3.2.2.28: double-stranded uracil-DNA glycosylase
This is an abbreviated version!
For detailed information about double-stranded uracil-DNA glycosylase, go to the full flat file.
Word Map on EC 3.2.2.28
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3.2.2.28
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thymine
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mispairs
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guanine
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deamination
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cytosine
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thymine-dna
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glycosylases
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pyrimidine
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etheno
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purine
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3,n4-ethenocytosine
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thermus
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adducts
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thermophilus
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single-stranded
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dutp
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exocyclic
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n2,3-ethenoguanine
- 3.2.2.28
- thymine
- mispairs
- guanine
-
deamination
- cytosine
-
thymine-dna
- glycosylases
- pyrimidine
-
etheno
- purine
- 3,n4-ethenocytosine
-
thermus
- adducts
- thermophilus
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single-stranded
- dutp
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exocyclic
- n2,3-ethenoguanine
Reaction
Specifically hydrolyses mismatched double-stranded DNA and polynucleotides, releasing free uracil =
Synonyms
double stranded DNA specific UDG, double-strand uracil-DNA glycosylase, double-stranded uracil-DNA glycosylase, dsDNA specific UDG, dsUDG, Dug, family 5 UDGb, family 5 uracil DNA glycosylase, G:T/U mismatch-specific DNA glycosylase, More, MUG, UDG, UdgB, uracil DNA glycosylase
ECTree
3.2.2.28 double-stranded uracil-DNA glycosylaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.2.2.28 - double-stranded uracil-DNA glycosylase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,N4-ethenocytosine-containing single-stranded DNA + H2O
3,N4-ethenocytosine + single-stranded DNA with abasic site
the enzyme excised both 3,N4-ethenocytosine and uracil from DNA. 3,N4-ethenocytosine is significantly better as a substrate in terms of binding and hydrolysis. The tighter binding of the 3,N4-ethenocytosine containing substrate by MUG probably also accounts for its activity against single-stranded DNA containing 3,N4-ethenocytosine. Cleavage of the single-stranded substrate is 1500fold slower than the double-stranded substrate
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-
?
3,N4-ethenocytosine-mismatched double-stranded DNA + H2O
3,N4-ethenocytosine + double-stranded DNA with abasic site
hypoxanthine-mismatched double-stranded DNA + H2O
hypoxanthine + double-stranded DNA with abasic site
xanthine-mismatched double-stranded DNA + H2O
xanthine + double-stranded DNA with abasic site
xanthine-mismatched single-stranded DNA + H2O
xanthine + single-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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-
-
?
3,N4-ethenocytosine-mismatched double-stranded DNA + H2O
3,N4-ethenocytosine + double-stranded DNA with abasic site
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3,N4-ethenocytosine is recognized and efficiently excised from the 3,N4-ethenocytosine/G mismatch
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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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Dug is active on duplex oligonucleotides (34-mers) that contain site-specific 3,N4-ethenocytosine/G, and 3,N4-ethenocytosine/A mismatches
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-
?
3,N4-ethenocytosine-mismatched double-stranded DNA + H2O
3,N4-ethenocytosine + double-stranded DNA with abasic site
the enzyme excised both 3,N4-ethenocytosine and uracil from DNA. 3,N4-ethenocytosine is significantly better as a substrate in terms of binding and hydrolysis. The tighter binding of the 3,N4-ethenocytosine containing substrate by MUG probably also accounts for its activity against single-stranded DNA containing 3,N4-ethenocytosine. Cleavage of the single-stranded substrate is 1500fold slower than the double-stranded substrate. Of the different substrates tested, a duplex containing the 3,N4-ethenocytosine pair has the highest affinity for the enzyme, U/G is the next best substrate
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-
?
hypoxanthine-mismatched double-stranded DNA + H2O
hypoxanthine + double-stranded DNA with abasic site
the enzyme also acts as a hypoxanthine DNA glycosylase with the strongest activity on the G/I base pair but no activity detected on the C/I base pair
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-
?
