Quick Search:

uzh logo
Browse by:

Zurich Open Repository and Archive

Maintenance: Tuesday, 5.7.2016, 07:00-08:00

Maintenance work on ZORA and JDB on Tuesday, 5th July, 07h00-08h00. During this time there will be a brief unavailability for about 1 hour. Please be patient.

Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-31472

Sartori, A A; Fitz-Gibbon, S; Yang, H; Miller, J H; Jiricny, J (2002). A novel uracil-DNA glycosylase with broad substrate specificity and an unusual active site. EMBO Journal, 21(12):3182-3191.

[img] PDF - Registered users only
View at publisher


Uracil-DNA glycosylases (UDGs) catalyse the removal of uracil by flipping it out of the double helix into their binding pockets, where the glycosidic bond is hydrolysed by a water molecule activated by a polar amino acid. Interestingly, the four known UDG families differ in their active site make-up. The activating residues in UNG and SMUG enzymes are aspartates, thermostable UDGs resemble UNG-type enzymes, but carry glutamate rather than aspartate residues in their active sites, and the less active MUG/TDG enzymes contain an active site asparagine. We now describe the first member of a fifth UDG family, Pa-UDGb from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum, the active site of which lacks the polar residue that was hitherto thought to be essential for catalysis. Moreover, Pa-UDGb is the first member of the UDG family that efficiently catalyses the removal of an aberrant purine, hypoxanthine, from DNA. We postulate that this enzyme has evolved to counteract the mutagenic threat of cytosine and adenine deamination, which becomes particularly acute in organisms living at elevated temperatures.


66 citations in Web of Science®
67 citations in Scopus®
Google Scholar™



0 downloads since deposited on 09 Jul 2010
0 downloads since 12 months

Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Institute of Molecular Cancer Research
07 Faculty of Science > Institute of Molecular Cancer Research
Dewey Decimal Classification:570 Life sciences; biology
Deposited On:09 Jul 2010 14:20
Last Modified:05 Apr 2016 13:58
Publisher:Nature Publishing Group
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:10.1093/emboj/cdf309
PubMed ID:12065430

Users (please log in): suggest update or correction for this item

Repository Staff Only: item control page