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show all sequences of 3.2.2.28

Mosbaugh, D.W.: Escherichia coli double-strand uracil-DNA glycosylase: involvement in uracil-mediated DNA base excision repair and stimulation of activity by endonuclease IV

Sung, J.S.; Biochemistry 39, 10224-10235 (2000)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
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)
Commentary
Organism
-
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
double-strand uracil-DNA glycosylase is insensitive to uracil-DNA glycosylase inhibitor protein, i.e. Ugi
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
18670
-
matrix-assisted laser desorption-ionization mass spectrometry
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Purification (Commentary)
Commentary
Organism
native and recombinant protein
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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)
Activating Compound
Commentary
Organism
Structure
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)
Commentary
Organism
-
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
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)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
18670
-
matrix-assisted laser desorption-ionization mass spectrometry
Escherichia coli
Purification (Commentary) (protein specific)
Commentary
Organism
native and recombinant protein
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
732137
Xia
Specificity and catalytic mech ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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289
18413-18426
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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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