The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: adenosine-5′-diphospho-5′-[DNA] diphosphatase
Reaction: (1) adenosine-5′-diphospho-5′-[DNA] + H2O = AMP + phospho-5′-[DNA]
(2) adenosine-5′-diphospho-5′-(ribonucleotide)-[DNA] + H2O = AMP + 5′-phospho-(ribonucleotide)-[DNA]
Other name(s): aprataxin; 5′-App5′-DNA adenylate hydrolase; APTX (gene name); HNT3 (gene name)
Systematic name: adenosine-5′-diphospho-5′-[DNA] hydrolase (adenosine 5′-phosphate-forming)
Comments: Aprataxin is a DNA-binding protein involved in different types of DNA break repair. The enzyme acts (among other activities) on abortive DNA ligation intermediates that contain an adenylate covalently linked to the 5′-phosphate DNA terminus. It also acts when the adenylate is covalently linked to the 5′-phosphate of a ribonucleotide linked to a DNA strand, which is the result of abortive ligase activty on products of EC, ribonuclease H, an enzyme that cleaves RNA-DNA hybrids on the 5′ side of the ribonucleotide found in the 5′-RNA-DNA-3′ junction. Aprataxin binds the adenylate group to a histidine residue within the active site, followed by its hydrolysis from the nucleic acid and eventual release, leaving a 5′-phosphate terminus that can be efficiently rejoined. The enzyme also possesses the activities of EC, guanosine-5′-diphospho-5′-[DNA] diphosphatase, and EC, DNA-3′-diphospho-5′-guanosine diphosphatase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Ahel, I., Rass, U., El-Khamisy, S.F., Katyal, S., Clements, P.M., McKinnon, P.J., Caldecott, K.W. and West, S.C. The neurodegenerative disease protein aprataxin resolves abortive DNA ligation intermediates. Nature 443 (2006) 713–716. [DOI] [PMID: 16964241]
2.  Tumbale, P., Williams, J.S., Schellenberg, M.J., Kunkel, T.A. and Williams, R.S. Aprataxin resolves adenylated RNA-DNA junctions to maintain genome integrity. Nature 506 (2014) 111–115. [DOI] [PMID: 24362567]
[EC created 2017 as EC, transferred 2019 to EC]

Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald