followed by G-U and A-U, UDGb is active on ethenocytosine-G and 5-fluorouracil-G pairs, and UDGb also performs processing of uracil and hydroxymethyluracil from single-stranded DNA, but highly prefers double-stranded DNA substrates, no activity on G-T pairs, overview
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additional information
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the preferred substrate of UDGb is hydroxymethyl-uracil mispaired with guanine, followed by G-U and A-U, UDGb is active on ethenocytosine-G and 5-fluorouracil-G pairs, and UDGb also performs processing of uracil and hydroxymethyluracil from single-stranded DNA, but highly prefers double-stranded DNA substrates, no activity on G-T pairs, overview
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additional information
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the preferred substrate of UDGb is hydroxymethyl-uracil mispaired with guanine, followed by G-U and A-U, UDGb is active on ethenocytosine-G and 5-fluorouracil-G pairs, and UDGb also performs processing of uracil and hydroxymethyluracil from single-stranded DNA, but highly prefers double-stranded DNA substrates, no activity on G-T pairs, overview
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additional information
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substrate specificity, overview
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additional information
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the enzyme shows a broad and species-specific substrate spectrum, substrate binding structure, overview. The common most efficiently processed substrates of all are uracil and 3,N4-ethenocytosine opposite guanine and 5-fluorouracil in any double-stranded DNA context, the enzyme is able to hydrolyze a non-damaged 5'-methylcytosine opposite G, and the double strand and mismatch dependency of the enzymes varies with the substrate, G-T mismatch is no substrate for Thp1p. Thp1p shows little preference for mismatched substrate and processes uracil opposite A or in an ssDNA context with remarkable efficiency, overview
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additional information
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the enzyme shows a broad and species-specific substrate spectrum, substrate binding structure, overview. The common most efficiently processed substrates of all are uracil and 3,N4-ethenocytosine opposite guanine and 5-fluorouracil in any double-stranded DNA context, the enzyme is able to hydrolyze a non-damaged 5'-methylcytosine opposite G, and the double strand and mismatch dependency of the enzymes varies with the substrate, G-T mismatch is no substrate for Thp1p. Thp1p shows little preference for mismatched substrate and processes uracil opposite A or in an ssDNA context with remarkable efficiency, overview
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additional information
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the removal of ribose-linked uracil from DNA backbone is inefficient. The enzyme cannot remove 2,2'-anhydro uridine, hypoxanthine, and 7-deazaxanthine from single-stranded DNA and single-stranded DNA
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additional information
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the removal of ribose-linked uracil from DNA backbone is inefficient. The enzyme cannot remove 2,2'-anhydro uridine, hypoxanthine, and 7-deazaxanthine from single-stranded DNA and single-stranded DNA
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additional information
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the enzyme initiates base excision repair, BER, using a closed circular DNA substrate containing a unique U-G base pair
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additional information
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the enzyme is capable of removing uracil from DNA containing either a U-A or a U-G base pair. The enzyme is also active on single-stranded DNA containing uracil
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additional information
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the enzyme is capable of removing uracil from DNA containing either a U-A or a U-G base pair. The enzyme is also active on single-stranded DNA containing uracil
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additional information
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the enzyme is capable of removing uracil from DNA containing either a U-A or a U-G base pair. The enzyme is also active on single-stranded DNA containing uracil
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additional information
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Q7WYV4
UDG is an essential enzyme for maintaining the integrity of genomic information, it is the first enzyme of a base excision repair, BER, pathway that corrects uracil lesions. TthUDG specifically recognizes uracil that is flipped out from double-stranded DNA, in a manner similar to that of the family 1 human UDG, rather than binding to the guanine base of the complementary strand in mismatched DNA, as does the family 2 Escherichia coli MUG
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additional information
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UDG removes uracil generated by the deamination of cytosine or misincorporation of deoxyuridine monophosphate. The fifth UDG family lacks a polar residue in the active-site motif, which mediates the hydrolysis of the glycosidic bond by activation of a water molecule in UDG families 1 to 4
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additional information
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family 5 UDGB in complex with rAP-G DNA and rAP-A DNA, substrate specificity and binding structure analysis, modelling, overview
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additional information
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the enzyme does not show any detectable activity on other deaminated bases than uracil
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additional information
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the enzyme does not show any detectable activity on other deaminated bases than uracil
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additional information
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UDG removes uracil generated by the deamination of cytosine or misincorporation of deoxyuridine monophosphate. The fifth UDG family lacks a polar residue in the active-site motif, which mediates the hydrolysis of the glycosidic bond by activation of a water molecule in UDG families 1 to 4
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additional information
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family 5 UDGB in complex with rAP-G DNA and rAP-A DNA, substrate specificity and binding structure analysis, modelling, overview
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additional information
?
