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Information on EC 3.2.1.143 - poly(ADP-ribose) glycohydrolase
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EC Tree
3.2.1.143 poly(ADP-ribose) glycohydrolaseSpecify your search results
Word Map
- 3.2.1.143
-
polyadp-ribose
-
polyadp-ribosylation
- parp-1
- polymerase-1
-
adp-ribosylation
-
genotoxic
-
parylation
- gallotannins
- analysis
- drug development
-
parthanatos
-
automodification
-
adp-ribosylhydrolase
- pharmacology
-
padpr
- olaparib
- molecular biology
- aif
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
poly(adp-ribose) glycohydrolase, parg1, par glycohydrolase, poly (adp-ribose) glycohydrolase, adprhl2, poly(adp-ribose)glycohydrolase, parg110, adp-ribose glycohydrolase, adp-ribosyl-acceptor hydrolase 3, drparg, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADP-ribose glycohydrolase
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ARH3
DrPARG
FOXG_05947
Genbank AB019366-derived protein GI 6518480
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Genbank U78975-derived protein GI 2062407
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glycohydrolase, poly(adenosine diphosphoribose)
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glycohydrolase, poly(adenosine diphosphoribose) (cattle clone 4/5)
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glycohydrolase, poly(adenosine diphosphoribose) (Rattus norvegicus strain BUF gene Parg)
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PAR glycohydrolase
PARG
PARG1
poly(adenosine diphosphoribose) glycohydrolase
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poly(adenosine diphosphoribose) glycosidase
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poly(ADP-ribose) glycohydrolase
poly(ADP-ribose) glycohydrolase (Arabidopsis thaliana gene At2g31860)
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poly(ADP-ribose) glycohydrolase (Arabidopsis thaliana gene At2g31870)
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poly(ADP-ribose) glycohydrolase (cattly clone 4/5)
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poly(ADP-ribose) glycohydrolase 1
poly(ADP-ribose)glycohydrolase
poly(ADP-ribosyl) glycohydrolase
PARG
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poly(ADP-ribosyl) glycohydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
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(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
canonical enzyme catalytic mechanism, modelling, overview
(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
catalytic mechanism, modelling, overview
(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
catalytic mechanism, structure-function analysis, overview
(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
enzyme catalytic mechanism, overview
(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
Asp314 is located proximal to the 1''-O-linkage in substrates. Asp314 might protonate the leaving group (general acid), forming an oxocarbenium ion intermediate, and then activate the water (general base) for back-side attack. The W1 ligand of MgB can serve as the nucleophile attacking the anomeric C1'' of the ribose''
(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
reaction mechanism and structure, overview
(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of O-glycosyl bonds
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CAS REGISTRY NUMBER
COMMENTARY
190209-88-2
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253766-41-5
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253766-42-6
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253767-74-7
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9068-16-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-O-acetyl-ADP-ribose + H2O
ADP-ribose + acetate
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rate of hydrolysis by isoform ARH3 is 250fold that observed with isoform ARH1, isoform ARH2 is inactive with this substrate
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?
ADP-ribose dimer + H2O
2 ADP-ribose
the N-1 adenine group interacts with the amide nitrogen of the conserved Leu752 in human PARG, while the beta-phosphate forms H-bonds with the conserved Ala750, enzyme-substrate binding structure, crystal structure analysis, overview
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?
histone-bound poly(ADP-ribose) + H2O
ADP-ribose + ADP-ribose oligomer + ?
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C14-labelled poly(ADP-ribose) produced by PARP-1 (poly(ADP-ribose) polymerase) of labelled NAD+
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?
poly(ADP-ribose)n-poly(ADP-ribose) polymerase + H2O
ADP-ribose + poly(ADP-ribose) polymerase
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?
propargyl ADP-ribose dimer + H2O
propargyl ADP-ribose + ADP-ribose
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?
PARP1-XRCC1 + H2O
?
efficient disassembly of complexes of the DNA scaffold repair protein XRCC1 and the poly(ADP-ribose) polymerase 1 by poly(ADP-ribose) glycohydrolase (PARG)
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?
