Information on EC 3.1.11.8 - guanosine-5'-diphospho-5'-[DNA] diphosphatase

for references in articles please use BRENDA:EC3.1.11.8
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.11.8
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RECOMMENDED NAME
GeneOntology No.
guanosine-5'-diphospho-5'-[DNA] diphosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
guanosine-5'-diphospho-5'-[DNA] + H2O = phospho-5'-[DNA] + GMP
show the reaction diagram
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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 3.1.11.7, adenosine-5'-diphospho-5'-[DNA] diphosphatase and EC 3.1.12.2, DNA-3'-diphospho-5'-guanosine diphosphatase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Gppp-BODIPY + H2O
?
show the reaction diagram
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?
guanosine-5'-diphospho-5'-[DNA] + H2O
phospho-5'-[DNA] + GMP
show the reaction diagram
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0131
Gppp-BODIPY
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pH 7.2, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004
Gppp-BODIPY
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pH 7.2, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.031
Gppp-BODIPY
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pH 7.2, 22°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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aprataxin is ubiquitously expressed
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
of the two splicing variants of APTX mRNA, the short and the long forms, long-form APTX mRNA is the major isoform
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
689insT
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recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
840delT
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recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
A198V
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recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
D267G
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recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
H260A
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recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
K197Q
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recessive mutation associated with ataxia but not oculomotor apraxia, mild presentation allele
P206L
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recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
R199H
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recessive mutation associated with ataxia and oculomotor apraxia, protein retains substantial function, consistent with altered activity
T739C
FLJ20157
homozygous mutation idientified in a patient with ataxia-oculomotor apraxia type 1
V263G
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recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
W279R
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recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
W279X
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recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine