EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.2.2.28 | 3,N4-ethenocytosine-containing single-stranded DNA + H2O |
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 |
Escherichia coli |
3,N4-ethenocytosine + single-stranded DNA with abasic site |
- |
? |
| 3.2.2.28 | 3,N4-ethenocytosine-mismatched double-stranded DNA + H2O |
- |
Escherichia coli |
3,N4-ethenocytosine + double-stranded DNA with abasic site |
- |
? |
| 3.2.2.28 | 3,N4-ethenocytosine-mismatched double-stranded DNA + H2O |
3,N4-ethenocytosine is recognized and efficiently excised from the 3,N4-ethenocytosine/G mismatch |
Escherichia coli |
3,N4-ethenocytosine + double-stranded DNA with abasic site |
- |
? |
| 3.2.2.28 | 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 |
Escherichia coli |
3,N4-ethenocytosine + double-stranded DNA with abasic site |
- |
? |
| 3.2.2.28 | 3,N4-ethenocytosine-mismatched double-stranded DNA + H2O |
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 |
Escherichia coli |
3,N4-ethenocytosine + double-stranded DNA with abasic site |
- |
? |
| 3.2.2.28 | hypoxanthine-mismatched double-stranded DNA + H2O |
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 |
Thermus thermophilus |
hypoxanthine + double-stranded DNA with abasic site |
- |
? |
| 3.2.2.28 | hypoxanthine-mismatched double-stranded DNA + H2O |
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 |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 |
hypoxanthine + double-stranded DNA with abasic site |
- |
? |
| 3.2.2.28 | more |
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 |
Escherichia coli |
? |
- |
? |
| 3.2.2.28 | more |
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 |
Escherichia coli |
? |
- |
? |
| 3.2.2.28 | more |
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 |
Escherichia coli |
? |
- |
? |
