Information on EC 3.2.1.143 - poly(ADP-ribose) glycohydrolase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.2.1.143
-
RECOMMENDED NAME
GeneOntology No.
poly(ADP-ribose) glycohydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolyses poly(ADP-D-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-D-ribose
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
hydrolysis of O-glycosyl bonds
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
190209-88-2
-
253766-41-5
-
253766-42-6
-
253767-74-7
-
9068-16-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-O-acetyl-ADP-ribose + H2O
ADP-ribose + acetate
show the reaction diagram
-
rate of hydrolysis by isoform ARH3 is 250fold that observed with isoform ARH1, isoform ARH2 is inactive with this substrate
-
-
?
histone-bound poly(ADP-ribose) + H2O
ADP-ribose + ADP-ribose oligomer + ?
show the reaction diagram
-
C14-labelled poly(ADP-ribose) produced by PARP-1 (poly(ADP-ribose) polymerase) of labelled NAD+
-
-
?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
show the reaction diagram
poly(ADP-ribose) + H2O
ADP-ribose + ADP-ribose oligomer
show the reaction diagram
poly(ADP-ribose) + H2O
ADP-ribose oligomer + ADP-ribose
show the reaction diagram
poly(ADP-ribose)n + H2O
?
show the reaction diagram
poly(ADP-ribose)n + H2O
ADP-ribose
show the reaction diagram
poly(ADP-ribose)n-poly(ADP-ribose) polymerase + H2O
ADP-ribose + poly(ADP-ribose) polymerase
show the reaction diagram
-
-
-
?
poly(ADP-ribosyl)ated-Hrp38 + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
show the reaction diagram
poly(ADP-ribose)n + H2O
?
show the reaction diagram
poly(ADP-ribosyl)ated-Hrp38 + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required for hydrolysis of O-acetyl-ADP-ribose
MgCl2
10 mM, activation
Sodium phosphate
-
100 mM, slight activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(17-chloro-3b-hydroxy-androsta-5,16-diene)-succinyl-glutathione
-
-
(3Z)-5-bromo-1-(2,6-dichlorobenzyl)-3-[4-oxo-3-[2-(1H-tetrazol-5-yl)ethyl]-2-thioxo-1,3-thiazolidin-5-ylidene]-1,3-dihydro-2H-indol-2-one
-
specific detergent-insensitive inhibition
(3Z)-5-chloro-1-(2,6-dichlorobenzyl)-3-[4-oxo-3-[2-(1H-tetrazol-5-yl)ethyl]-2-thioxo-1,3-thiazolidin-5-ylidene]-1,3-dihydro-2H-indol-2-one
-
specific detergent-insensitive inhibition
1,2,3,4,6-pentakis-O-galloyl-beta-D-glucoside
-
about 25% inhibition at 10 microM in vitro
1,3,6-tris-O-galloyl-beta-D-glucoside
-
about 25% inhibition at 10 microM in vitro
1-Naphthylamine
-
1 mM, 45% inhibition
12-O-tetradecanoyl-phorbol-13-acetate
-
reduction of nuclear enzyme activity to 30-40% of control, cytosolic activity remains unchanged. Reduction is suppressed by protein kinase C inhibitor H7. Enzyme expression is reduced in presence of 12-O-tetradecanoyl-phorbol-13-acetate
2':3'-cyclic NADP+
-
-
2-(3-chloro-4-(naphthalen-2-yloxy)phenylcarbamoyl)benzoic acid
-
-
2-N3-adenosine diphosphate (hydroxymethyl)pyrrolidinediol
-
50% inhibition at 0.290 mM, native protein and 50% inhibition at 0.148 mM, recombinant catalytic fragment
2-naphthalene sulfonic acid
-
5 mM, 26% inhibition
2-Naphthylamine
-
1 mM, 50% inhibition
3,5-dichloro-2-hydroxy-N-(3-methyl-4-(naphthalen-2-yloxy)phenyl)benzamide
-
-
3,5-dichloro-2-hydroxy-N-(4-(naphthalen-2-yloxy)-3-(trifluoromethyl)phenyl)benzamide
-
-
3,5-dichloro-2-hydroxy-N-(4-(naphthalen-2-yloxy)phenyl)benzamide
-
-
3,5-dichloro-2-hydroxy-N-m-tolylbenzamide
-
between 10% and 30% inhibition at 0.5 mM
-
3,5-dichloro-2-hydroxy-N-o-tolylbenzamide
-
between 10% and 30% inhibition at 0.5 mM
-
3,5-dichloro-2-hydroxy-N-p-tolylbenzamide
-
between 10% and 30% inhibition at 0.5 mM
-
3,5-dichloro-N-(2-chlorophenyl)-2-hydroxybenzamide
-
between 10% and 30% inhibition at 0.5 mM
-
3,5-dichloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxy-N-methylbenzamide
-
-
3,5-dichloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
-
-
3,5-dichloro-N-(3-chloro-4-(p-tolyloxy)phenyl)-2-hydroxybenzamide
-
-
3,5-dichloro-N-(3-chloro-4-phenoxyphenyl)-2-hydroxybenzamide
-
-
3,5-dichloro-N-(3-chlorophenyl)-2-hydroxybenzamide
-
-
3,5-dichloro-N-(3-fluoro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
-
-
3,5-dichloro-N-(4-chlorophenyl)-2-hydroxybenzamide
-
-
3,5-dichloro-N-[3-chloro-4-(naphthalen-2-yloxy)phenyl]-2-hydroxybenzamide
-
-
3-bromo-5-chloro-N-[5-chloro-2-[(1-chloronaphthalen-2-yl)oxy]phenyl]-2-hydroxybenzamide
-
-
3-bromo-N-[2-[2-bromo-6-methyl-3-(propan-2-yl)phenoxy]-5-chlorophenyl]-5-chloro-2-hydroxybenzamide
-
-
3-chloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
-
-
3-galloyl-D-glucose
-
about 50% inhibition at 1 microM, 65% inhibition at 10 microM, about 85% at 100 microM in vitro, no inhibitory effect in HeLa cell death at 10 microM, induced by methylating agent 1-methyl-3-nitro-1-nitrosoguanidine (100 microM), because cell-permeability is probably hindered
3-[(5Z)-5-[1-(2-chlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
specific detergent-insensitive inhibition
3-[(5Z)-5-[5-bromo-1-(2,6-dichlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
specific detergent-insensitive inhibition
3-[(5Z)-5-[5-bromo-1-(2-chloro-6-fluorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
specific detergent-insensitive inhibition
3-[(5Z)-5-[5-chloro-1-(2,6-dichlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
specific detergent-insensitive inhibition
4-amino-3-hydroxynaphthalene 1-sulfonic acid
-
5 m, 79% inhibition
5-chloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
-
-
6,9-diamino-2-ethoxyacridine lactate
-
-
8-bromoadenosine 3',5'-monophosphate
-
5 mM, 13% inhibition
8-chlorophenylthioadenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
-
50% inhibition at 0.12 mM, recombinant catalytic fragment
8-methylaminoadenosine 3',5'-monophosphate
-
5 mM, 14% inhibition
8-n-octyl-amino-adenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
-
binding structure with mutant enzyme K616A/Q617A/K618A/E688A/K689A/K690A
8-N3-adenosine diphosphate (hydroxymethyl)pyrrolidinediol
-
50% inhibition at 390 nM, native protein and 50% inhibition at 0.0014 mM, recombinant catalytic fragment
acetone
-
20%, 95% inhibition
adenine(5'-9)ribofuranoside
-
5 mM, 24% inhibition
-
adenosine 3':5'-cyclic monophosphate
adenosine 5'-carboxylic acid
-
5 mM, 26% inhibition
adenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
-
ADP-HPD, binding structure with mutant enzyme K616A/Q617A/K618A/E688A/K689A/K690A
-
adenosine 5'-diphosphate-(hydroxymethyl)-pyrrolidinediol
ADP-HPD, an analogue of ADP-ribose
adenosine cyclic 2':3'-monophosphate
adenosine diphosphate (hydroxymethyl) pyrrolidinediol
adenosine diphosphate (hydroxymethyl)-pyrrolidinediol
adenosine diphosphate (hydroxymethyl)pyrrolidine
-
50% inhibition at 0.019 mM, native protein and 50% inhibition at 0.063 mM, recombinant catalytic fragment
adenosine diphosphate (hydroxymethyl)pyrrolidine-monoalcohol
-
50% inhibition at 330nM, native protein and 50% inhibition at 440 nM, recombinant catalytic fragment
adenosine diphosphate (hydroxymethyl)pyrrolidinediol
ADP-(hydroxymethyl)pyrrolidinediol
-
-
ADP-HPD
-
about 40% inhibition at 1 microM, about 70% inhibition at 10 microM, about 85% inhibition at 100 microM in vitro
ADP-ribose
Ahx
-
50% inhibition at 0.001 mM, recombinant catalytic fragment
CaCl2
Congo red
-
detergent-sensitive inhibition with complete loss of inhibition in the presence of detergent
cyclic dAMP
-
5 mM, 34% inhibition
eosin Y
-
-
eosine Y
-
-
ethacridine
-
-
-
ethanol
-
20%, 91% inhibition
F3Ahx
-
50% inhibition at 0.57 mM, recombinant catalytic fragment
gallic acid
-
0.1 mg/ml, 9% inhibition
gallotannin
-
galloylgallic acid
-
0.1 mg/ml, 11% inhibition
glucuronic acid
-
0.1 mg/ml, 14% inhibition
GPI 16552
-
pharmacological inhibitor, treatment of wild-type mice shows a protective effect in dinitrobenzene sulfonic acid-induced colitis
GPI 18214
-
pharmacological inhibitor, treatment of wild-type mice shows a protective effect in dinitrobenzene sulfonic acid-induced colitis
-
guanosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
-
50% inhibition above 1 mM, native protein and 50% inhibition at 0.970 mM,+ recombinant catalytic fragment
guanosine cyclic 3':5'-monophosphate
HgCl2
-
-
histone
methyl 2-O-galloyl-beta-D-glucoside
-
about 25% inhibition at 1 microM, 65% inhibition at 10 microM, about 85% inhibition at 100 microM in vitro
methyl 3-O-galloyl-beta-D-glucoside
-