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Q7WYV4
UDG is an essential enzyme for maintaining the integrity of genomic information, it is the first enzyme of a base excision repair, BER, pathway that corrects uracil lesions. TthUDG specifically recognizes uracil that is flipped out from double-stranded DNA, in a manner similar to that of the family 1 human UDG, rather than binding to the guanine base of the complementary strand in mismatched DNA, as does the family 2 Escherichia coli MUG
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additional information
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SMUG1 is a monofunctional DNA glycosylase specific for uracil residues, and has appreciable selectivity for single-stranded rather than double-stranded DNA substrates, overview
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3,N4-ethenocytosine-mismatched double-stranded DNA + H2O
3,N4-ethenocytosine + double-stranded DNA with abasic site
3,N4-ethenocytosine-mismatched single-stranded DNA + H2O
3,N4-ethenocytosine + single-stranded DNA with abasic site
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?
5-fluorouracil-mismatched double-stranded DNA + H2O
5-fluorouracil + double-stranded DNA with abasic site
5-formyluracil-mismatched double-stranded DNA + H2O
5-formyluracil + double-stranded DNA with abasic site
5-formyluracil-mismatched single-stranded DNA + H2O
5-formyluracil + single-stranded DNA with abasic site
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?
5-hydroxymethyl-uracil-mismatched double-stranded DNA + H2O
5-hydroxymethyl-uracil + double-stranded DNA with abasic site
the preferred substrate of UDGb is hydroxymethyl-uracil mispaired with guanine, followed by G-U and A-U, UDGb is active on ethenocytosine-G and 5-fluorouracil-G pairs, and UDGb also performs processing of uracil and hydroxymethyluracil from single-stranded DNA, but highly prefers double-stranded DNA substrates
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5-hydroxymethyl-uracil-mismatched single-stranded DNA + H2O
5-hydroxymethyl-uracil + single-stranded DNA with abasic site
the preferred substrate of UDGb is hydroxymethyl-uracil mispaired with guanine, followed by G-U and A-U, UDGb is active on ethenocytosine-G and 5-fluorouracil-G pairs, and UDGb also performs processing of uracil and hydroxymethyluracil from single-stranded DNA, but highly prefers double-stranded DNA substrates
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5-hydroxymethyluracil-mismatched double-stranded DNA + H2O
5-hydroxymethyluracil + double-stranded DNA with abasic site
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5-hydroxymethyluracil-mismatched single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
5-hydroxyuracil-mismatched double-stranded DNA + H2O
5-hydroxyuracil + double-stranded DNA with abasic site
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?
5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
5-methylcytosine-mismatched double-stranded DNA + H2O
5-methylcytosine + double-stranded DNA with abasic site
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ethenocytosine-mismatched double-stranded DNA + H2O
3,N4-ethenocytosine + double-stranded DNA with abasic site
UDGb is active on ethenocytosine-G
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hypoxanthine-mismatched double-stranded DNA + H2O
hypoxanthine + double-stranded DNA with abasic site
the UDGb from Pyrobaculum aerophilum, belonging to a fifth UDG family, catalyzes the removal of uracil as well as of hypoxanthine from DNA by cleavage of e.g. hypoxanthine-thymine pairs, possessing an active site, that lacks the polar amino acid residue, see also EC 3.2.2.15, substrate specificity and active site structure, overview
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thymine-mismatched double-stranded DNA + H2O
thymine + double-stranded DNA with abasic site
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?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
uracil-mismatched DNA + H2O
uracil + DNA with abasic site
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
additional information
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3,N4-ethenocytosine-mismatched double-stranded DNA + H2O
3,N4-ethenocytosine + double-stranded DNA with abasic site
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3,N4-ethenocytosine-mismatched double-stranded DNA + H2O
3,N4-ethenocytosine + double-stranded DNA with abasic site
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?
