| EC |
3.2.2.28 |
| Accepted name: |
double-stranded uracil-DNA glycosylase |
| Reaction: |
Specifically hydrolyses mismatched double-stranded DNA and polynucleotides, releasing free uracil |
| Other name(s): |
Mug; double-strand uracil-DNA glycosylase; Dug; dsUDG; double-stranded DNA specific UDG; dsDNA specific UDG; UdgB (ambiguous); G:T/U mismatch-specific DNA glycosylase; UDG (ambiguous) |
| Systematic name: |
uracil-double-stranded DNA deoxyribohydrolase (uracil-releasing) |
| Comments: |
No activity on DNA containing a T/G mispair or single-stranded DNA containing either a site-specific uracil or 3,N4-ethenocytosine residue [2], significant role for double-stranded uracil-DNA glycosylase in mutation avoidance in non-dividing E. coli [3]. Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. Uracil-DNA glycosylase (EC 3.2.2.27) and EC 3.2.2.28 form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolysing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalysing the removal of mis-incorporated uracil from DNA. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Barrett, T.E., Scharer, O.D., Savva, R., Brown, T., Jiricny, J., Verdine, G.L. and Pearl, L.H. Crystal structure of a thwarted mismatch glycosylase DNA repair complex. EMBO J. 18 (1999) 6599–6609. [DOI] [PMID: 10581234] |
| 2. |
Sung, J.S. and 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. Biochemistry 39 (2000) 10224–10235. [DOI] [PMID: 10956012] |
| 3. |
Mokkapati, S.K., Fernandez de Henestrosa, A.R. and Bhagwat, A.S. Escherichia coli DNA glycosylase Mug: a growth-regulated enzyme required for mutation avoidance in stationary-phase cells. Mol. Microbiol. 41 (2001) 1101–1111. [DOI] [PMID: 11555290] |
|
| [EC 3.2.2.28 created 2009] |
| |
|
| |
|
Printable version