about 25% inhibition at 1 microM, 65% inhibition at 10 microM, about 85% inhibition at 100 microM in vitro
MgCl2
-
10 mM, 18% inhibition
N'',N'''-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]carbonohydrazide
-
-
N'',N'''-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]carbonohydrazide
-
-
N'1,N'3-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]propanedihydrazide
-
-
N'1,N'3-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]propanedihydrazide
-
-
N'1,N'4-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]butanedihydrazide
-
-
N'1,N'4-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]butanedihydrazide
-
-
N'1,N'4-bis[(E)-(3,4-dihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
slight inhibition
N'1,N'5-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]pentanedihydrazide
-
-
N'1,N'5-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]pentanedihydrazide
-
-
N'1-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-N'3-[(Z)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
-
-
N'1-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-N'4-[(Z)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
-
N'1-[(E)-(2,3-dihydroxyphenyl)methylidene]-N'3-[(Z)-(2,3-dihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
-
-
N'1-[(E)-(2,4,6-trihydroxyphenyl)methylidene]-N'3-[(Z)-(2,4,6-trihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
-
-
N'1-[(E)-(2,4,6-trihydroxyphenyl)methylidene]-N'4-[(Z)-(2,4,6-trihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
-
N'1-[(E)-(2,4-dihydroxyphenyl)methylidene]-N'3-[(Z)-(2,4-dihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
-
-
N'1-[(E)-(3,4,5-trihydroxyphenyl)methylidene]-N'3-[(Z)-(3,4,5-trihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
-
-
N'1-[(E)-(3,4,5-trihydroxyphenyl)methylidene]-N'4-[(Z)-(3,4,5-trihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
-
N'1-[(E)-(3,4-dihydroxyphenyl)methylidene]-N'3-[(Z)-(3,4-dihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
-
-
N'1-[(E)-(4,6-dihydroxycyclohexa-1,3-dien-1-yl)methylidene]-N'4-[(E)-(2,4-dihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
slight inhibition
N'1-[(E)-(5,6-dihydroxycyclohexa-1,3-dien-1-yl)methylidene]-N'4-[(E)-(2,3-dihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
slight inhibition
N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
-
-
N-bis-(3-phenyl-propyl)9-oxo-fluorene-2,7-diamide
-
i.e. GPI 16552, pharmacological inhibitor. Enzyme inhibition results in significant reduction of spinal cord inflammation and tissue injury, neutrophil infiltration, cytokine production, and apoptosis upon spinal cord injury. Additionally, inhibition significantly ameliorates the recovery of limb function
N-bis-(3-phenylpropyl)-9-oxofluorene-2,7-diamide
-
GPI 16552
N-[4-[(3-bromonaphthalen-2-yl)oxy]-3-chlorophenyl]-3,5-dichloro-2-hydroxybenzamide
-
-
N1-naphthylethanenediamine
-
5 mM, 70% inhibition
N6,O2'-dibutyryl adenosine cyclic 3':5'-monophosphate
-
10 mM, 11% inhibition
N6-benzyladenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
-
50% inhibition above 1 mM, recombinant catalytic fragment
N6-hexyladenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
-
50% inhibition at 0.51 mM, recombinant catalytic fragment
N6-monobutyryl adenosine cyclic 3':5'-monophosphate
-
10 mM, 50% inhibition
naphthylamine
-
-
nobotanin B
-
inhibition of enzyme activity. In presence of inhibitor, reduction of cell death after exposure to hydrogen peroxide, N-methyl-D-aspartate, or N-methyl-N-nitro-N-nitrosoguanidine
nuclear matrix proteins
-
due to non-covalent interactions of the protein with free ADP-ribose polymers
-
p-chloromercuribenzenesulfonate
phloxine B
phosphorodiamidate morpholino oligonucleotide
-
antisense phosphorodiamidate morpholino oligonucleotide blocks exon 1 of the full length nuclear PARG 111 kDa isoform, slowing down the rate of nuclear poly(ADP-ribose) degradation, attenuating poly(ADP-ribose) polymerase-1 mediated cell death, reducing PARG expression as shown by immunostaining, upon incubation with 50 microM alcylating agent N-methyl-N'-nitro-N'-nitrosoguanidine to induce cell death blocking of nuclear PARG reduced cell condensation and cell death, no inhibitory influence on cytosol PARG
-
Poly(A)
poly(etheno ADP-ribose)
-
inhibits hydrolysis of ribose-ribose bonds by the enzyme, highly resistant to digestion by the enzyme
Poly(G)
-
inhibitory effect is eliminated when 250 mM KCl is present in the reaction mixture
poly(I)
poly(L-Arg)
-
-
poly(L-Lys)
poly(L-Orn)
-
-
-
polyvinylsulfate
-
-
protamine
RBPI-3
a rhodanine-containing mammalian PARG inhibitor, enzyme-inhibitor structure analysis, overview. RBPI-3 binds predominantly via a pi-pi stacking interaction with Tyr296 and the conserved Phe398. To accommodate the binding of RBPI-3, Phe398 moves into the adenosine binding pocket. The RBPI-3 carboxyl moiety occupies a region corresponding to the ADP-ribose alpha-phosphate group and H-bonds to main chain atoms of Lys365 and Gln254. The RBPI-3 di-chlorobenzyl moiety extends into the solvent and is disordered
RNA
-
calf liver RNA
salicylanilides
-
-
-
sanguinin H-6
-
about 50% inhibition at 10 microM in vitro
SDS
-
0.01%, 96% inhibition
siRNA
-
small interfering RNA, down regulation of PARG to 50% 24 h after siRNA transfection, maximum of 84% inhibition after 72 compared to negative control with ineffective scrambled siRNA, siRNA produced in vitro from cDNA with 21-nucleotide sequence target in human coding region of the enzyme
-
Tannic acid
-
continous decrease in activity of nuclear enzyme activity, reduction in enzyme expression
tannin
-
0.01 mg/ml, 89% inhibition, competitive with respect to poly(ADP-ribose)
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-methyl-3-nitro-1-nitrosoguanidine
-
-
-
2-mercaptoethanol
adenosine 5'-tetraphosphate
-
5 mM, slight activation
ADP
-
5 mM, slight activation
ADP-glucose
-
5 mM, slight activation
AMP
-
5 mM, slight activation
ATP
-
5 mM, slight activation
dithiothreitol
NADH
-
5 mM, slight activation
NADP+
-
5 mM, slight activation
NADPH
-
5 mM, slight activation
P1,P5-di(adenosine-5')pentaphosphate
-
5 mM, slight activation
additional information
the N-terminal regulatory fragment can activate in trans the inactive enzyme fragment depleted with this segment. This suggests that, whereas the enzyme activity can be inhibited by disrupting the docking of this segment to its enzyme binding groove (via posttranslational modification or protein-proteins interactions), the enzyme can be reversibly activated once the disruptive factor is removed
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0054 - 0.0058
(ADP-ribose)15
0.00058 - 0.0066
(ADP-ribose)n
0.0003 - 0.009
Poly(ADP-ribose)
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
90
Poly(ADP-ribose)
Bos taurus
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
2-Naphthylamine
-
-
0.3
adenosine 3':5'-cyclic monophosphate
-
-
1.1
ADP-ribose
-
-
1.5
CaCl2
-
-
10
N6-monobutyryl adenosine cyclic 3':5'-monophosphate
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0045
(3Z)-5-bromo-1-(2,6-dichlorobenzyl)-3-[4-oxo-3-[2-(1H-tetrazol-5-yl)ethyl]-2-thioxo-1,3-thiazolidin-5-ylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH not specified in the publication, 37C
0.0123
(3Z)-5-chloro-1-(2,6-dichlorobenzyl)-3-[4-oxo-3-[2-(1H-tetrazol-5-yl)ethyl]-2-thioxo-1,3-thiazolidin-5-ylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH not specified in the publication, 37C
0.072
2-(3-chloro-4-(naphthalen-2-yloxy)phenylcarbamoyl)benzoic acid
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.025
3,5-dichloro-2-hydroxy-N-(3-methyl-4-(naphthalen-2-yloxy)phenyl)benzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.021
3,5-dichloro-2-hydroxy-N-(4-(naphthalen-2-yloxy)-3-(trifluoromethyl)phenyl)benzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.042
3,5-dichloro-2-hydroxy-N-(4-(naphthalen-2-yloxy)phenyl)benzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.14
3,5-dichloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxy-N-methylbenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.012
3,5-dichloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.026
3,5-dichloro-N-(3-chloro-4-(p-tolyloxy)phenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.061
3,5-dichloro-N-(3-chloro-4-phenoxyphenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.261