PARP1-XRCC1 + H2O
?
PARG rapidly reverses the PARylation of PARP1 and efficiently disassembles the PARP1-XRCC1 complex
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?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
binding structure of ADP-ribose to wild-type and mutant enzymes, overview
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?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
the activity is dependent on the conserved glutamate residues
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?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
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?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
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?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
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?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
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?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
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?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
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?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
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?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
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?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
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?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
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?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
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?
poly(ADP-ribose) + H2O
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a commercial Bt-NAD ribosylated PARP1 substrate
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?
poly(ADP-ribose) + H2O
?
commercial Bt-NAD ribosylated PARP1 substrate
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?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
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?
poly(ADP-ribose) + H2O
ADP-ribose + ADP-ribose oligomer
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tritium-labelled poly(ADP-ribose) produced by PARP-1 (poly(ADP-ribose) polymerase) with tritium-labelled NAD + sonicated DNA containing histones, and bovine albumin
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?
poly(ADP-ribose) + H2O
ADP-ribose + ADP-ribose oligomer
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P32-labelled poly(ADP-ribose) produced by PARP-1 (poly(ADP-ribose) polymerase) of labelled NAD+
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?
poly(ADP-ribose) + H2O
ADP-ribose oligomer + ADP-ribose
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?
poly(ADP-ribose)n + H2O
?
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the enzyme may regulate functionally the chain length of poly(ADP-ribose) which plays a role in DNA synthesis or in the structure of chromatin
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?
poly(ADP-ribose)n + H2O
?
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the enzyme is responsible for the catabolism of poly(ADP-ribose), the enzyme is a crucial determinant of polymer metabolism which is known to be implicated in DNA repair and other cellular processes
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?
poly(ADP-ribose)n + H2O
?
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regulates differentially the levels of large and small poly(ADP-ribose) in the cell
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?
poly(ADP-ribose)n + H2O
?
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poly(ADP-ribose) glycohydrolase II may be involved in extranuclear de(ADP-ribosyl)n-ation, but not in membrane de-mono(ADP-ribosyl)ation
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?
poly(ADP-ribose)n + H2O
ADP-ribose
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n greater 20, degradation proceeds in a biphasic as well as bimodal manner
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?
poly(ADP-ribose)n + H2O
ADP-ribose
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and lower molecular weight poly(ADP-ribose)n fragment products, no product: phosphoribosyl-AMP
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?
poly(ADP-ribose)n + H2O
ADP-ribose
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and lower molecular weight poly(ADP-ribose)n fragment products, no product: phosphoribosyl-AMP
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?
additional information
?
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several isoforms, functions in embryonic development, genotixicity, cell cycle regulation, mitotic spindle assembly, development, differentiation, and cell death
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?
additional information
?
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enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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?
additional information
?
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enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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?
additional information
?
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enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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?
additional information
?
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enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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?
additional information
?
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enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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?
additional information
?
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enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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?
additional information
?
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enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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?
additional information
?
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enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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?
additional information
?
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enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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?
additional information
?
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enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
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?
additional information
?
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poly(ADP-ribose) polymerase and poly(ADP-ribose) glycohydrolase promote chromatin silencing at least in part by regulating the localization and function of silencing protein SIR2 and possible other nuclear proteins
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?
additional information
?
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the enzyme is responsible for the cleavage of poly(ADP-D-ribose) into the single ADP-ribose unit by hydrolyzing the ribose-ribose bonds within the polymer chain
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?
additional information
?
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the enzyme cannot hydrolyze the bond between terminal ADP-ribose and glutamate residues of automodifed PARP1
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?
additional information
?
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shuttling of enzyme between nucleus and cytoplasm and proper control of poly(ADP-ribose) metabolism throughout cell cycle may be an important role in regulating cell cycle progression and centrosome duplication
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?
additional information
?
