Information on EC 3.2.2.19 - [protein ADP-ribosylarginine] hydrolase

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

EC NUMBER
COMMENTARY hide
3.2.2.19
-
RECOMMENDED NAME
GeneOntology No.
[protein ADP-ribosylarginine] hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Nomega-(ADP-D-ribosyl)-L-arginine + H2O = ADP-D-ribose + L-arginine
show the reaction diagram
(2)
-
-
-
protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O = ADP-D-ribose + protein-L-arginine
show the reaction diagram
(1)
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of N-glycosyl bond
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.
CAS REGISTRY NUMBER
COMMENTARY hide
98668-52-1
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
-
-
-
-
?
2'-phospho-ADP-ribosylarginine + H2O
2'-phospho-ADP-ribose + arginine
show the reaction diagram
-
-
-
?
ADP-ribose-4-dimethylaminoazobenzene-4-sulfonyl arginine methyl ester + H2O
4-dimethylaminoazobenzene-4-sulfonyl arginine methyl ester + ADP-ribose
show the reaction diagram
ADP-ribose-arginine + H2O
ADP-ribose + arginine
show the reaction diagram
ADP-ribose-L-arginine + H2O
ADP-ribose + L-arginine
show the reaction diagram
ADP-ribosylarginine methyl ester + H2O
ADP-ribose + arginine methyl ester
show the reaction diagram
-
-
-
?
ADP-ribosylguanidine + H2O
ADP-ribose + guanidine
show the reaction diagram
-
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
show the reaction diagram
casein ADP-ribosylated + H2O
ADP-ribose + casein
show the reaction diagram
-
-
-
?
cholera toxin A1-subunit ADP-ribosylated + H2O
cholera toxin A1-subunit + ADP-ribose
show the reaction diagram
histones ADP-ribosylated + H2O
?
show the reaction diagram
-
-
-
-
?
lysozyme ADP-ribosylated + H2O
?
show the reaction diagram
-
-
-
-
?
maltose binding protein ADP-ribosylated + H2O
maltose binding protein + ADP-ribose
show the reaction diagram
-
MBP is ADP-ribosylated by an arginine-specific ADP-ribosyltransferase cholera toxin
-
?
Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + L-arginine
show the reaction diagram
nonmuscle actin ADP-ribosylated + H2O
nonmuscle actin + ADP-ribose
show the reaction diagram
O-acetyl-ADP-ribose + H2O
ADP-ribose + acetate
show the reaction diagram
-
the reaction is catalyzed by isoform ARH3 only
-
-
?
protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + protein-L-arginine
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
2'-O-acetyl-ADP-ribose + H2O
ADP-ribose + acetate
show the reaction diagram
-
-
-
-
?
ADP-ribose-arginine + H2O
ADP-ribose + arginine
show the reaction diagram
Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + L-arginine
show the reaction diagram
O-acetyl-ADP-ribose + H2O
ADP-ribose + acetate
show the reaction diagram
-
the reaction is catalyzed by isoform ARH3 only
-
-
?
protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O
ADP-ribose + protein-L-arginine
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine 5'-diphosphate(hydroxymethyl)pyrrolidinediol
-
-
ADP-ribose
-
-
ADP-ribosylarginine methyl ester
-
-
-
ADPribose
alphaNAD+
Arginine methyl ester
betaNAD+
-
inhibition by alphaNAD+ stronger than by betaNAD+
dithiothreitol
-
incubation in 20 mM at 37C leads to rapid loss of activity but addition of Mg2+ stabilizes the hydrolase against thermal inactivation
N-ethylmaleimide
-
after incubation with dithiothreitol at 30C the thiol-sensitive and the thiol-resistant hydrolase are inactivated by NEM at 4C , exposure to dithiothreitol at 4C is sufficient to permit subsequent inactivation of the thiol-sensitive but not the thiol-resistant form by NEM
NaCl
-
inhibition with 200 mM
NAD+
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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+
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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NaF
-
more than 80% inhibition with 5 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0472
2'-phospho-ADP-ribosylarginine
-
-
0.0053
ADP-ribose-4-dimethylaminoazobenzene-4-sulfonyl arginine methyl ester
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in presence of 15 mM magnesium and 5 mM DTT
-
0.0262 - 0.065
ADP-ribosylarginine
0.005
ADP-ribosylarginine methyl ester
-
as a GST-fusion protein
-
0.0271
ADP-ribosylguanidine
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-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002
ADP-ribose
-
competitive inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000395
-
thiol-sensitive form
0.0000476
-
-
0.0000487