3,5-dichloro-N-(3-chlorophenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.027
3,5-dichloro-N-(3-fluoro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.5
3,5-dichloro-N-(4-chlorophenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.012
3,5-dichloro-N-[3-chloro-4-(naphthalen-2-yloxy)phenyl]-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.022
3-bromo-5-chloro-N-[5-chloro-2-[(1-chloronaphthalen-2-yl)oxy]phenyl]-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.026
3-bromo-N-[2-[2-bromo-6-methyl-3-(propan-2-yl)phenoxy]-5-chlorophenyl]-5-chloro-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.061
3-chloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.95
3-galloyl-D-glucose
Bos taurus
-
enzyme for 240 min at 37°C
0.0465
3-[(5Z)-5-[1-(2-chlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH not specified in the publication, 37C
0.0029
3-[(5Z)-5-[5-bromo-1-(2,6-dichlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH not specified in the publication, 37C
0.003
3-[(5Z)-5-[5-bromo-1-(2-chloro-6-fluorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH not specified in the publication, 37C
0.0058
3-[(5Z)-5-[5-chloro-1-(2,6-dichlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH not specified in the publication, 37C
0.117
5-chloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.0163
8-n-octyl-amino-adenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
Homo sapiens
-
with wild-type enzyme, pH 7.0, 25C
0.0011 - 0.0031
adenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
-
0.00012
adenosine 5'-diphosphate-(hydroxymethyl)-pyrrolidinediol
Mus musculus
O88622
pH and temperature not specified in the publication
0.0001
adenosine diphosphate (hydroxymethyl) pyrrolidinediol
Rattus norvegicus
-
pH 7.5, 37C
0.00066
adenosine diphosphate (hydroxymethyl)pyrrolidinediol
Bos taurus
-
37C
0.00012
ADP-(hydroxymethyl)pyrrolidinediol
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
3.2
ADP-HPD
Bos taurus
-
enzyme for 240 min at 37°C
0.0019
eosine Y
Bos taurus
-
37C
7.2
methyl 2-O-galloyl-beta-D-glucoside
Bos taurus
-
enzyme for 240 min at 37°C
7.1
methyl 3-O-galloyl-beta-D-glucoside
Bos taurus
-
enzyme for 240 min at 37°C
0.0031
N'',N'''-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]carbonohydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.0028
N'',N'''-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]carbonohydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.0016
N'1,N'3-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]propanedihydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.0154
N'1,N'3-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]propanedihydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.0098
N'1,N'4-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]butanedihydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.0082
N'1,N'4-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]butanedihydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.0139
N'1,N'5-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]pentanedihydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.0274
N'1,N'5-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]pentanedihydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.0031
N'1-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-N'3-[(Z)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.001
N'1-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-N'4-[(Z)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.0148
N'1-[(E)-(2,3-dihydroxyphenyl)methylidene]-N'3-[(Z)-(2,3-dihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.0188
N'1-[(E)-(2,4,6-trihydroxyphenyl)methylidene]-N'3-[(Z)-(2,4,6-trihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.0099
N'1-[(E)-(2,4,6-trihydroxyphenyl)methylidene]-N'4-[(Z)-(2,4,6-trihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.0401
N'1-[(E)-(2,4-dihydroxyphenyl)methylidene]-N'3-[(Z)-(2,4-dihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.0032
N'1-[(E)-(3,4,5-trihydroxyphenyl)methylidene]-N'3-[(Z)-(3,4,5-trihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.0021
N'1-[(E)-(3,4,5-trihydroxyphenyl)methylidene]-N'4-[(Z)-(3,4,5-trihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.0192
