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A1 peptide of cholera toxin + NAD+
nicotinamide + ?
-
four mol of ADP-ribose are incorporated into 1 mol of A1 peptide. Modification of the A1 peptide increases its enzymatic activity up to 4fold
-
-
?
actin + NAD+
nicotinamide + ?
agmatine + NAD+
nicotinamide + ?
arginine + NAD+
nicotinamide + ADP-ribose-L-arginine
-
-
-
-
?
basic fibroblast growth factor FGF-2 + NAD+
nicotinamide + ?
beta-lactoglobulin + NAD+
nicotinamide + ?
-
-
-
-
?
bovine plasma albumin + NAD+
nicotinamide + ?
-
-
-
-
?
bovine serum albumin + NAD+
nicotinamide + ?
-
poor ADP-ribose acceptor
-
-
?
casein + NAD+
nicotinamide + ?
diethylamino-(benzylidineamino)guanidine + NAD+
nicotinamide + ?
-
-
-
-
?
DNase I + NAD+
nicotinamide + ?
-
-
-
-
?
guanidine + NAD+
nicotinamide + ?
-
-
-
-
?
guanidinobutyrate + NAD+
nicotinamide + ?
-
-
-
-
?
guanidinopropionate + NAD+
nicotinamide + ?
-
-
-
-
?
histone + NAD+
nicotinamide + ?
histone + NAD+
Nomega-[(2'-phospho-ADP)-D-ribosyl]-histone-L-arginine + nicotinamide + H+
-
isozyme ART2 is active with high and low molecular weight histones, membrane-bound and PI-PLC released ART2 preferentially ADP-ribosylate high or low MW histones, respectively
-
-
?
histone f1 + NAD+
nicotinamide + ?
-
-
-
-
?
histone f2a + NAD+
nicotinamide + ?
-
-
-
-
?
histone f2b + NAD+
nicotinamide + ?
-
-
-
-
?
histone f3 + NAD+
nicotinamide + ?
-
-
-
-
?
histone H2B + NAD+
Nomega-[(2'-phospho-ADP)-D-ribosyl]-histone H2B-L-arginine + nicotinamide
Meleagris sp.
-
-
-
-
?
human alpha-defensin-1 + NAD+
nicotinamide + ?
human alpha-globulin + NAD+
nicotinamide + ?
-
-
-
-
?
human beta-defensin-1 + NAD+
nicotinamide + ?
-
-
-
-
?
human beta-globulin + NAD+
nicotinamide + ?
-
-
-
-
?
human gamma-globulin + NAD+
nicotinamide + ?
-
-
-
-
?
human neutrophil peptide-1 + NAD+
Nomega-(ADP-D-ribosyl)-L-arginine-human neutrophil peptide-1 + nicotinamide
karyopherin-beta1 + NAD+
nicotinamide + ?
-
-
-
?
L-arginine methyl ester + NAD+
nicotinamide + Nomega-(ADP-D-ribosyl)-L-arginine
L-arginine methyl ester + NADP+
nicotinamide + N2-(2'-phospho-ADP-D-ribosyl)-L-arginine
-
-
-
-
?
lysozyme + NAD+
nicotinamide + ?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
agmatine as ADPribose acceptor is used
-
-
?
NAD+ + actin
nicotinamide + H+ + (ADP-ribosyl)-actin
NAD+ + agmatine
nicotinamide + Nomega-(ADP-D-ribosyl)-agmatine
NAD+ + alpha-actin-L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-alpha-actin-L-arginine
-
skeletal muscle alpha actin
-
-
?
NAD+ + beta-actin
nicotinamide + H+ + (ADP-ribosyl)-beta-actin
-
modification occurs at residue Arg177
-
?
NAD+ + beta/gamma-actin-L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-beta/gamma-actin-L-arginine
-
non-muscle beta/gamma actin
-
-
?
NAD+ + eEF2 L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-eEF2-L-arginine
-
-
-
?
NAD+ + gamma-actin
nicotinamide + H+ + (ADP-ribosyl)-gamma-actin
-
modification occurs at residue Arg177
-
?
NAD+ + gamma-actin-L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-gamma-actin-L-arginine
-
smooth muscle gamma actin
-
-
?
NAD+ + glucose-regulated protein of 78 kDa/immunoglobulin heavy-chainbinding protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-glucose-regulated protein of 78 kDa/immunoglobulin heavy-chainbinding protein-L-arginine
-
-
-
?
NAD+ + human neutrophil peptide-1
nicotinamide + Nomega-(ADP-D-ribosyl)-human neutrophil peptide-1
NAD+ + MazF L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-MazF-L-arginine
Tequatrovirus T4
-
the enzyme ADP-ribosylates MazF at an arginine residue at position 4
-
-
?
