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Information on EC 3.2.2.19 - [protein ADP-ribosylarginine] hydrolase
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3.2.2.19 [protein ADP-ribosylarginine] hydrolaseIUBMB Comments
The enzyme will remove ADP-D-ribose from arginine residues in ADP-ribosylated proteins.
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Word Map
- 3.2.2.19
-
adp-ribosylation
-
nad:arginine
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polyadp-ribose
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mono-adp-ribosylation
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pargs
-
arginine-specific
- adp-ribose-arginine
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macrodomains
- nsp3
-
monoadp-ribosylated
- mono-adp-ribosyltransferase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
adp-ribosylhydrolase, adp-ribosylarginine hydrolase, adprhl1, adprh, adp-ribosylhydrolase 3, poly-(adp-ribose) glycohydrolase, harh1, adp-ribosylhydrolase 1, o-acetyl-adp-ribose hydrolase, adp-ribosyl(arginine)protein hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADP-ribose-L-arginine cleavage enzyme
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-
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ADP-ribose-L-arginine cleaving enzyme
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-
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ADP-ribosylarginine glycohydrolase
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-
-
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ADP-ribosylarginine hydrolase
ADPRH
ARH1
ARH3
Nomega-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
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-
-
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[protein ADP-ribosylarginine] hydrolase
additional information
-
the enzyme is a member of the ADP-ribosylhydrolase family
ADP-ribosylarginine hydrolase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Nomega-(ADP-D-ribosyl)-L-arginine + H2O = ADP-D-ribose + L-arginine
(2)
-
-
-
protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O = ADP-D-ribose + protein-L-arginine
(1)
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
hydrolysis of N-glycosyl bond
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-
-
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SYSTEMATIC NAME
IUBMB Comments
protein-Nomega-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
The enzyme will remove ADP-D-ribose from arginine residues in ADP-ribosylated proteins.
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CAS REGISTRY NUMBER
COMMENTARY
98668-52-1
-
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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'-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-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
maltose binding protein ADP-ribosylated + H2O
maltose binding protein + ADP-ribose
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MBP is ADP-ribosylated by an arginine-specific ADP-ribosyltransferase cholera toxin
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?
O-acetyl-ADP-ribose + H2O
ADP-ribose + acetate
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the reaction is catalyzed by isoform ARH3 only
-
-
?
ADP-ribose DABSYL-L-arginine methyl ester + H2O
DABSYL-L-arginine methyl ester + ADP-ribose
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-
-
?
ADP-ribose DABSYL-L-arginine methyl ester + H2O
DABSYL-L-arginine methyl ester + ADP-ribose
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-
-
?
ADP-ribose DABSYL-L-arginine methyl ester + H2O
DABSYL-L-arginine methyl ester + ADP-ribose
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-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
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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
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-
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
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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
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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
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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
-
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
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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
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as a GST-fusion protein, ADP-ribosylarginine formed by chicken heterophil arginine-specific ADP-ribosyltransferase
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-
?
alpha-subunit of stimulating GTP-binding protein ADP-ribosylated + H2O
alpha-subunit of stimulating GTP-binding protein + ADP-ribose
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-
-
?
alpha-subunit of stimulating GTP-binding protein ADP-ribosylated + H2O
alpha-subunit of stimulating GTP-binding protein + ADP-ribose
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the GDP-bound form of ADP-ribosylated stimulating GTP-binding protein-alpha is more rapidly hydrolyzed than the GTPgammaS-bound form
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?
cholera toxin A1-subunit ADP-ribosylated + H2O
cholera toxin A1-subunit + ADP-ribose
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-
-
?
cholera toxin A1-subunit ADP-ribosylated + H2O
cholera toxin A1-subunit + ADP-ribose
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-
-
?
nonmuscle actin ADP-ribosylated + H2O
nonmuscle actin + ADP-ribose
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-
-
?
nonmuscle actin ADP-ribosylated + H2O
nonmuscle actin + ADP-ribose
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-
-
?
protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + protein-L-arginine
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-
-
-
?
protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + protein-L-arginine
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-
-
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?
additional information
?
-
ADPRH cleaves the glycosidic bond of ADP-ribose attached to an Arg residue of a protein
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-
?
additional information
?
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ADPRH cleaves the glycosidic bond of ADP-ribose attached to an Arg residue of a protein
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-
?
additional information
?
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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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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
O-acetyl-ADP-ribose + H2O
ADP-ribose + acetate
-
the reaction is catalyzed by isoform ARH3 only
-
-
?
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
-
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
-
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
-
-
?
protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + protein-L-arginine
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-
-
-
?
protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + protein-L-arginine
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-
-
-
?
additional information
?
-
ADPRH cleaves the glycosidic bond of ADP-ribose attached to an Arg residue of a protein
-
-
?
additional information
?
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-
ADPRH cleaves the glycosidic bond of ADP-ribose attached to an Arg residue of a protein
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
required. The presence of both Mg2+ ions is required for the correct positioning of the distal ribose. The activity is abolished upon mutation of even a single Mg2+ coordinating residue
Mg2+
-
enhances, activation is maximal with 5-10 mM dithiothreitol and 5-10 mM Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
incubation in 20 mM at 37°C leads to rapid loss of activity but addition of Mg2+ stabilizes the hydrolase against thermal inactivation
N-ethylmaleimide
-
after incubation with dithiothreitol at 30°C the thiol-sensitive and the thiol-resistant hydrolase are inactivated by NEM at 4°C , exposure to dithiothreitol at 4°C is sufficient to permit subsequent inactivation of the thiol-sensitive but not the thiol-resistant form by NEM
NAD+
-
10 mM Mg2+ or 10 mM Mg2+ plus 5 mM dithiothreitol reduces the extent of inactivation of thiol-sensitive and thiol-resistant hydrolase by NAD+
NAD-arginine ADP-ribosyltransferase
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10 mM Mg2+ or 10 mM Mg2+ plus 5 mM dithiothreitol reduces the extent of inactivation of thiol-sensitive and thiol-resistant hydrolase by NAD-arginine ADP-ribosyltransferase
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ADPribose
-
inhibition by ADPribose stronger than by ADP and AMP
alphaNAD+
-
inhibition by ADPribose stronger than by alphaNAD+ and betaNAD+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
enhances, activation is maximal with 5-10 mM dithiothreitol and 5-10 mM MgCl2
dithiothreitol
-
synergistically stimulated by Mg2+ and dithiothreitol
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0053
ADP-ribose DABSYL-L-arginine methyl ester
-
in presence of 15 mM magnesium and 5 mM DTT
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00009
0.00016
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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brenda
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-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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-
brenda
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red nucleus, Darkschewitsch nucleus and medial parabrachial nucleus of the lower brainstem
brenda
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medial habenular nucleus and lateral habenular nucleus of the habenula
brenda