N'1-[(E)-(3,4-dihydroxyphenyl)methylidene]-N'3-[(Z)-(3,4-dihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37C
0.5
N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.08
N-[4-[(3-bromonaphthalen-2-yl)oxy]-3-chlorophenyl]-3,5-dichloro-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37C
0.005
phloxine B
Bos taurus
-
37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00102
-
full length enzyme PARG111, pH and temperature not specified in the publication
0.182
-
-
13.4
-
poly(ADP-ribose) glycohydrolase II
13.8
-
-
32.1
-
-
35.6
-
purified recombinant catalytic enzyme domain, at pH 7.2, 37C
69.95
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 7
-
-
7 - 7.5
-
-
7.2
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
-
pH 6.0: about 50% of maximal activity, pH 8.5: about 35% of maximal activity
6 - 9
-
the enzyme is active between pH 6 and 9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
-
30C: about 25% of maximal activity, 55C: about 50% of maximal activity, no activity at 60C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
high abundance
Manually annotated by BRENDA team
-
embryonic stem cell
Manually annotated by BRENDA team
the enzyme is expressed in a life stage-dependant manner
Manually annotated by BRENDA team
-
differentiating rat germinal cell, presence of both enzyme isoforms of 60 kDa and 110 kDa
Manually annotated by BRENDA team
-
primary culture, highest ratio of nuclear to cytoplasmic enzyme activity
Manually annotated by BRENDA team
predominant expression in nerve cells of head and tail; predominant expression in nerve cells of head and tail
Manually annotated by BRENDA team
-
promyelocytic leukemia cell line
Manually annotated by BRENDA team
predominant expression in nerve cells of head and tail; predominant expression in nerve cells of head and tail
Manually annotated by BRENDA team
high abundance
Manually annotated by BRENDA team
high abundance
Manually annotated by BRENDA team
predominant expression in nerve cells of head and tail; predominant expression in nerve cells of head and tail
Manually annotated by BRENDA team
additional information
present in all tissues tested
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
during mitosis
Manually annotated by BRENDA team
-
GFP-fusion protein of enzyme, and its 74 kDA and 85 kDa apoptotic fragments
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / Henssen B9)
Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / Henssen B9)
Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / Henssen B9)
Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / Henssen B9)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
-
gel filtration
51000
-
gel filtration
53000
-
sucrose density gradient centrifugation
55000
x * 55000, SDS-PAGE of His-tagged protein
56000
-
gel filtration
57000
-
poly(ADP-ribose) glycohydrolase II, gel filtration
58000
-
1 * 58000, SDS-PAGE
59500
-
1 * 59500, poly(ADP-ribose) glycohydrolase II, SDS-PAGE
60000
-
x * 60000, poly(ADP-ribose) glycohydrolase G1, G2 and G3, SDS-PAGE
72000
-
gel filtration
74000
-
x * 74000, poly(ADP-ribose) glycohydrolase G4, SDS-PAGE
75500
-
1 * 75500, SDS-PAGE
90000
-
x * 90000, purified recombinant catalytic enzyme domain, SDS-PAGE
91256
x * 91256, calculated for His-tagged protein, x * 138000, SDS-PAGE of His-tagged protein, enzyme behaves abnormally in SDS-PAGE
100000
-
x * 100000, SDS-PAGE
103000
-
x * 110000, and x * 103000, SDS-PAGE
110000
-
x * 110000, and x * 103000, SDS-PAGE
138000
x * 91256, calculated for His-tagged protein, x * 138000, SDS-PAGE of His-tagged protein, enzyme behaves abnormally in SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
PARG59 expression constructs with amino acids encoded by exon 4 at the N-terminus are targeted to the mitochondria. Deletion and missense mutants allow identification of a canonical N-terminal mitochondrial targeting sequence consisting of the first 16 amino acids encoded by PARG exon 4. Sub-mitochondrial localization experiments indicate that this mitochondrial PARG isoform is targeted to the mitochondrial matrix
