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2'-O-acetyl-ADP-ribose + H2O
ADP-ribose + acetate
-
-
-
-
?
2'-phospho-ADP-ribosylarginine + H2O
2'-phospho-ADP-ribose + arginine
-
-
-
?
ADP-ribose DABSYL-L-arginine methyl ester + H2O
DABSYL-L-arginine methyl ester + ADP-ribose
ADP-ribose-arginine + H2O
ADP-ribose + arginine
ADP-ribose-L-arginine + H2O
ADP-ribose + L-arginine
ADP-ribosylarginine + H2O
ADP-ribose + L-arginine
ADP-ribosylarginine methyl ester + H2O
ADP-ribose + arginine methyl ester
-
-
-
?
ADP-ribosylguanidine + H2O
ADP-ribose + guanidine
-
at pH less than 7, the enzme exhibits more activity toward ADP-ribosylguanidine than toward ADP-ribosylarginine. The ratio of activity in assays containing ADP-ribosylarginine to those with ADP-ribosylguanidine increases with pH
-
?
alpha-subunit of stimulating GTP-binding protein ADP-ribosylated + H2O
alpha-subunit of stimulating GTP-binding protein + ADP-ribose
casein ADP-ribosylated + H2O
ADP-ribose + casein
-
-
-
?
cholera toxin A1-subunit ADP-ribosylated + H2O
cholera toxin A1-subunit + ADP-ribose
histones ADP-ribosylated + H2O
?
-
-
-
-
?
lysozyme ADP-ribosylated + H2O
?
-
-
-
-
?
maltose binding protein ADP-ribosylated + H2O
maltose binding protein + ADP-ribose
-
MBP is ADP-ribosylated by an arginine-specific ADP-ribosyltransferase cholera toxin
-
?
Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + L-arginine
nonmuscle actin ADP-ribosylated + H2O
nonmuscle actin + ADP-ribose
O-acetyl-ADP-ribose + H2O
ADP-ribose + acetate
-
the reaction is catalyzed by isoform ARH3 only
-
-
?
protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + protein-L-arginine
additional information
?
-
ADP-ribose DABSYL-L-arginine methyl ester + H2O
DABSYL-L-arginine methyl ester + ADP-ribose
-
-
-
?
ADP-ribose DABSYL-L-arginine methyl ester + H2O
DABSYL-L-arginine methyl ester + ADP-ribose
-
-
-
?
ADP-ribose DABSYL-L-arginine methyl ester + H2O
DABSYL-L-arginine methyl ester + ADP-ribose
-
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
ADP-ribosylarginine hydrolase presumably regenerates an arginine site that can be ADP-ribosylated by NAD-arginine ADP-ribosyltransferase. The balance between these two opposing enzymatic activities may control some aspects of cellular metabolism
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
-
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
the presence of ADP-ribosyltransferases and ADP-ribosylhydrolases may lead to an ADP-ribosylation/de-ADP-ribosylation cycle, lending further support to the hypothesis that this covalent modification may have a regulatory function in animal cells
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
the presence of different enzymes and effectors controlling ADP-ribosylarginine synthesis and degradation is reminiscent of the protein kinase-phosphatase system
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
-
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
the presence of ecto-ADP-ribosyltransferase and arginine-specific ADP-ribosylation of cell-surface protein have been reported. Application of the method on the extracellular ADP-ribosylation of intact cells may help to reveal the role of the modification in physiological events such as cell adhesion or cell-cell communication
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
-
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
in Rhodospirillium rubrum, a nitrogen-fixing microorganism, ADP-ribosylation of an arginine residue in a nitrogenase inhibits its activity. Inactivation of the nitrogenase can be reversed by a hydrolase which cleaves the ADP-ribose-arginine bond
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
in nitrogen fixing bacteria, Rhodospirillium rubrum, ADP-ribosylation-de-ADP-ribosylation of a specific arginine-residue of dinitrogenase reductase has been shown to regulate the enzyme activity
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
the existence of a ADP-ribosylation cycle was established in the bacterium Rhodospirillium rubrum where it regulates dinitrogenase reductase, a key enzyme in nitrogen fixation
-
-
?
ADP-ribose-L-arginine + H2O
ADP-ribose + L-arginine
-
-
-
-
?
ADP-ribose-L-arginine + H2O
ADP-ribose + L-arginine
-
-
-
?
ADP-ribose-L-arginine + H2O
ADP-ribose + L-arginine
-
-
-
?
ADP-ribose-L-arginine + H2O
ADP-ribose + L-arginine
-
-
-
?
ADP-ribose-L-arginine + H2O
ADP-ribose + L-arginine
-
-
-
-
?