5-fluorouracil-mismatched double-stranded DNA + H2O
5-fluorouracil + double-stranded DNA with abasic site
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5-fluorouracil-mismatched double-stranded DNA + H2O
5-fluorouracil + double-stranded DNA with abasic site
UDGb is active on 5-fluorouracil-G pairs
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5-fluorouracil-mismatched double-stranded DNA + H2O
5-fluorouracil + double-stranded DNA with abasic site
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5-formyluracil-mismatched double-stranded DNA + H2O
5-formyluracil + double-stranded DNA with abasic site
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?
5-formyluracil-mismatched double-stranded DNA + H2O
5-formyluracil + double-stranded DNA with abasic site
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?
5-hydroxymethyluracil-mismatched single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
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5-hydroxymethyluracil-mismatched single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
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5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
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5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
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5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
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uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
isoform UNG1, which in contrast to isoform UNG2 lacks a PCNA-binding motif, may be specialized to act on single stranded DNA (ssDNA) through its ability to bind ssDNA-binding protein RPA
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uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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isoform UNG1, which in contrast to isoform UNG2 lacks a PCNA-binding motif, may be specialized to act on single stranded DNA (ssDNA) through its ability to bind ssDNA-binding protein RPA
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uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-mismatched DNA + H2O
uracil + DNA with abasic site
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uracil-mismatched DNA + H2O
uracil + DNA with abasic site
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uracil-mismatched DNA + H2O
uracil + DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
the enzyme removes uracil from DNA, which can occur by misincorporation of dUMP in place of dTMP during DNA synthesis or by deamination of cytosine, resulting in U-A or U-G mispairs
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
the enzyme initiates repair of uracil-DNA is achieved in a base-excision pathway
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
family 2 mismatch-specific uracil DNA glycosylase (MUG) is known to exhibit glycosylase activity on three mismatched base pairs, T/U, G/U and C/U. Family 1 uracil N-glycosylase (UNG) is an extremely efficient enzyme that can remove uracil from any uracil-containing base pairs including the A/U base pair
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
the enzyme initiates repair of uracil-DNA is achieved in a base-excision pathway
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
the enzyme initiates repair of uracil-DNA is achieved in a base-excision pathway
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
cytosine bases can be deaminated spontaneously to uracil, causing DNA damage. Uracil-DNA glycosylase repairs this kind of DNA damage
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
cytosine bases can be deaminated spontaneously to uracil, causing DNA damage. Uracil-DNA glycosylase repairs this kind of DNA damage
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?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
under physiological conditions of 60 mM NaCl, pH 7.5, increasing amounts of viral UNG cleave both 45mer U-G and PS-U oligonucleotides. Monkeypox virus, which occurs naturally in Africa, can cause a smallpoxlike disease in humans. The DNA repair protein uracil-DNA glycosylase, UNG, is one of the viral enzymes important for poxvirus pathogenesis, thus inhibition of UNG is a therapeutic strategy, overview
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
under physiological conditions of 60 mM NaCl, pH 7.5, increasing amounts of viral UNG cleave both 45mer U-G and PS-U oligonucleotides. Monkeypox virus, which occurs naturally in Africa, can cause a smallpoxlike disease in humans. The DNA repair protein uracil-DNA glycosylase, UNG, is one of the viral enzymes important for poxvirus pathogenesis, thus inhibition of UNG is a therapeutic strategy, overview
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
the highly preferred substrate of UDGa is uracil mispaired with guanine, followed by A-U pairs, no activity with hydroxymethyl-uracil mispaired with guanine, overview
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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the formation of archaeal chromatin is highly repressive to UDG1 activity, mechanistic basis for coupling UDG1 to the replication fork, modelling, overview
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
UDG is a DNA repair enzyme removing uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP, and it is the primary activity in the DNA base excision repair pathway, overview
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
UDG is a DNA repair enzyme removing uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP, and it is the primary activity in the DNA base excision repair pathway, overview
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
Q7WYV4
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
Q7WYV4
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
the DNA repair protein uracil-DNA glycosylase is one of the viral enzymes important for poxvirus pathogenesis, it is part of the base excision repair pathway, BER
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
UDG catalyzes excision of uracil from DNA. The viral UDG plays an essential role in viral replication as a component of the DNA polymerase processivity factor. It adopts a catalysis-independent role in DNA replication that involves interaction with a viral protein, A20, to form the processivity factor. UDG-A20 association is essential for assembling of the processive DNA polymerase complex, overview
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uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
family 2 mismatch-specific uracil DNA glycosylase (MUG) is known to exhibit glycosylase activity on three mismatched base pairs, T/U, G/U and C/U. Family 1 uracil N-glycosylase (UNG) is an extremely efficient enzyme that can remove uracil from any uracil-containing base pairs including the A/U base pair
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
Monkeypox virus, which occurs naturally in Africa, can cause a smallpox-like disease in humans. The DNA repair protein uracil-DNA glycosylase, UNG, is one of the viral enzymes important for poxvirus pathogenesis, thus inhibition of UNG is a therapeutic strategy, overview
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?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
Monkeypox virus, which occurs naturally in Africa, can cause a smallpox-like disease in humans. The DNA repair protein uracil-DNA glycosylase, UNG, is one of the viral enzymes important for poxvirus pathogenesis, thus inhibition of UNG is a therapeutic strategy, overview
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?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
UDGs of the four UDG families catalyze the removal of uracil from DNA by flipping it out of the double helix into their binding pockets, where the glycosidic bond is hydrolyzed by a water molecule activated by an aromatic amino acid, while the UDGb from Pyrobaculum aerophilum, belonging to a fifth UDG family, catalyzes the removal of uracil, possessing an active site, that lacks the polar amino acid residue, see also EC 3.2.2.15, substrate specificity and active site structure, overview
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
Q7WYV4
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
Q7WYV4
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
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?
additional information
?
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AtUNG is the major UDG activity in Arabidopsis thaliana AtUNG excises uracil in vivo but generates toxic AP sites when processing abundant U:A pairs in dTTP-depleted cells
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additional information
?
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5-methylcytosine and thymine derivatives are processed with an appreciable efficiency only by the human and the Drosophila enzymes
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?
additional information
?
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5-methylcytosine and thymine derivatives are processed with an appreciable efficiency only by the human and the Drosophila enzymes
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?
additional information
?
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family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by base-sampling probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. Although structures are not yet available for family-3/SMUG and family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family
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?
additional information
?
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uracil-DNA glycosylases are ubiquitously found enzymes that hydrolyze the N-glycosidic bond of deoxyuridine, generating from deamination of cytosine, in DNA, UNG enzymes specifically excise Ura bases from both double-stranded and single-stranded DNA with a slight preference for the latter substrate, and shows no activity against normal DNA bases or against uracil in RNA. As potentially mutagenic and deleterious for cell regulation, uracil must be removed from DNA
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?
additional information
?
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dual role of hSMUG1 as a backup enzyme for UNG and a primary repair enzyme for a subset of oxidized pyrimidines such as 5-formyluracil, 5-hydroxymethyluracil, and 5-hydroxyuracil
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?
additional information
?
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dual role of hSMUG1 as a backup enzyme for UNG and a primary repair enzyme for a subset of oxidized pyrimidines such as 5-formyluracil, 5-hydroxymethyluracil, and 5-hydroxyuracil
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?
additional information
?
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family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by base-sampling probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. Although structures are not yet available for family-3/SMUG and family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family
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?
additional information
?
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hSMUG1 removes uracil from both double- and single-stranded DNA in nuclear chromatin, hSMUG1 has a broad substrate specificity, including 5-hydroxymethyluracil, and 3,N4-ethenocytosine. hSMUG1 acts as a broad specificity backup and is the major 5-hydroxymethyluracil-DNA glycosylase in nuclear cell extracts, overview
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?
additional information
?
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hSMUG1 removes uracil from both double- and single-stranded DNA in nuclear chromatin, hSMUG1 has a broad substrate specificity, including 5-hydroxymethyluracil, and 3,N4-ethenocytosine. hSMUG1 acts as a broad specificity backup and is the major 5-hydroxymethyluracil-DNA glycosylase in nuclear cell extracts, overview
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?
additional information
?
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hSMUG1 removes uracil from both double- and single-stranded DNA, including 5-hydroxy-2'-deoxyuridine and 5-carboxy-2'-deoxyuridine, substrate selectivity mechanism, overview
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?
additional information
?
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hSMUG1 removes uracil from both double- and single-stranded DNA, including 5-hydroxy-2'-deoxyuridine and 5-carboxy-2'-deoxyuridine, substrate selectivity mechanism, overview
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additional information
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hUNG2 removes uracil from both double- and single-stranded DNA in nuclear chromatin. hUNG2 in nuclear extracts initiates base excision repair of plasmids containing either U-A and U-G in vitro. hUNG2 is responsible for both prereplicative removal of deaminated cytosine and postreplicative removal of misincorporated uracil at the replication fork, it is the major enzyme for removal of deaminated cytosine outside of replication foci, overview
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additional information
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hUNG2 removes uracil from both double- and single-stranded DNA in nuclear chromatin. hUNG2 in nuclear extracts initiates base excision repair of plasmids containing either U-A and U-G in vitro. hUNG2 is responsible for both prereplicative removal of deaminated cytosine and postreplicative removal of misincorporated uracil at the replication fork, it is the major enzyme for removal of deaminated cytosine outside of replication foci, overview
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additional information
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UDG initiates DNA base excision repair, BER, by hydrolyzing the uracil base from the deoxyribose. BER repairs a wide range of base lesions through the use of many different DNA glycosylases specific for distinct types of DNA damage, UDG activity is cell-cycle dependent and generally higher in proliferating cells than in non-cycling cells, overview
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additional information
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UNG2 is an important enzyme in the base excision repair pathway, interaction with Ugene is involved in the phenotype of colon cancer, Ugene interacts with the base excision repair pathway, overview
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additional information
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uracil DNA glycosylase acts in removing uracil from the sugar backbone of DNA, leaving abasic sites and initiating the uracil base-excision-repair pathway, BER. The human UNG2 enzyme, but not UNG1, is packaged and incorporated into HIV-1 virions via specific interaction with the integrase domain of the Gag-Pol precursor, the virally Vpr protein might also able to mediate the incorporation of UNG2, packaged UNG2 can process uracil from DNA, indicating that HIV-1 has the ability to control dUTP misincorporation in viral DNA, the enzyme is essential to the HIV-1 life cycle. HIV-1 RT and UNG2 recombinant proteins can process uracil from primer-template substrate, molecular mechanism
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additional information
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hSMUG1 shows excision activity for 5-formyluracil, a major thymine lesion formed by ionizing radiation, opposite all normal bases in DNA
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additional information
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UNG2 of the human host is required by HIV-1 strain R5, but not by X4HIV, during the early stage of infection
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additional information
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uracil DNA glycosylase does not show any activity on G:IU, i.e. iodouridine, or A:IU mispairs
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additional information
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uracil in single-stranded DNA, resulting from incorporation of dUMP during replication and from spontaneous or enzymatic deamination of cytosine, causing U:A pairs or U:G mismatches, respectively, has to be removed by the enzyme. Nuclear UNG2 is apparently the sole contributor to the post-replicative repair of U:A lesions and to the removal of uracil from U:G contexts in immunoglobulin genes as part of somatic hypermutation and class-switch recombination processes in adaptive immunity. UNG2 and SMUG1 contribute to U:G repair. UNG2 is highly specific for uracil, SMUG1 also efficiently removes 5-hydroxymethyluracil
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additional information