NAD+ + muscle actin
nicotinamide + H+ + (ADP-ribosyl)-muscle actin
substrate source rabbit skeletal muscle
modification occurs at residue Arg177
-
?
NAD+ + non-muscle actin from human platelets
nicotinamide + (ADP-D-ribosyl)-non-muscle actin from human platelets
-
-
-
-
?
NAD+ + polyarginine
nicotinamide + Nomega-(ADP-D-ribosyl)-polyarginine
-
-
-
?
NAD+ + protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
NAD+ + protein poly-L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-poly-L-arginine
-
-
-
?
NAD+ + protein R10H6 L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein N10H6-L-arginine
-
-
-
?
NAD+ + rabbit muscle actin
nicotinamide + (ADP-D-ribosyl)-rabbit muscle actin
-
-
-
-
?
NAD+ + [actin]-L-arginine177
nicotinamide + [actin]-N-(ADP-D-ribosyl)-L-arginine177 + H+
nicotinamide + Nomega-(ADP-D-ribosyl)-agmatine-L-arginine
NAD+ + agmatine L-arginine
-
-
-
-
r
ovalbumin + NAD+
nicotinamide + ?
p-nitrobenzylidine aminoguanidine + NAD+
nicotinamide + mono-ADP-ribosylated p-nitrobenzylidine aminoguanidine
P2X7 purinoceptor protein + NAD+
Nomega-[(2'-phospho-ADP)-D-ribosyl]-P2X7 purinoceptor protein-L-arginine + nicotinamide
-
isozyme ART2
-
-
?
P2X7(k) + NAD+
nicotinamide + ?
-
the P2X7(k) variant is sensitive to activation by ADP-ribosylation whereas the P2X7(a) variant is insensitive
-
-
?
P33 + NAD+
nicotinamide + ?
p33 protein + NAD+
nicotinamide + ?
-
-
-
?
polyarginine + NAD+
nicotinamide + ?
polylysine + NAD+
nicotinamide + ?
-
poor ADP-ribose acceptor
-
-
?
Ras + NAD+
nicotinamide + ?
-
ADP-ribosylation of Ras at Arg41 and Arg 128. The double mutant RasR141K/R128K is ribosylated at an alternative sitem Arg135
-
-
?
RhoA + NAD+
Nomega-(ADP-D-ribosyl)-L-asparagine41-RhoA + nicotinamide
-
the enzyme modifies the low-molecular-mass GTPase RhoA specifically at Asn41
-
-
?
RhoB + NAD+
Nomega-(ADP-D-ribosyl)-L-asparagine41-RhoB + nicotinamide
-
the enzyme modifies the low-molecular-mass GTPase RhoB specifically at Asn41
-
-
?
RhoC + NAD+
Nomega-(ADP-D-ribosyl)-L-asparagine41-RhoC + nicotinamide
-
the enzyme modifies the low-molecular-mass GTPase RhoC specifically at Asn41
-
-
?
soy bean trypsin inhibitor + NAD+
nicotinamide + ?
-
-
-
-
?
soybean trypsin inhibitor + NAD+
Nomega-(ADP-D-ribosyl)-L-arginine-soybean trypsin inhibitor + nicotinamide
-
-
-
-
?
trypsin inhibitor + NAD+
nicotinamide + ?
-
-
-
-
?
wild-type exoenzyme C3 + NAD+
Nomega-(ADP-D-ribosyl)-L-arginine86-wild-type exoenzyme C3 + nicotinamide
-
the recombinant mutant Q217E enzyme modifies the recombinant wild-type enzyme at Arg86
-
-
?
additional information
?
-
actin + NAD+
nicotinamide + ?
-
non-muscle beta/gamma actin, skeletal muscle alpha actin, smooth muscle gamma actin
-
-
?
actin + NAD+
nicotinamide + ?
-
alpha-actin and beta/gamma-actin
-
-
?
actin + NAD+
nicotinamide + ?
-
the ADP ribosylation of actin in the heterophils may be involved in the cellular processes such as phagocytosis, secretion and migration
-
-
?
actin + NAD+
nicotinamide + ?
2% of the activity with p33
-
-
?
actin + NAD+
nicotinamide + ?
3% of the activity with p33
-
-
?
actin + NAD+
nicotinamide + ?
-
no activity with the enzyme from skeletal muscle sarcoplasmic reticulum
-
-
?
agmatine + NAD+
nicotinamide + ?
-
-
-
-
?
agmatine + NAD+
nicotinamide + ?
-
-
-
-
?
agmatine + NAD+
nicotinamide + ?
-
-
-
-
?
agmatine + NAD+
nicotinamide + ?
-
-
-
-
?
agmatine + NAD+
nicotinamide + ?
-
-
-
-
?
agmatine + NAD+
nicotinamide + ?