ADP-ribose-L-arginine + H2O
ADP-ribose + L-arginine
-
as a GST-fusion protein, ADP-ribosylarginine formed by chicken heterophil arginine-specific ADP-ribosyltransferase
-
-
?
ADP-ribosylarginine + H2O
ADP-ribose + L-arginine
-
-
-
-
?
ADP-ribosylarginine + H2O
ADP-ribose + L-arginine
-
-
-
-
?
alpha-subunit of stimulating GTP-binding protein ADP-ribosylated + H2O
alpha-subunit of stimulating GTP-binding protein + ADP-ribose
-
-
-
?
alpha-subunit of stimulating GTP-binding protein ADP-ribosylated + H2O
alpha-subunit of stimulating GTP-binding protein + ADP-ribose
-
the GDP-bound form of ADP-ribosylated stimulating GTP-binding protein-alpha is more rapidly hydrolyzed than the GTPgammaS-bound form
-
?
cholera toxin A1-subunit ADP-ribosylated + H2O
cholera toxin A1-subunit + ADP-ribose
-
-
-
?
cholera toxin A1-subunit ADP-ribosylated + H2O
cholera toxin A1-subunit + ADP-ribose
-
-
-
?
Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + L-arginine
-
-
-
-
?
Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + L-arginine
-
-
-
-
?
nonmuscle actin ADP-ribosylated + H2O
nonmuscle actin + ADP-ribose
-
-
-
?
nonmuscle actin ADP-ribosylated + H2O
nonmuscle actin + ADP-ribose
-
-
-
?
protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + protein-L-arginine
-
-
-
-
?
protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + protein-L-arginine
-
-
-
-
?
additional information
?
-
-
structure-function relationship, overview
-
-
?
additional information
?
-
ADPRH cleaves the glycosidic bond of ADP-ribose attached to an Arg residue of a protein
-
-
?
additional information
?
-
-
ADPRH cleaves the glycosidic bond of ADP-ribose attached to an Arg residue of a protein
-
-
?
additional information
?
-
-
isoform ARH1 catalyzes the hydrolysis of the N-glycosidic bond of mono-(ADP-ribosyl)ated arginine, while isoform ARH3 hydrolyzes poly-(ADP-ribose) and O-acetyl-ADP-ribose
-
-
?
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2'-O-acetyl-ADP-ribose + H2O
ADP-ribose + acetate
-
-
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + L-arginine
O-acetyl-ADP-ribose + H2O
ADP-ribose + acetate
-
the reaction is catalyzed by isoform ARH3 only
-
-
?
protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + protein-L-arginine
additional information
?
-
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
ADP-ribosylarginine hydrolase presumably regenerates an arginine site that can be ADP-ribosylated by NAD-arginine ADP-ribosyltransferase. The balance between these two opposing enzymatic activities may control some aspects of cellular metabolism
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
-
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
the presence of ADP-ribosyltransferases and ADP-ribosylhydrolases may lead to an ADP-ribosylation/de-ADP-ribosylation cycle, lending further support to the hypothesis that this covalent modification may have a regulatory function in animal cells
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
the presence of different enzymes and effectors controlling ADP-ribosylarginine synthesis and degradation is reminiscent of the protein kinase-phosphatase system
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
-
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
the presence of ecto-ADP-ribosyltransferase and arginine-specific ADP-ribosylation of cell-surface protein have been reported. Application of the method on the extracellular ADP-ribosylation of intact cells may help to reveal the role of the modification in physiological events such as cell adhesion or cell-cell communication
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
-
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
in Rhodospirillium rubrum, a nitrogen-fixing microorganism, ADP-ribosylation of an arginine residue in a nitrogenase inhibits its activity. Inactivation of the nitrogenase can be reversed by a hydrolase which cleaves the ADP-ribose-arginine bond
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
in nitrogen fixing bacteria, Rhodospirillium rubrum, ADP-ribosylation-de-ADP-ribosylation of a specific arginine-residue of dinitrogenase reductase has been shown to regulate the enzyme activity
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
-
the existence of a ADP-ribosylation cycle was established in the bacterium Rhodospirillium rubrum where it regulates dinitrogenase reductase, a key enzyme in nitrogen fixation
-
-
?
Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + L-arginine
-
-
-
-
?
Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + L-arginine
-
-
-
-
?
protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + protein-L-arginine
-
-
-
-
?
protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + protein-L-arginine
-
-
-
-
?
additional information
?
-
ADPRH cleaves the glycosidic bond of ADP-ribose attached to an Arg residue of a protein
-
-
?
additional information
?
-
-
ADPRH cleaves the glycosidic bond of ADP-ribose attached to an Arg residue of a protein
-
-
?