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uracil-DNA glycosylases are ubiquitously found enzymes that hydrolyze the N-glycosidic bond of deoxyuridine, generating from deamination of cytosine, in DNA, UNG enzymes specifically excise Ura bases from both double-stranded and single-stranded DNA with a slight preference for the latter substrate, and shows no activity against normal DNA bases or against uracil in RNA. As potentially mutagenic and deleterious for cell regulation, uracil must be removed from DNA
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additional information
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family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by base-sampling probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. Although structures are not yet available for family-3/SMUG and family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family
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additional information
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viral uracil DNA glycosylase, UL2, in conjunction with the HSV-1 DNA polymerase catalytic subunit, UL30, cellular AP endonuclease and DNA ligase IIIalpha/XRCC1, perform uracil-initiated base excision repair. UL30 exhibits apurinic/apyrimidinic and 5'-deoxyribose phosphate lyase activities. UL2 and UL30 co-localize to viral prereplicative sites. The interaction between HSV-1 proteins UL2 and Pol occurs in HSV-1 infected cells
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additional information
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UL114 and DNA polymerase catalytic subunit UL54 act in concert during base excision repair of the viral genome
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additional information
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DNA uracil repair occurs ubiquitously throughout all existant life forms. Base excision repair is triggered by a uracil DNA glycosylase, UDG. The organism uniquely initiates DNA repair by direct strand incision next to the DNA-U residue, a reaction catalyzed by the DNA uridine endonuclease Mth212, detailed mechanism, overview
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additional information
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DNA uracil repair occurs ubiquitously throughout all existant life forms. Base excision repair is triggered by a uracil DNA glycosylase, UDG. The organism uniquely initiates DNA repair by direct strand incision next to the DNA-U residue, a reaction catalyzed by the DNA uridine endonuclease Mth212, detailed mechanism, overview
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additional information
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SMUG1 is specialized for antimutational uracil excision in mammalian cells. Ung knockout mice display no increase in mutation frequency due to the second UDG activity, SMUG1
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additional information
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deamination of cytosine in DNA leads to formation of uracil, which is removed by uracil DNA glycosylase, UNG. The N-terminus of UNG is required for class switch recombination activity, overview
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additional information
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uracil in single-stranded DNA, resulting from incorporation of dUMP during replication and from spontaneous or enzymatic deamination of cytosine, causing U:A pairs or U:G mismatches, respectively, has to be removed by the enzyme. Nuclear UNG2 is apparently the sole contributor to the post-replicative repair of U:A lesions and to the removal of uracil from U:G contexts in immunoglobulin genes as part of somatic hypermutation and class-switch recombination processes in adaptive immunity. UNG2 and SMUG1 contribute to U:G repair. UNG2 is highly specific for uracil, SMUG1 also efficiently removes 5-hydroxymethyluracil
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additional information
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MtuNei1 recognizes oxidized pyrimidines on both double-stranded and single-stranded DNA and exhibits uracil DNA glycosylase activity. MtuNei2 and MtuNei1 can prevent G to T transversions probably by removing oxidized guanine products, such as Sp and urea
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additional information
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MtuNei1 recognizes oxidized pyrimidines on both double-stranded and single-stranded DNA and exhibits uracil DNA glycosylase activity. MtuNei2 and MtuNei1 can prevent G to T transversions probably by removing oxidized guanine products, such as Sp and urea
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additional information
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UDG initiates uracil excision repair to safeguard the genomic integrity, mechanism, overview
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additional information
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UdgB removes aberrant bases uracil, from deaminated cytosine, and hypoxanthine, from deaminated adenine, and 5-fluorouracil from DNA with high efficiency
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additional information
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UDG initiates uracil excision repair to safeguard the genomic integrity, mechanism, overview
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additional information
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the preferred substrate of UDGb is hydroxymethyl-uracil mispaired with guanine, followed by G-U and A-U, UDGb is active on ethenocytosine-G and 5-fluorouracil-G pairs, and UDGb also performs processing of uracil and hydroxymethyluracil from single-stranded DNA, but highly prefers double-stranded DNA substrates, no activity on G-T pairs, overview
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additional information
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the preferred substrate of UDGb is hydroxymethyl-uracil mispaired with guanine, followed by G-U and A-U, UDGb is active on ethenocytosine-G and 5-fluorouracil-G pairs, and UDGb also performs processing of uracil and hydroxymethyluracil from single-stranded DNA, but highly prefers double-stranded DNA substrates, no activity on G-T pairs, overview
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additional information