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant mutant K616A/Q617A/K618A/E688A/K689A/K690A, also in selenomethionine-labeld form, in complex with inhibitors, sitting drop vapour diffusion, mixing protein in SEC buffer at 7.5 mg/mL with a precipitant consisting of 28% PEG 3350, 0.2 M magnesium chloride, 0.1 M PCTP (0.04 M sodium propionate, 0.02 M sodium cacodylate, 0.04 M Bis-Tris propane), pH 7.5, in a 1:1 ratio to give a 0.004 ml drop, 20C, X-ray diffraction structure determination and analysis at 1.75-1.83 A resolution, molecular replacement
-
enzyme catalytic domain free or in complexes with ADP-ribose and inhibitor ADP-HPD, as well as four enzyme catalytic residues mutants, X-ray diffraction structure determination and analysis
purified truncated native and selenomethionine-labeled enzymes comprising residues 385-972 and lacking the A-domain, free or in complex with adenosine diphosphate (hydroxymethyl) pyrrolidinediol, hanging drop vapour diffusion method, mixing of 15 mg/ml protein in 25 mM HEPES, pH 7.5, 150 mM NaCl, 5% glycerol and 2 mM DTT, with an equal volume of well solution containing 16-20% w/v PEG 2000 monomethylether, 0.1 M Tris-HCl, pH 7.5, 0.1 M NaCl, and 0.2 M potassium thiocyanate, 22C, X-ray diffraction structure determination and analysis at 1.95 A resolution
purified recombinant His-tagged enzyme in complex with ADP-ribose or inhibitor RBPI-3, and as selenomethionine-labeled enzyme, sitting drop vapour diffusion method, 15 mg/ml protein is mixed with a 1:1 molar ratio with ADP-ribose, and with an equal volume of a solution containing 0.15 M potassium thiocyanate, 0.1 M Tris, pH 8.5, and 15% PEG 6000, or with 0.2 M potassium bromide, 0.1 M Tris, pH 7.5, and 15% PEG 4000, X-ray diffraction structure determination and analysis at 1.95 A resolution
in complexes with ADP-ribose and inhibitor adenosine 5'-diphosphate (hydroxymethyl) pyrrolidinediol
-
reaction mechanism modelling on crystal structure PDB ID 3SIG
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
37C, 10 min, stable
208525
6 - 9
-
optimal stability
208517
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
10 min, stable
45
-
10 min, about 10% loss of activity
50
-
10 min, complete inactivation
additional information
-
poly(ADP-ribose) protects the enzyme from thermal inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
poly(ADP-ribose) protects the enzyme from thermal inactivation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, retains 90-100% of its activity for at least 1.5 years
-
-20C, stable for at least 6 months
-
-80C, stable for 3 months
-
4C, 20% loss of activity after 1 month, addition of 0.1 mg/ml bovine serum albumin or 0.1 M NaCl to the diluted enzyme solution stabilizes the enzyme activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 poly(ADP-ribose) glycohydrolase isoforms: G1, G2, G3, G4
-
cytoplasmic enzyme
-
Ni-NTA column chromatography
-
poly(ADP-ribose) glycohydrolase II
-
recombinant His-tagged wild-type and selenomethionine-labeled enzymes from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and gel filtration
recombinant His6-tagged truncated enzyme, native and selenomethionine-labeled, from Escherichia coli strain BL21 by nickel affinity and heparin affinity chromatography, and gel filtration
recombinant N-terminally, TEV protease-cleavable His6-tagged wild-type and mutant enzymes, and selenomethionine-labeled enzyme from Escherichia coli strains BL21 (DE3) GOLD and B834 (DE3) by nickel affinity chromatography and gel filtration
-
Talon immobilized metal affinity resin column chromatography and glutathione-Sepharose column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli K12 TB1 and Rosetta ells
-
expression as glutathione S-transferase fusion protein
-
expression in Escherichia coli
expression in Escherichia coli as His-tagged protein; expression in Escherichia coli as His-tagged protein
expression in HeLa cell
expression of His-tagged wild-type and mutant enzymes and selenomethionine-labeled enzyme in Escherichia coli strain BL21 (DE3) GOLD
-
expression of isoform PARG59 in HeLa cell
-
fusion to enhanced green fluorescent protein and expression in Drosophila melanogaster
-
phylogenetic analysis, expression of wild-type and selenomethionin-labeled enzymes in Escherichia coli strain Rosetta (DE3)
