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Information on EC 3.6.1.72 - DNA-3'-diphospho-5'-guanosine 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 3' decapping of DNA-ppG (formed by EC 6.5.1.8, 3'-phosphate/5'-hydroxy nucleic acid ligase) . 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 its eventual release. The enzyme also possesses the activity of EC 3.6.1.71, adenosine-5'-diphospho-5'-[DNA] diphosphatase, and EC 3.6.1.70, guanosine-5'-diphospho-5'-[DNA] 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
[DNA]-3'-diphospho-5'-guanosine
+
=
[DNA]-3'-phosphate
+
Synonyms
aprataxin, APTX, DNA-3'pp5'G guanylate hydrolase, EC 3.1.12.2, HNT3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aprataxin
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APTX
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DNA-3'pp5'G guanylate hydrolase
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HNT3
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SYSTEMATIC NAME
IUBMB Comments
[DNA]-3'-diphospho-5'-guanosine hydrolase (guanosine 5'-phosphate-forming)
Aprataxin is a DNA-binding protein that catalyses (among other activities) the 3' decapping of DNA-ppG (formed by EC 6.5.1.8, 3'-phosphate/5'-hydroxy nucleic acid ligase) [1]. 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 its eventual release. The enzyme also possesses the activity of EC 3.6.1.71, adenosine-5'-diphospho-5'-[DNA] diphosphatase, and EC 3.6.1.70, guanosine-5'-diphospho-5'-[DNA] diphosphatase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[DNA]-3'-diphospho-5'-(6-O-methylguanosine) + H2O
[DNA]-3'-phosphate + 6-O-methyl-GMP
show the reaction diagram
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?
[DNA]-3'-diphospho-5'-guanosine + H2O
[DNA]-3'-phosphate + GMP
show the reaction diagram
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-
-
?
[DNA]-3'-diphospho-5'-inosine + H2O
[DNA]-3'-phosphate + IMP
show the reaction diagram
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-
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?
additional information
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aprataxin is a DNA 3'-de-capping enzyme, converting DNAppG to DNA3'p and GMP. Aprataxin hydrolyzes inosine and 6-O-methylguanosine caps, but not adeoxyguanosine cap. The enzyme also possesses the activity of EC 3.1.11.7, adenosine-5'-diphospho-5'-[DNA] diphosphatase, and EC 3.1.11.8, guanosine-5'-diphospho-5'-[DNA] diphosphatase
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[DNA]-3'-diphospho-5'-guanosine + H2O
[DNA]-3'-phosphate + GMP
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D63A
mutation impairs DNAppG decapping
His147A
mutation abolishes DNAppG decapping activity
His149A
mutation abolishes DNAppG decapping activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Das, U.; Chauleau, M.; Ordonez, H.; Shuman, S.
Impact of DNA3pp5G capping on repair reactions at DNA 3' ends
Proc. Natl. Acad. Sci. USA
111
11317-11322
2014
Schizosaccharomyces pombe (O74859), Schizosaccharomyces pombe ATCC 24843 (O74859)
Manually annotated by BRENDA team
Das, U.; Chauleau, M.; Ordonez, H.; Shuman, S.
Impact of DNA3pp5G capping on repair reactions at DNA 3 ends
Proc. Natl. Acad. Sci. USA
111
11317-11322
2014
Schizosaccharomyces pombe (O74859), Schizosaccharomyces pombe 972 (O74859)
Manually annotated by BRENDA team