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the preferred substrate of UDGb is hydroxymethyl-uracil mispaired with guanine, followed by G-U and A-U, UDGb is active on ethenocytosine-G and 5-fluorouracil-G pairs, and UDGb also performs processing of uracil and hydroxymethyluracil from single-stranded DNA, but highly prefers double-stranded DNA substrates, no activity on G-T pairs, overview
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additional information
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Q7WYV4
UDG is an essential enzyme for maintaining the integrity of genomic information, it is the first enzyme of a base excision repair, BER, pathway that corrects uracil lesions. TthUDG specifically recognizes uracil that is flipped out from double-stranded DNA, in a manner similar to that of the family 1 human UDG, rather than binding to the guanine base of the complementary strand in mismatched DNA, as does the family 2 Escherichia coli MUG
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additional information
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UDG removes uracil generated by the deamination of cytosine or misincorporation of deoxyuridine monophosphate. The fifth UDG family lacks a polar residue in the active-site motif, which mediates the hydrolysis of the glycosidic bond by activation of a water molecule in UDG families 1 to 4
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additional information
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UDG removes uracil generated by the deamination of cytosine or misincorporation of deoxyuridine monophosphate. The fifth UDG family lacks a polar residue in the active-site motif, which mediates the hydrolysis of the glycosidic bond by activation of a water molecule in UDG families 1 to 4
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additional information
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Q7WYV4
UDG is an essential enzyme for maintaining the integrity of genomic information, it is the first enzyme of a base excision repair, BER, pathway that corrects uracil lesions. TthUDG specifically recognizes uracil that is flipped out from double-stranded DNA, in a manner similar to that of the family 1 human UDG, rather than binding to the guanine base of the complementary strand in mismatched DNA, as does the family 2 Escherichia coli MUG
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D173F
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site-directed mutagenesis
D173R
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site-directed mutagenesis
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
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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D93A
site-directed mutagenesis, inactive mutant
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
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site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
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H187Q
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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
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
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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
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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
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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
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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
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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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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
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
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displays reduced activity of about 70% of the wild type value
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D150W
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completely lacks DNA glycosylase activity
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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
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the mutant shows about 180 of wild type uracil removal activity
G87V
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a SMUG1 mutant, the mutation affects the thymine expulsion
G87Y
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a SMUG1 mutant, the mutation affects the thymine expulsion
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
N163D
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a SMUG1 mutant, the mutation affects the substrate binding
N85A
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a SMUG1 mutant, the mutation affects the H2O coordination
W231A
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the mutant shows about 20% of wild type uracil removal activity
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
L169A
the mutant retains most of the wild type activity
N171A
the mutant retains most of the wild type activity
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
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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
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
site-directed mutagenesis, inactive mutant
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
D150W
completely lacks DNA glycosylase 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 less than 20% of wild type uracil removal 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
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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
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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
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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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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
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mutagenesis of motifs A and B strongly attenuates the enzyme activity of UDGb
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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
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