recombinant expression of His6-tagged truncated enzyme comprising residues 385-972 in Escherichia coli strain BL21 co-expressing GroESL chaperone
the catalytic domain is expressed in Escherichia coli Rosetta2 (DE3) cells as a fusion protein with a glutathione S-transferase tag at the N-terminus and a hexahistidine tag at the C-terminus
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D738N
no enzymic activity, no structural effect of mutation
E708N
119% of wild-type activity, no structural effect of mutation
E728N
18% of wild-type activity, no structural effect of mutation
E756N
29% of wild-type activity; no enzymic activity, no structural effect of mutation
E756N/E757N |
no enzymic activity
E757N
no enzymic activity, no structural effect of mutation
E774N
61% of wild-type activity
E780N
57% of wild-type activity
E788N
100% of wild-type activity
D253N
decrease in catalytic activity
D536N
loss of catalytic activity
E271N
complete loss of catalytic activity
E272N
complete loss of catalytic activity
E554N
decrease in catalytic activity
E555N
loss of catalytic activity
Y311A
almost complete loss of catalytic activity
Y594A
decrease in catalytic activity
A874W
-
the mutant shows about 45% activity compared to the wild type enzyme
D77N/D78N
-
mutation abolishes the hydrolytic activity on O-acetyl-ADP-ribose
E688A
-
site-directed mutagenesis, a surface entropy reduction mutation
E755A
-
inactive
E756A
-
inactive
F875A
-
the mutant shows about 1% activity compared to the wild type enzyme
K616A
-
site-directed mutagenesis, a surface entropy reduction mutation
K616A/Q617A/K618A/E688A/K689A/K690A
-
site-directed mutagenesis, six surface entropy reduction mutations
K618A
-
site-directed mutagenesis, a surface entropy reduction mutation
K689A
-
site-directed mutagenesis, a surface entropy reduction mutation
K690A
-
site-directed mutagenesis, a surface entropy reduction mutation
L11D
-
the mutation increases enzyme activity to 148%
L11D/L13D
-
the mutant almost entirely abolishes enzyme activity (4% activity)
L11D/L13D/L14D
-
the mutant results in no detectable activity (less than 0.1% activity)
N740A
-
the mutant shows about 30% activity compared to the wild type enzyme
Q617A
-
site-directed mutagenesis, a surface entropy reduction mutation
R10A
-
the mutation results in a significant increase in activity (144%)
R2A/R3A/R6A/R10A
-
the mutant shows 113% enzyme activity
R3A
-
the mutant shows 105% enzyme activity
R6A
-
the mutation results in a significant increase in activity (248%)
D77N/D78N
no enzymic activity, binding of ADP-ribose is similar to wild-type
E238Q/E239Q
catalytic activity similar to wild-type
E261Q/E262Q
catalytic activity similar to wild-type
E748N
site-directed mutagenesis, the mutant is inactive, activity is disrupted due to significant conformational changes
E748Q
site-directed mutagenesis, the mutant activity is highly reduced compared to the wild-type enzyme
E749N
site-directed mutagenesis, the mutant is inactive, activity is disrupted due to significant conformational changes
E749Q
site-directed mutagenesis, the mutant activity is highly reduced compared to the wild-type enzyme
F868A
site-directed mutagenesis, the mutant activity is reduced compared to the wild-type enzyme
G737A/G738A
site-directed mutagenesis, the mutant activity is reduced compared to the wild-type enzyme
G866A
site-directed mutagenesis, the mutant activity is reduced compared to the wild-type enzyme
E114A
-
the mutant shows about 2% activity compared to the wild type enzyme
E115A
-
inactive
F227A
-
inactive
S298K
-
the mutant shows about 2% activity compared to the wild type enzyme
V226W
-
the mutant shows about 5% activity compared to the wild type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
non-radioactive and quantitative assay system for PARG activity based on dot-blot assay using anti-poly(ADP-ribose) and nitrocellulose membrane. The maximum velocity Vmax and the Michaelis constant Km of PARG reaction according to this method are 4.46 microM and 128.33 micromol/min/mg, respectively
drug development
medicine
pharmacology
the enzyme is a promising therapeutic target for the treatment of Chagas' disease