BRENDA - Reference to 3.2.2.28; Id = 690873

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

-

Escherichia coli

additional information

double-strand uracil-DNA glycosylase is insensitive to uracil-DNA glycosylase inhibitor protein, i.e. Ugi

Escherichia coli

18670

-

matrix-assisted laser desorption-ionization mass spectrometry

Escherichia coli

-

native and recombinant protein

Escherichia coli

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

-

?

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

-

Escherichia coli

additional information

double-strand uracil-DNA glycosylase is insensitive to uracil-DNA glycosylase inhibitor protein, i.e. Ugi

Escherichia coli

18670

-

matrix-assisted laser desorption-ionization mass spectrometry

Escherichia coli

native and recombinant protein

Escherichia coli

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

-

?

732137

Xia

Specificity and catalytic mech ...

Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579

J. Biol. Chem.

289

18413-18426

2014

-

1

-

5

-

1

-

7

-

3

-

1

-

9

-

1

-

5

-

1

-

7

-

1

-

9

-

679463

Srinath

Substrate specificities and fu ...

Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Ra / ATCC 25177

DNA Repair

6

1517-1528

2007

-

1

-

1

-

1

-

2

-

1

-

2

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

2

-

1

-

1

-

1

-

692966

O'Neill

Mismatch uracil glycosylase fr ...

Escherichia coli

J. Biol. Chem.

278

20526-20532

2003

-

1

-

1

-

4

-

1

-

4

-

694210

Mokkapati

Escherichia coli DNA glycosyla ...

Escherichia coli

Mol. Microbiol.

41

1101-1111

2001

-

1

-

1

-

1

-

1

-

2

-

1

-

1

-

1

-

2

-

690873

Sung

Mosbaugh, D.W.: Escherichia co ...

Escherichia coli

Biochemistry

39

10224-10235

2000

1

-

1

-

1

-

1

-

2

-

1

-

3

-

1

-

1

-

1

-

1

-

1

-

3

-

692063

Barrett

Crystal structure of a thwarte ...

Escherichia coli

EMBO J.

18

6599-6609

1999

-

1

-

1

-

1

-

691667

Barrett

Crystal structure of a G:T/U m ...

Escherichia coli

Cell

92

117-129

1998

-

1

-

2

-

1

-

1

-

1

-

1

-

694927

Saparbaev

3,N4-ethenocytosine, a highly ...

Escherichia coli

Proc. Natl. Acad. Sci. USA

95

8508-8513

1998

-

2

-

3

-

3

-

2

-

2

-

3

-

2

-

694330

Gallinari

A new class of uracil-DNA glyc ...

Escherichia coli

Nature

383

735-738

1996

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1

-

1

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4

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2

-

1

-

1

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2

-

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

Data extracted from this reference: