3.2.2.19: [protein ADP-ribosylarginine] hydrolase
This is an abbreviated version!
For detailed information about [protein ADP-ribosylarginine] hydrolase, go to the full flat file.
Word Map on EC 3.2.2.19
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3.2.2.19
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adp-ribosylation
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nad:arginine
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polyadp-ribose
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mono-adp-ribosylation
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pargs
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arginine-specific
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adp-ribose-arginine
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macrodomains
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nsp3
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monoadp-ribosylated
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mono-adp-ribosyltransferase
- 3.2.2.19
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adp-ribosylation
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nad:arginine
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polyadp-ribose
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mono-adp-ribosylation
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pargs
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arginine-specific
- adp-ribose-arginine
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macrodomains
- nsp3
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monoadp-ribosylated
- mono-adp-ribosyltransferase
Reaction
Synonyms
AAH, ADP-ribose-L-arginine cleavage enzyme, ADP-ribose-L-arginine cleaving enzyme, ADP-ribosyl(arginine)protein hydrolase, ADP-ribosyl-acceptor hydrolase, ADP-ribosylarginine glycohydrolase, ADP-ribosylarginine hydrolase, ADP-ribosylhydrolase, ADP-ribosylhydrolase 1, ADP-ribosylhydrolase 3, ADP-ribosylhydrolase-like 1, ADPRH, AdprHl1, ARH1, ARH3, hARH1, mono-ADP-ribosyl-arginine hydrolase, More, Nomega-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase, O-acetyl-ADP-ribose hydrolase, PARG, poly(ADP-ribose) glycohydrolase, poly-(ADP-ribose) glycohydrolase, [protein ADP-ribosylarginine] hydrolase
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Substrates Products
Substrates Products on EC 3.2.2.19 - [protein ADP-ribosylarginine] hydrolase
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REACTION DIAGRAM
2'-phospho-ADP-ribosylarginine + H2O
2'-phospho-ADP-ribose + arginine
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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
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ADP-ribosylguanidine + H2O
ADP-ribose + guanidine
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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
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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
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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
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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
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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
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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
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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
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ADP-ribose-arginine + H2O
ADP-ribose + arginine
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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
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ADP-ribose-arginine + H2O
ADP-ribose + arginine
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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
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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
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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-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-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-ribose
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nonmuscle actin ADP-ribosylated + H2O
nonmuscle actin + ADP-ribose
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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
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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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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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