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transient decrease in nuclear enzyme activity is important for the onset of differentiation of HL-60 cells to macrophage-like cells
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?
additional information
?
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poly(ADP-ribose) glycohydrolase is a critical component of single-strand break repair and accelerates this process in concert with poly(ADP-ribose) polymerase
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?
additional information
?
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poly(ADP-ribose) glycohydrolase is the only enzyme known to catalyse hydrolysis of the O-glycosidic linkages of ADP-ribose polymers
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?
additional information
?
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poly(ADP-ribose) glycohydrolase is the only enzyme known to catalyse hydrolysis of the O-glycosidic linkages of ADP-ribose polymers
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?
additional information
?
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the enzyme can effectively process the added poly-/oligo(ADP-ribose) units from both GST-Smad3 and PARP-1, but fails to act as a mono(ADP-ribose) hydrolase, inability of the enzme to cleave the last ADP-ribose unit, which is coupled to the protein substrate
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?
additional information
?
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assay using the PARylated PARP1 substrates, poly(ADP-ribose)-linked N-terminal DNA-binding domain of PARP1, i.e. PAR polymerase 1, a nicked DNA. Poly(ADP-ribose) binding structures of wild-type and D314A mutant, overview
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?
additional information
?
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assay using the PARylated PARP1 substrates, poly(ADP-ribose)-linked N-terminal DNA-binding domain of PARP1, i.e. PAR polymerase 1, a nicked DNA. Poly(ADP-ribose) binding structures of wild-type and D314A mutant, overview
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?
additional information
?
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development of a high-throughput homogeneous time-resolved fluorescence (HTRF) assay method, 6His-TEV-PAR(32:1)PARP-1(2-1014) substrate, combinantion with the activity of poly(ADP-ribose) polymerase, PARP. Enzyme PARG binds to PARylated PARP-1 and cleaves off the PAR moiety, which activates PARP-1 preventing the production of a fluorescent signal. Inactive PARP-1 leads to the production of the measurable fluoresecnt signal, mechanism and evaluation, overview
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?
additional information
?
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development of a high-throughput homogeneous time-resolved fluorescence (HTRF) assay method, 6His-TEV-PAR(32:1)PARP-1(2-1014) substrate, combinantion with the activity of poly(ADP-ribose) polymerase, PARP. Enzyme PARG binds to PARylated PARP-1 and cleaves off the PAR moiety, which activates PARP-1 preventing the production of a fluorescent signal. Inactive PARP-1 leads to the production of the measurable fluoresecnt signal, mechanism and evaluation, overview
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?
additional information
?
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structure of poly(ADP-ribose) glycohydrolase (PARG) in complex with the poly(ADP-ribose) (PAR) substrate reveals that PARG-PAR contacts are provided almost exclusively by the macrodomain. The accessory domain (which is part of the PARG catalytic region) has only limited interaction with PAR, but it structurally supports the PARG catalytic loop and may have an important role in regulation of PARG catalytic activity. The PARG-PAR structure also reveals that PARGs preferably bind PAR at the chain termini and primarily act as exo-glycohydrolases (whereby PARG sequentially degrades terminal ADP-ribose units). While binding along the PAR chain and endo-glycohydrolytic cleavage of PAR is structurally possible, it appears to be less efficient. Due to active site constraints and the conformation of bound PAR, canonical PARGs are unlikely to efficiently bind the aforementioned putative PAR branch sites
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?
additional information
?
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synthesis of derivatives of the ADP-ribose dimer and development of a PAR Binding assay, overview. Propargyl ADP-ribose dimer binds to E756N and E755N mutants of human PARG with KD values of 83 nM and 208 nM, respectively. Fluorescent propargyl ADP-ribose dimer does not bind proteins devoid of PAR binding activity such as bovine serum albumin even at high concentrations of protein. Wild-type PARG is unable to process the truncated substrates 2'-O-alpha-D-ribofuranosyladenosine and 2'-O-(5-O-phosphono-a-D-ribofuranosyl)adenosine 5'-phosphate)
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?
additional information
?
