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Information on EC 3.6.1.70 - guanosine-5'-diphospho-5'-[DNA] diphosphatase and Organism(s) Schizosaccharomyces pombe and UniProt Accession O74859

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IUBMB 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 3.6.1.71, adenosine-5'-diphospho-5'-[DNA] diphosphatase and EC 3.6.1.72, DNA-3'-diphospho-5'-guanosine diphosphatase.
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Schizosaccharomyces pombe
UNIPROT: O74859
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The taxonomic range for the selected organisms is: Schizosaccharomyces pombe
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
guanosine-5'-diphospho-5'-[DNA]
+
=
phospho-5'-[DNA]
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Synonyms
aprataxin, APTX, EC 3.1.11.8, HNT3, pp5'G5'-DNA guanylate hydrolase, pp5'G5'DNA diphosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aprataxin
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APTX
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HNT3
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pp5'G5'-DNA guanylate hydrolase
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pp5'G5'DNA diphosphatase
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SYSTEMATIC NAME
IUBMB Comments
guanosine-5'-diphospho-5'-[DNA] hydrolase (guanosine 5'-phosphate-forming)
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 3.6.1.71, adenosine-5'-diphospho-5'-[DNA] diphosphatase and EC 3.6.1.72, DNA-3'-diphospho-5'-guanosine diphosphatase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
guanosine-5'-diphospho-5'-[DNA] + H2O
phospho-5'-[DNA] + GMP
show the reaction diagram
substrate 12-mer Gpp-DNA strand
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additional information
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aprataxin additionally is a DNA 3'-de-capping enzyme, converting DNAppG to DNA3'p and GMP, reaction of EC 3.1.12.2. Aprataxin hydrolyzes inosine and 6-O-methylguanosine caps, but not adeoxyguanosine cap
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
3'-phosphate RNA ligase RtcB3 caps DNA and RNA 5'-PO4 ends to form GppDNA and GppRNA products, respectively. GppDNA formed by RtcB3 can be decapped to pDNA by the DNA repair enzyme aprataxin
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure in complex with GMP, to 1.5 A resolution. GMP binds at the same position and in the same anti nucleoside conformation as AMP, and aprataxin makes more extensive nucleobase contacts with guanine than with adenine, via a hydrogen bonding network to the guanine O6, N1, N2 base edge
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maughan, W.P.; 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
3616-3624
2015
Schizosaccharomyces pombe (O74859), Schizosaccharomyces pombe 972 (O74859)
Manually annotated by BRENDA team
Chauleau, M.; Jacewicz, A.; Shuman, S.
DNA3pp5G de-capping activity of aprataxin: effect of cap nucleoside analogs and structural basis for guanosine recognition
Nucleic Acids Res.
43
6075-6083
2015
Schizosaccharomyces pombe (O74859), Schizosaccharomyces pombe ATCC 24843 (O74859)
Manually annotated by BRENDA team