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Information on EC 3.2.1.143 - poly(ADP-ribose) glycohydrolase and Organism(s) Bos taurus and UniProt Accession O02776
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3.2.1.143 poly(ADP-ribose) glycohydrolaseSpecify your search results
Word Map
- 3.2.1.143
-
polyadp-ribose
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polyadp-ribosylation
- parp-1
- polymerase-1
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adp-ribosylation
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genotoxic
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parylation
- gallotannins
- analysis
- drug development
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parthanatos
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automodification
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adp-ribosylhydrolase
- pharmacology
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padpr
- olaparib
- molecular biology
- aif
- medicine
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADP-ribose glycohydrolase
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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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poly(adenosine diphosphoribose) glycohydrolase
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poly(adenosine diphosphoribose) glycosidase
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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-ribosyl) glycohydrolase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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?
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)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
ADP-ribose
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n greater 20, degradation proceeds in a biphasic as well as bimodal manner
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?
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
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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?
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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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2,3,4,6-pentakis-O-galloyl-beta-D-glucoside
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about 25% inhibition at 10 microM in vitro
1,3,6-tris-O-galloyl-beta-D-glucoside
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about 25% inhibition at 10 microM in vitro
2-N3-adenosine diphosphate (hydroxymethyl)pyrrolidinediol
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50% inhibition at 0.290 mM, native protein and 50% inhibition at 0.148 mM, recombinant catalytic fragment
3-galloyl-D-glucose
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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
8-chlorophenylthioadenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
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50% inhibition at 0.12 mM, recombinant catalytic fragment
8-N3-adenosine diphosphate (hydroxymethyl)pyrrolidinediol
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50% inhibition at 390 nM, native protein and 50% inhibition at 0.0014 mM, recombinant catalytic fragment
adenosine diphosphate (hydroxymethyl)pyrrolidine
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50% inhibition at 0.019 mM, native protein and 50% inhibition at 0.063 mM, recombinant catalytic fragment
adenosine diphosphate (hydroxymethyl)pyrrolidine-monoalcohol
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50% inhibition at 330nM, native protein and 50% inhibition at 440 nM, recombinant catalytic fragment
ADP-HPD
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about 40% inhibition at 1 microM, about 70% inhibition at 10 microM, about 85% inhibition at 100 microM in vitro
gallotannin
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25% inhibition at 10 micorM in vitro, reduced cell death in HeLa cells at 3 and 6 h exposure
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guanosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
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50% inhibition above 1 mM, native protein and 50% inhibition at 0.970 mM,+ recombinant catalytic fragment
methyl 2-O-galloyl-beta-D-glucoside
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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
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about 25% inhibition at 1 microM, 65% inhibition at 10 microM, about 85% inhibition at 100 microM in vitro
N6-benzyladenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
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50% inhibition above 1 mM, recombinant catalytic fragment
N6-hexyladenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
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50% inhibition at 0.51 mM, recombinant catalytic fragment
adenosine diphosphate (hydroxymethyl)pyrrolidinediol
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partial noncompetitive inhibition
adenosine diphosphate (hydroxymethyl)pyrrolidinediol
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i.e. APD-HPD, 50% inhibition at 0.0031 mM, native protein and 50% inhibition at 0.0042 mM, recombinant catalytic fragment
additional information
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gallotannin is a complex mixture of hydrolysable tannins, gallic acid and various galloyl glucose derivatives with up to 12 galloyl residues, from oak gall, that inhibits PARG
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additional information
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no inhibitory effect of 100 microM gallic acid, of 10 microM methyl gallate, of 10 microM 2,3-digalloyl-D-glucose, of 10 microM 2,3-digalloyl-O-methyl-D-glucose, of 10 microM 2,3-hexahydroxydiphenoyl-D-glucose, of 10 microM 2,3-di(3-galloyl,4,5-dihydroxy-benzoyl)-D-glucose, of 10 microM epigallocatechin gallate, and of 10 and 100 microM 3-galloyl-1,2-O-isopropylidene-alpha-D-glucose in vitro, the latter can act in vivo as cell-permeable precursor of 3-D-galloyl-D-glucose preventing poly(ADP-ribose) degradation, reduced cell death in HeLa cells at 3 and 6 h exposure (10 or 100 microM), cell death induction by methylating agent 1-methyl-3-nitro-1-nitrosoguanidine (100 microM), increased intracellular NAD content without 1-methyl-3-nitro-1-nitrosoguanidine, no effect in the presence of this agent
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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activity is less in Tris-HCl buffer than in sodium phosphate buffer or N-2-hydroxyethylpiperazine-N-ethanesulfonic acid-NaOH buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
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30°C: about 25% of maximal activity, 55°C: about 50% of maximal activity, no activity at 60°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GFP-fusion protein of enzyme, and its 74 kDA and 85 kDa apoptotic fragments
additional information
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GFP-fusion protein of enzyme, and its 74 kDA and 85 kDa apoptotic fragments
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in response to DNA damage induced by gamma-irradiation translocation of 103 kDA isoform
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induction of redistribution of enzyme and its 74 kDA and 85 kDa apoptotic fragments from cytoplasm to nucleus by leptomycin B
additional information
contains a putative bipartite nuclear location signal
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additional information
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dynamic distribution between cytoplasm and nucleoplasm and high mobility of major enzyme isoforms
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PARG_BOVIN
977
0
110837
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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enzyme N-terminal sequence is important for moduling enzyme nucleocytoplasmic trafficking properties
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E756N
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
poly(ADP-ribose) protects the enzyme from thermal inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lin, W.; Ame, J.C.; Aboul-Ela, N.; Jacobson, E.L.; Jacobson, M.K.
Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase
J. Biol. Chem.
272
11895-11901
1997
Bos taurus (O02776), Bos taurus
Brochu, G.; Shah, G.M.; Poirier, G.G.
Purification of poly(ADP-ribose) glycohydrolase detection of its isoforms by a zymogram following one- or two-dimensional electrophoresis
Anal. Biochem.
218
265-272
1994
Bos taurus
Sugimura, T.; Yamada, M.; Miwa, M.; Matsushima, T.; Hidaka, T.; Nagao, M.; Inui, N.; Takayama, S.
Properties of poly(adenosine diphosphate ribose) polymerase, poly(adenosine diphosphate ribose) glycohydrolase and poly(adenosine diphosphate ribose)
Biochem. Soc. Trans.
1
642-644
1973
Bos taurus
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Miwa, M.; Sugimura, T.
Splitting of the ribose-ribose linkage of poly(adenosine diphosphate-ribose) by a calf thymus extract
J. Biol. Chem.
246
6362-6364
1971
Bos taurus
Miwa, M.; Tanaka, M.; Matsushima, T.; Sugimura, T.
Purification and properties of a glycohydrolase from calf thymus splitting ribose-ribose linkages of poly(adenosine diphosphate ribose)
J. Biol. Chem.
249
3475-3482
1974
Bos taurus
Hatakeyama, K.; Nemoto, Y.; Ueda, K.; Hayaishi, O.
Purification and characterization of poly(ADP-ribose) glycohydrolase. Different modes of action on large and small poly(ADP-ribose)
J. Biol. Chem.
261
14902-14911
1986
Bos taurus
Slama, J.T.; Aboul-Ela, N.; Jacobson, M.K.
Mechanism of inhibition of poly(ADP-ribose) glycohydrolase by adenosine diphosphate (hydroxymethyl)pyrrolidinediol
J. Med. Chem.
38
4332-4336
1995
Bos taurus
Patel, C.N.; Koh, D.W.; Jacobson, M.K.; Oliveira, M.A.
Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain
Biochem. J.
388
493-500
2005
Bos taurus (O02776), Bos taurus
Haince, J.F.; Ouellet, M.E.; McDonald, D.; Hendzel, M.J.; Poirier, G.G.
Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during radiation-induced DNA damage
Biochim. Biophys. Acta
1763
226-237
2006
Bos taurus, Homo sapiens
Bonicalzi, M.E.; Vodenicharov, M.; Coulombe, M.; Gagne, J.P.; Poirier, G.G.
Alteration of poly(ADP-ribose) glycohydrolase nucleocytoplasmic shuttling characteristics upon cleavage by apoptotic proteases
Biol. Cell.
95
635-644
2003
Bos taurus
Koh, D.W.; Coyle, D.L.; Mehta, N.; Ramsinghani, S.; Kim, H.; Slama, J.T.; Jacobson, M.K.
SAR analysis of adenosine diphosphate (hydroxymethyl)pyrrolidinediol inhibition of poly(ADP-ribose) glycohydrolase
J. Med. Chem.
46
4322-4332
2003
Bos taurus
Formentini, L.; Arapistas, P.; Pittelli, M.; Jacomelli, M.; Pitozzi, V.; Menichetti, S.; Romani, A.; Giovannelli, L.; Moroni, F.; Chiarugi, A.
Mono-galloyl glucose derivatives are potent poly(ADP-ribose) glycohydrolase (PARG) inhibitors and partially reduce PARP-1-dependent cell death
Br. J. Pharmacol.
155
1235-1249
2008
Bos taurus
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