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synthesis of derivatives of the ADP-ribose dimer and development of a PAR Binding assay, overview. Propargyl ADP-ribose dimer binds to E756N and E755N mutants of human PARG with KD values of 83 nM and 208 nM, respectively. Fluorescent propargyl ADP-ribose dimer does not bind proteins devoid of PAR binding activity such as bovine serum albumin even at high concentrations of protein. Wild-type PARG is unable to process the truncated substrates 2'-O-alpha-D-ribofuranosyladenosine and 2'-O-(5-O-phosphono-a-D-ribofuranosyl)adenosine 5'-phosphate)
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?
additional information
?
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enzyme is a necessary component of the poly(ADP-ribose) polymerase 1 mediated cell death pathway
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?
additional information
?
-
no substrate: mono-ADP-ribosylated proteins, ADP-ribose-arginine, ADP-ribose-cysteine, ADP-ribose-diphthaminde, ADP-ribose-asparagine
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-
?
additional information
?
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enzyme activity modulates the inflammatory response and tissue events associated with spinal cord trauma and participates in target organ damage under these conditions
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?
additional information
?
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modification of the adenine moiety of poly(ADP-ribose) abrogates the susceptibility to digestion by the enzyme
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-
?
additional information
?
-
the enzyme functions as an endo-glycosidase to release oligo(ADP-ribose) and as an exo-glycosidase to release ADP-ribose. Long poly(ADP-ribose) polymers are efficiently hydrolyzed by a combination of endo- and exo-glycosidic activity, whereas smaller digestion products are poor substrates for the enzyme allowing release of oligo(ADP-ribose) chains that are ligands for histones and DNA repair and damage checkpoint proteins such as XRCC1 and p53
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?
additional information
?
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quantitative, real-time assay of PAR-dependent protein-protein interactions and PAR turnover by PARG. PARG degrades the PAR posttranslational modification by a combination of exo- and endo-glycohydrolase activity, leaving a single ADP-ribose moiety attached to PARP1 that is a substrate for the mono(ADP-ribose) (MAR) hydrolases
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?
additional information
?
-
hydrolysis of glycosidic ribose-ribose bond
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-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
PARP1-XRCC1 + H2O
?
efficient disassembly of complexes of the DNA scaffold repair protein XRCC1 and the poly(ADP-ribose) polymerase 1 by poly(ADP-ribose) glycohydrolase (PARG)
-
-
?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
the activity is dependent on the conserved glutamate residues
-
-
?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
-
-
-
?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
-
-
-
?
poly(ADP-ribose)n + H2O
?
-
the enzyme may regulate functionally the chain length of poly(ADP-ribose) which plays a role in DNA synthesis or in the structure of chromatin
-
-
?
poly(ADP-ribose)n + H2O
?
-
the enzyme is responsible for the catabolism of poly(ADP-ribose), the enzyme is a crucial determinant of polymer metabolism which is known to be implicated in DNA repair and other cellular processes
-
-
?
poly(ADP-ribose)n + H2O
?
-
regulates differentially the levels of large and small poly(ADP-ribose) in the cell
-
-
?
poly(ADP-ribose)n + H2O
?
-
poly(ADP-ribose) glycohydrolase II may be involved in extranuclear de(ADP-ribosyl)n-ation, but not in membrane de-mono(ADP-ribosyl)ation
-
-
?
additional information
?
-
-
several isoforms, functions in embryonic development, genotixicity, cell cycle regulation, mitotic spindle assembly, development, differentiation, and cell death
-
-
?
additional information
?
-
-
poly(ADP-ribose) polymerase and poly(ADP-ribose) glycohydrolase promote chromatin silencing at least in part by regulating the localization and function of silencing protein SIR2 and possible other nuclear proteins
-
-
?
additional information
?
-
-
the enzyme is responsible for the cleavage of poly(ADP-D-ribose) into the single ADP-ribose unit by hydrolyzing the ribose-ribose bonds within the polymer chain
-
-
?