hypoxanthine-mismatched double-stranded DNA + H2O
hypoxanthine + double-stranded DNA with abasic site
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
the enzyme also acts as a hypoxanthine DNA glycosylase with the strongest activity on the G/I base pair but no activity detected on the C/I base pair
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-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
dsUDG can remove uracil from G/U mispairs
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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Dug is active on duplex oligonucleotides (34-mers) that contain site-specific U/G or U/A mismatches. Dug excises a near stoichiometric amount of uracil from U/G-containing oligonucleotide substrate. The lack of turnover is the result of strong binding by Dug to the reaction product apyrimidinic-site
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-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
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excision of uracil from U/G mismatch
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-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
the enzyme activity against the uracil-containing single-stranded DNA is so low that it is not likely to be of any significance. Of the different substrates tested, a duplex containing the 3,N4-ethenocytosine pair has the highest affinity for the enzyme, U/G is the next best substrate
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-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
the enzyme acts as a double-stranded uracil DNA glycosylase with a relatively low activity on the A/U base pair
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
the enzyme acts as a double-stranded uracil DNA glycosylase with a relatively low activity on the A/U base pair
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-
?
xanthine-mismatched double-stranded DNA + H2O
xanthine + double-stranded DNA with abasic site
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-
-
?
xanthine-mismatched double-stranded DNA + H2O
xanthine + double-stranded DNA with abasic site
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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-
-
?
additional information
?
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Mug is expressed poorly in exponentially growing cells and has no apparent role in mutation avoidance in these cells. Mug is fairly abundant in stationary-phase cells and has an important anti-mutator role at this stage of cell growth
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-
?
additional information
?
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5-Hydroxyuracil and inosine (hypoxanthine) show cleavage rates 23 orders of magnitude slower than 3,N4-ethenocytosine. Thymine, 5-hydroxymethyluracil, and 5-hydroxycytosine are cleaved to some extent, although extremely slowly
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-
?
additional information
?
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-
activity is not detected on DNA containing a T/G mispair or single-stranded DNA containing either a site-specific uracil or 3,N4-ethenocytosine residue. Endonuclease IV stimulates Dug activity by enhancing the rate and extent of uracil excision by promoting dissociation of Dug from the apyrimidinic-site/G-containing 34-mer. Catalytically active endonuclease IV is required to mediate Dug turnover
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-
?
additional information
?
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inactive on single-stranded oligo(U)
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-
?
additional information
?
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the excision of thymine in a G/T mismatch by dsUDG is extremely low. This enzymatic activity does not have a real biological significance
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-
?
additional information
?
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UdgB substrate specificity with diverse DNA oligomers, overview, the enzyme excises ethenocytosine and hypoxanthine from dsDNA, in addition to uracil present as a single-nucleotide bulge in dsDNA, but excision of 5-OH-C, dihydroxyuracil, and epsilonA is undetectable, MtuUdgB does not excise uracil from SSU9 ssDNA, mechanism of action, overview
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-
?
additional information
?
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Mycobacterium tuberculosis H37Ra / ATCC 25177
UdgB substrate specificity with diverse DNA oligomers, overview, the enzyme excises ethenocytosine and hypoxanthine from dsDNA, in addition to uracil present as a single-nucleotide bulge in dsDNA, but excision of 5-OH-C, dihydroxyuracil, and epsilonA is undetectable, MtuUdgB does not excise uracil from SSU9 ssDNA, mechanism of action, overview
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-
?
additional information
?
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the enzyme showed no activity on oxanine-containing DNA substrates, uracil-mismatched single-stranded DNA and hypoxanthine-mismatched single-stranded DNA
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-
?
additional information
?
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Thermus thermophilus HB8 / ATCC 27634 / DSM 579
the enzyme showed no activity on oxanine-containing DNA substrates, uracil-mismatched single-stranded DNA and hypoxanthine-mismatched single-stranded DNA
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-
?