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Ataxia
Biallelic Mutations in ADPRHL2, Encoding ADP-Ribosylhydrolase 3, Lead to a Degenerative Pediatric Stress-Induced Epileptic Ataxia Syndrome.
Ataxia
Novel imaging and clinical phenotypes of CONDSIAS disorder caused by a homozygous frameshift variant of ADPRHL2: a case report.
Breast Neoplasms
Variations in the mRNA expression of poly(ADP-ribose) polymerases, poly(ADP-ribose) glycohydrolase and ADP-ribosylhydrolase 3 in breast tumors and impact on clinical outcome.
Carcinogenesis
ADP-Ribosylarginine Hydrolase Regulates Cell Proliferation and Tumorigenesis.
Carcinogenesis
ADPRH is a prognosis-related biomarker and correlates with immune infiltrates in low grade glioma.
Cholera
ADP-ribosylarginine glycohydrolase catalyzing the release of ADP-ribose from the cholera toxin-modified alpha-subunits of GTP-binding proteins.
Cholera
Enhanced sensitivity to cholera toxin in female ADP-ribosylarginine hydrolase (ARH1)-deficient mice.
Communicable Diseases
Macrodomain ADP-ribosylhydrolase and the pathogenesis of infectious diseases.
Cystic Fibrosis
A comprehensive review of therapeutic approaches available for the treatment of cholera.
Glioma
ADPRH is a prognosis-related biomarker and correlates with immune infiltrates in low grade glioma.
Infections
An MHV macrodomain mutant predicted to lack ADP-ribose binding activity is severely attenuated, indicating multiple roles for the macrodomain in coronavirus replication.
Melanoma
Co-expression modules construction by WGCNA and identify potential prognostic markers of uveal melanoma.
Neoplasms
ADP-Ribosylarginine Hydrolase Regulates Cell Proliferation and Tumorigenesis.
Neoplasms
ADPRH is a prognosis-related biomarker and correlates with immune infiltrates in low grade glioma.
Neoplasms
Variations in the mRNA expression of poly(ADP-ribose) polymerases, poly(ADP-ribose) glycohydrolase and ADP-ribosylhydrolase 3 in breast tumors and impact on clinical outcome.
Seizures
Novel imaging and clinical phenotypes of CONDSIAS disorder caused by a homozygous frameshift variant of ADPRHL2: a case report.
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Moss, J.; Jacobson, M.K.; Stanley, S.J.
Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme
Proc. Natl. Acad. Sci. USA
82
5603-5607
1985
Meleagris gallopavo, Rhodospirillum rubrum
brenda
Moss, J.; Oppenheimer, N.J.; West, R.E.; Stanley, S.J.
Amino acid specific ADP-ribosylation: substrate specificity of an ADP-ribosylarginine hydrolase from turkey erythrocytes
Biochemistry
25
5408-5414
1986
Meleagris gallopavo
brenda
Moss, J.; Tsai, S.C.; Adamik, R.; Chen, H.C.; Stanley, S.J.
Purification and characterization of ADP-ribosylarginine hydrolase from turkey erythrocytes
Biochemistry
27
5819-5823
1988
Meleagris gallopavo, Rhodospirillum rubrum
brenda
Kim, E.S.; Graves, D.J.
Development of a high-performance liquid chromatography assay method and characterization of adenosine diphosphate-ribosylarginine hydrolase in skeletal muscle
Anal. Biochem.
187
251-257
1990
Gallus gallus, Oryctolagus cuniculus, Rattus norvegicus, Rhodospirillum rubrum
brenda
Moss, J.; Stanley, S.J.; Nightingale, M.S.; Murtagh, J.J.; Monaco, L.; Mishima, K.; Chen, H.C.; Williamson, K.C.; Tsai, S.C.
Molecular and immunological characterization of ADP-ribosylarginine hydrolases
J. Biol. Chem.
267
10481-10488
1992
Bos taurus, Cavia porcellus, Ovis aries, Meleagris gallopavo, Mus musculus, Rattus norvegicus, Rhodospirillum rubrum, Sus scrofa
brenda
Takada, T.; Iida, K.; Moss, J.
Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase
J. Biol. Chem.
268
17837-17843
1993
Bos taurus, Cavia porcellus, Homo sapiens, Meleagris gallopavo, Mus musculus, Rattus norvegicus, Rhodospirillum rubrum
brenda
Maehama, T.; Nishina, H.; Katada, T.
ADP-ribosylarginine glycohydrolase catalyzing the release of ADP-ribose from the cholera toxin-modified alpha-subunits of GTP-binding proteins
J. Biochem.
116
1134-1138
1994
Rattus norvegicus
brenda
Takada, T.; Okazaki, I.J.; Moss, J.
ADP-Ribosylarginine hydrolases
Mol. Cell. Biochem.
138
119-122
1994
Oryctolagus cuniculus, Ovis aries, Meleagris gallopavo, Mus musculus, Rattus norvegicus, Rhodospirillum rubrum, Sus scrofa
brenda
Ohno, T.; Tsuchiya, M.; Osago, H.; Hara, N.; Jidoi, J.; Shimoyama, M.
Detection of arginine-ADP-ribosylated protein using recombinant ADP-ribosylarginine hydrolase
Anal. Biochem.
231
115-122
1995
Mus musculus, Rattus norvegicus, Rhodospirillum rubrum
brenda
Miyaoka, T.; Tsuchiya, M.; Yamada, K.; Badruzzaman, M.; Yamamori, C.; Ishino, H.; Shimoyama, M.
Immunohistochemical localization of ADP-ribosylarginine hydrolase in rodent CNS
Brain Res.
746
1-9
1997
Mus musculus, Rattus norvegicus, Rhodospirillum rubrum
brenda
Moss, J.; Zolkiewska, A.; Okazaki, I.
ADP-ribosylarginine hydrolases and ADP-ribosyltransferases
Adv. Exp. Med. Biol.
419
25-33
1997
Bos taurus, Cavia porcellus, Oryctolagus cuniculus, Ovis aries, Meleagris gallopavo, Mus musculus, Rattus norvegicus, Rhodospirillum rubrum
brenda
Konczalik, P.; Moss, J.
Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases
J. Biol. Chem.
274
16736-16740
1999
Bos taurus, Homo sapiens, Meleagris gallopavo, Mus musculus, Rattus norvegicus, Rhodospirillum rubrum
brenda
Ono, T.; Kasamatsu, A.; Oka, S.; Moss, J.
The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases
Proc. Natl. Acad. Sci. USA
103
16687-16691
2006
Homo sapiens
brenda
Osago, H.; Terashima, M.; Hara, N.; Yamada, K.; Tsuchiya, M.
A new detection method for arginine-specific ADP-ribosylation of protein - A combinational use of anti-ADP-ribosylarginine antibody and ADP-ribosylarginine hydrolase
J. Biochem. Biophys. Methods
70
1014-1019
2008
Rattus norvegicus
brenda
Kato, J.; Zhu, J.; Liu, C.; Moss, J.
Enhanced sensitivity to cholera toxin in ADP-ribosylarginine hydrolase-deficient mice
Mol. Cell. Biol.
27
5534-5543
2007
Mus musculus
brenda
Kernstock, S.; Koch-Nolte, F.; Mueller-Dieckmann, J.; Weiss, M.S.; Mueller-Dieckmann, C.
Cloning, expression, purification and crystallization as well as X-ray fluorescence and preliminary X-ray diffraction analyses of human ADP-ribosylhydrolase 1
Acta Crystallogr. Sect. F
65
529-532
2009
Homo sapiens (P54944), Homo sapiens
brenda
Li, X.D.; Huergo, L.F.; Gasperina, A.; Pedrosa, F.O.; Merrick, M.; Winkler, F.K.
Crystal structure of dinitrogenase reductase-activating glycohydrolase (DraG) reveals conservation in the ADP-ribosylhydrolase fold and specific features in the ADP-ribose-binding pocket
J. Mol. Biol.
390
737-746
2009
Homo sapiens
brenda
Mashimo, M.; Kato, J.; Moss, J.
Structure and function of the ARH family of ADP-ribosyl-acceptor hydrolases
DNA Repair
23
88-94
2014
Mus musculus
brenda
Isabelle, M.; Gagne, J.P.; Gallouzi, I.E.; Poirier, G.G.
Quantitative proteomics and dynamic imaging reveal that G3BP-mediated stress granule assembly is poly(ADP-ribose)-dependent following exposure to MNNG-induced DNA alkylation
J. Cell Sci.
125
4555-4566
2012
Homo sapiens
brenda
Drown, B.S.; Shirai, T.; Rack, J.G.M.; Ahel, I.; Hergenrother, P.J.
Monitoring poly(ADP-ribosyl)glycohydrolase activity with a continuous fluorescent substrate
Cell Chem. Biol.
25
1562-1570
2018
Homo sapiens (P54922)
brenda
Smith, S.J.; Towers, N.; Saldanha, J.W.; Shang, C.A.; Mahmood, S.R.; Taylor, W.R.; Mohun, T.J.
The cardiac-restricted protein ADP-ribosylhydrolase-like 1 is essential for heart chamber outgrowth and acts on muscle actin filament assembly
Dev. Biol.
416
373-388
2016
Xenopus laevis (Q6AZR2), Xenopus laevis
brenda