-
-
-
?
basic fibroblast growth factor FGF-2 + NAD+
nicotinamide + ?
-
-
-
-
?
basic fibroblast growth factor FGF-2 + NAD+
nicotinamide + ?
-
-
-
-
?
casein + NAD+
nicotinamide + ?
-
-
-
-
?
casein + NAD+
nicotinamide + ?
8% of the activity with p33
-
-
?
FGF-2 + NAD+
?
-
ADP-ribosylation of FGF-2 may provide an additional level of control of FGF-2 activity
-
-
?
FGF-2 + NAD+
?
-
ADP-ribosylation of FGF-2 may provide an additional level of control of FGF-2 activity
-
-
?
histone + NAD+
nicotinamide + ?
-
-
-
-
?
histone + NAD+
nicotinamide + ?
130% of the activity with p33
-
-
?
histone + NAD+
nicotinamide + ?
67% of the activity with p33
-
-
?
histone + NAD+
nicotinamide + ?
-
-
-
-
?
histone + NAD+
nicotinamide + ?
-
-
-
-
?
human alpha-defensin-1 + NAD+
nicotinamide + ?
-
poorly recognised substrate
-
-
?
human alpha-defensin-1 + NAD+
nicotinamide + ?
-
-
-
-
?
human neutrophil peptide-1 + NAD+
Nomega-(ADP-D-ribosyl)-L-arginine-human neutrophil peptide-1 + nicotinamide
-
human neutrophil peptide-1, HNP-1, from neutrophil cell surface, ADP-ribosylation of HNP-1 is primarily an activity of ART1 and occurs in inflammatory conditions and disease, lack of modified HNP-1 due to enzyme deficiency in the sputum leads to cystic fibrosis
-
-
?
human neutrophil peptide-1 + NAD+
Nomega-(ADP-D-ribosyl)-L-arginine-human neutrophil peptide-1 + nicotinamide
-
human neutrophil peptide-1, HNP-1, from neutrophil cell surface, isozyme ART1 shows high activity on Arg14 and Arg24, while isozymes ART3, ART4, ART5 are less or not active
-
-
?
human neutrophil peptide-1 + NAD+
Nomega-(ADP-D-ribosyl)-L-arginine-human neutrophil peptide-1 + nicotinamide
-
human neutrophil peptide-1, HNP-1, from neutrophil cell surface, isozyme ART1 is active on Arg14 and Arg24
-
-
?
L-arginine methyl ester + NAD+
nicotinamide + Nomega-(ADP-D-ribosyl)-L-arginine
-
-
-
?
L-arginine methyl ester + NAD+
nicotinamide + Nomega-(ADP-D-ribosyl)-L-arginine
-
-
-
-
?
lysozyme + NAD+
nicotinamide + ?
-
-
-
-
?
lysozyme + NAD+
nicotinamide + ?
Tequatrovirus T4
-
-
-
-
?
NAD+ + actin
nicotinamide + H+ + (ADP-ribosyl)-actin
-
Clostridium botulinum C2 toxin ADP-ribosylates actin isoforms gizzard gamma-smooth muscle actin, spleen beta- and gamma-cytoplasmic actin, and gamma-smooth muscle actin isoforms of aortic smooth muscle actin
-
-
?
NAD+ + actin
nicotinamide + H+ + (ADP-ribosyl)-actin
Clostridium perfringens iota toxin ADP-ribosylates all actin isoforms tested, i.e. alpha-skeletal muscle actin, alpha-cardiac muscle actin, gizzard gamma-smooth muscle actin, spleen beta- and gamma-cytoplasmic actin, and aortic smooth muscle actin containing alpha- and gamma-smooth muscle actin isoforms
-
-
?
NAD+ + agmatine
nicotinamide + Nomega-(ADP-D-ribosyl)-agmatine
-
-
-
-
?
NAD+ + agmatine
nicotinamide + Nomega-(ADP-D-ribosyl)-agmatine
-
-
-
-
?
NAD+ + agmatine
nicotinamide + Nomega-(ADP-D-ribosyl)-agmatine
-
the enzyme labels L-arginine with ADP-ribose from the NAD(+) substrate at the amino nitrogen of the guanidinium side chain
-
-
r
NAD+ + human neutrophil peptide-1
nicotinamide + Nomega-(ADP-D-ribosyl)-human neutrophil peptide-1
-
the enzyme ADP-ribosylates human neutrophil peptide-1 on arginine 14 and 24
-
-
?
NAD+ + human neutrophil peptide-1
nicotinamide + Nomega-(ADP-D-ribosyl)-human neutrophil peptide-1
-
the enzyme ADP-ribosylates human neutrophil peptide-1 on arginine 14 and 24
-
-
?
NAD+ + protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
-
-
-
-
?