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thiol-resistant form
0.00008
-
partially purified from kidney
0.00009
-
partially purified from liver; partially purified from muscle
0.00016
-
partially purified from heart; partially purified from lung
0.00045
-
partially purified from spleen
0.00046
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partially purified from testis
0.00049
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partially purified from brain
0.00183
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as a GST-fusion protein in cerebrospinal fluid
0.00815
-
as a GST-fusion protein in brain cytosol
0.32
-
as a GST-fusion protein
0.55
-
as a GST-fusion protein
3.15
-
after 20000fold purification
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
hydrolysis of O-acetyl-[14C]ADP-ribose catalyzed by ARH3
7.5
-
activity assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
activity assay
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isoform ARH1 and ARH3
Manually annotated by BRENDA team
-
brain cytosol
Manually annotated by BRENDA team
-
isoform ARH3
Manually annotated by BRENDA team
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isoform ARH3
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
111000
-
x * 111000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 111000, SDS-PAGE
monomer
-
1 * 39000, SDS-PAGE
additional information
-
structure comparison to the Azospirillum brasilense enzyme DraG
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant hARH1 in complex with K+ and ADP, mixing of equal volumes of protein solution containing 15-20 mg/ml protein in 20 mM HEPES, pH 7.0, 100 mM NaCl and 3 mM DTT with reservoir solution containing 150 mM lithium acetate and 25% w/v PEG 3350, at 20C, equilibration over 0.75 ml reservoir solution, 2 weeks, X-ray diffraction structure determination and analysis at 1.9 A resolution
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
20000 fold by DE-52, phenyl-Sepharose, hydroxylapatite, Affi-Gel 501 organo-mercurial agarose, Ultrogel AcA 54
-
20000 fold by DE-52, phenyl-Sepharose, hydroxylapatite, Affi-Gel 501 organo-mercurial agarose, Ultrogel AcA 54; partial
-
200000fold by DE-52, phenyl-Sepharose, hydroxylapatite, Ultrogel AcA 54, Mono Q chromatography
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200000fold by DE-52, phenyl-Sepharose, hydroxylapatite, Ultrogel AcA 54, Mono Q chromatography; depending on the procedure used for purification, either a thiol-resistant or a thiol-sensitive species can be isolated. Organomercurial chromatography apparently results in the formation of the thiol-sensitive species of hydrolase as the exposure of the thiol-resistant form to HgCl2 does
-
200000fold by DE-52, phenyl-Sepharose, hydroxylapatite, Ultrogel AcA 54, Mono Q chromatography; partial by successive chromatography on DE-52 cellulose, phenyl-Sepharose and organomercurial agarose
-
800fold by DE-52, phenyl-Sepharose, carboxymethylcellulose, organomercurial agarose, Ultrogel AcA 54
-
as a GST-fusion protein almost to homogeneity by affinity-column chromatography of glutathione-Sepharose
-
homogenate of chicken muscle cells from tissue culture was centrifugated and the supernatant dialyzed
-
partial
partial by successive chromatography on DE-52 cellulose, phenyl-Sepharose and organomercurial agarose
-
recombinant His-tagged hARH1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
using glutathione-Sepharose 4B
-
using His-Bind metal chelation resin
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression as a glutathione S-transferase-linked fusion protein in Escherichia coli
-
expression as a glutathione S-transferase-linked fusion protein in Escherichia coli; wild-type and mutant rat hydrolases are expressed in Escherichia coli
-
expression in Escherichia coli
-
expression of His-tagged hARH1 in Escherichia coli strain BL21(DE3)
fragments are cloned into a lambda FIX II vector, pGEM 3Z vector and the pKO Scrambler vector, cloned into a pcDNA4/V5-His or pGEX-2T vector to produce the recombinant wild-type plasmid
-
wild-type and mutant human hydrolases are expressed in Escherichia coli
-
wild-type and mutant rat hydrolases are expressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D77/78N
-
mutant does not hydrolyze poly(ADP-ribose)
E238/239Q
-
mutant hydrolyzes O-acetyl-ADP-ribose at rates similar to that of the wild-type
E261/262Q
-
mutant hydrolyzes O-acetyl-ADP-ribose at rates similar to that of the wild-type
E756D
-
the mutation completely abolishes catalytic activity