The Enzyme Database

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EC 3.1.11.8     
Accepted name: guanosine-5′-diphospho-5′-[DNA] diphosphatase
Reaction: guanosine-5′-diphospho-5′-[DNA] + H2O = phospho-5′-[DNA] + GMP
Other name(s): aprataxin; pp5′G5′DNA diphosphatase; pp5′G5′-DNA guanylate hydrolase; APTX (gene name); HNT3 (gene name)
Systematic name: guanosine-5′-diphospho-5′-[DNA] hydrolase (guanosine 5′-phosphate-forming)
Comments: Aprataxin is a DNA-binding protein that catalyses (among other activities) the 5′ decapping of Gpp-DNA (formed by homologs of RtcB3 from the bacterium Myxococcus xanthus). The enzyme binds the guanylate group to a histidine residue at its active site, forming a covalent enzyme-nucleotide phosphate intermediate, followed by the hydrolysis of the guanylate from the nucleic acid and eventual release. The enzyme forms a 5′-phospho terminus that can be efficiently joined by "classical" ligases. The enzyme also possesses the activitiy of EC 3.1.11.7, adenosine-5′-diphospho-5′-[DNA] diphosphatase and EC 3.1.12.2, DNA-3′-diphospho-5′-guanosine diphosphatase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Maughan, W.P. and Shuman, S. Characterization of 3′-phosphate RNA ligase paralogs RtcB1, RtcB2, and RtcB3 from Myxococcus xanthus highlights DNA and RNA 5′-phosphate capping activity of RtcB3. J. Bacteriol. 197 (2015) 3616–3624. [PMID: 26350128]
[EC 3.1.11.8 created 2017]
 
 


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