Data extracted from this reference:
Activating Compound
endonuclease IV
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
Escherichia coli
Cloned(Commentary)
Inhibitors
additional information
double-strand uracil-DNA glycosylase is insensitive to uracil-DNA glycosylase inhibitor protein, i.e. Ugi
Escherichia coli
Molecular Weight [Da]
18670
matrix-assisted laser desorption-ionization mass spectrometry
Escherichia coli
Organism
Purification (Commentary)
native and recombinant protein
Escherichia coli
Substrates and Products (Substrate)
3,N4-ethenocytosine-mismatched double-stranded DNA + H2O
Dug is active on duplex oligonucleotides (34-mers) that contain site-specific 3,N4-ethenocytosine/G, and 3,N4-ethenocytosine/A mismatches
690873
Escherichia coli
3,N4-ethenocytosine + double-stranded DNA with abasic site
?
additional information
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
690873
Escherichia coli
?
uracil-mismatched double-stranded DNA + H2O
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
690873
Escherichia coli
uracil + double-stranded DNA with abasic site
?
Activating Compound (protein specific)
endonuclease IV
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
Escherichia coli
Cloned(Commentary) (protein specific)
Inhibitors (protein specific)
additional information
double-strand uracil-DNA glycosylase is insensitive to uracil-DNA glycosylase inhibitor protein, i.e. Ugi
Escherichia coli
Molecular Weight [Da] (protein specific)
18670
matrix-assisted laser desorption-ionization mass spectrometry
Escherichia coli
Purification (Commentary) (protein specific)
native and recombinant protein
Escherichia coli
Substrates and Products (Substrate) (protein specific)
3,N4-ethenocytosine-mismatched double-stranded DNA + H2O
Dug is active on duplex oligonucleotides (34-mers) that contain site-specific 3,N4-ethenocytosine/G, and 3,N4-ethenocytosine/A mismatches
690873
Escherichia coli
3,N4-ethenocytosine + double-stranded DNA with abasic site
?
additional information
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
690873
Escherichia coli
?
uracil-mismatched double-stranded DNA + H2O
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
690873
Escherichia coli
uracil + double-stranded DNA with abasic site
?
Other publictions for EC 3.2.2.28
732137
Xia
Specificity and catalytic mech ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
J. Biol. Chem.
289
18413-18426
2014
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679463
Srinath
Substrate specificities and fu ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Ra / ATCC 25177
DNA Repair
6
1517-1528
2007
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692966
O'Neill
Mismatch uracil glycosylase fr ...
Escherichia coli
J. Biol. Chem.
278
20526-20532
2003
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694210
Mokkapati
Escherichia coli DNA glycosyla ...
Escherichia coli
Mol. Microbiol.
41
1101-1111
2001
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690873
Sung
Mosbaugh, D.W.: Escherichia co ...
Escherichia coli
Biochemistry
39
10224-10235
2000
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692063
Barrett
Crystal structure of a thwarte ...
Escherichia coli
EMBO J.
18
6599-6609
1999
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691667
Barrett
Crystal structure of a G:T/U m ...
Escherichia coli
Cell
92
117-129
1998
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694927
Saparbaev
3,N4-ethenocytosine, a highly ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
95
8508-8513
1998
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694330
Gallinari
A new class of uracil-DNA glyc ...
Escherichia coli
Nature
383
735-738
1996
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