NAD+ + protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
-
-
-
-
?
NAD+ + protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
-
-
-
?
NAD+ + protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
-
-
-
-
?
NAD+ + protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
-
-
-
-
?
NAD+ + protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
-
-
-
?
NAD+ + protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
-
-
-
?
NAD+ + protein L-arginine
nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
-
-
-
?
NAD+ + [actin]-L-arginine177
nicotinamide + [actin]-N-(ADP-D-ribosyl)-L-arginine177 + H+
-
-
-
?
NAD+ + [actin]-L-arginine177
nicotinamide + [actin]-N-(ADP-D-ribosyl)-L-arginine177 + H+
-
-
-
-
?
NAD+ + [actin]-L-arginine177
nicotinamide + [actin]-N-(ADP-D-ribosyl)-L-arginine177 + H+
-
-
-
-
?
NAD+ + [actin]-L-arginine177
nicotinamide + [actin]-N-(ADP-D-ribosyl)-L-arginine177 + H+
-
-
-
-
?
NAD+ + [actin]-L-arginine177
nicotinamide + [actin]-N-(ADP-D-ribosyl)-L-arginine177 + H+
-
-
-
?
NAD+ + [actin]-L-arginine177
nicotinamide + [actin]-N-(ADP-D-ribosyl)-L-arginine177 + H+
-
-
-
-
?
ovalbumin + NAD+
nicotinamide + ?
-
-
-
-
?
ovalbumin + NAD+
nicotinamide + ?
-
poor ADP-ribose acceptor
-
-
?
p-nitrobenzylidine aminoguanidine + NAD+
nicotinamide + mono-ADP-ribosylated p-nitrobenzylidine aminoguanidine
-
-
-
?
p-nitrobenzylidine aminoguanidine + NAD+
nicotinamide + mono-ADP-ribosylated p-nitrobenzylidine aminoguanidine
-
-
-
?
P33 + NAD+
nicotinamide + ?
-
preferential endogenous acceptor
-
-
?
P33 + NAD+
nicotinamide + ?
-
no activity with the enzyme from skeletal muscle sarcoplasmic reticulum
-
-
?
polyarginine + NAD+
nicotinamide + ?
-
-
-
-
?
polyarginine + NAD+
nicotinamide + ?
in contrast to its mammalian orthologues, the chicken protein contains an intact R-S-EXE motif
-
-
?
polyarginine + NAD+
nicotinamide + ?
-
-
-
-
?
polyarginine + NAD+
nicotinamide + ?
-
-
-
-
?
polyarginine + NAD+
nicotinamide + ?
Tequatrovirus T4
-
-
-
-
ir
additional information
?
-
-
no substrates: alpha-skeletal muscle actin, alpha-smooth muscle actin or alpha-cardiac muscle actin. The N-terminal region of actin isoforms define the substrate specificity for ADP-ribosylation by Clostridium botulinum C2 toxin
-
-
?
additional information
?
-
in absence of actin, enzyme displays weak NAD+ glycohydrolase activity
-
-
?
additional information
?
-
-
the enzyme exhibits ADP-ribosyltransferase and NAD+ glycohydrolase activity, modeling of interaction od substrate and catalytic residues, overview
-
-
?
additional information
?
-
-
enzyme is involved in posttranslational modification of proteins
-
-
?
additional information
?
-
-
substrate specificity, beta-defensin-1 is a poor substrate, overview
-
-
?
additional information
?
-
-
no activity with NAD+ as substrate
-
-
?
additional information
?
-
Meleagris sp.
-
the enzyme is involved in signal transduction and cytoskeletal realignment
-
-
?
additional information
?
-
-
enzyme catalyzes auto-ADP ribosylation
-
-
?
additional information
?
-
-
in contrast to Yac-1, the Yac-2 enzyme has significant NAD glycohydrolase activity and may preferentially hydrolyze NAD+
-
-
?
additional information
?
-
-
regulation of cytotoxic T cell functions
-
-
?
additional information
?
-
-
the enzyme might be involved in regulating T cell and immune system activity
-
-
?
additional information
?
-
-
enzyme is involved in posttranslational modification of proteins
-
-
?
additional information
?
-
-
involved in immune regulation
-
-
?
additional information
?
-
-
protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in regulation of cellular activities specific amino acid of the acceptor protein, overview
-
-
?
additional information
?
-
-
ART2, in the absence of histone acceptor, has NAD+ glycohydrolase activity, overview, serum proteins are ADP-ribosylated in a thiol-specific manner, soluble recombinant ART2 lacking the GPI anchor shows a different histone specificity than does native cell-bound ART2, the membrane or solution environment of ART2 plays a pivotal role in determining its substrate specificity
-
-
?
additional information
?
-
-
CD38, a potent ecto-NAD-glycohydrolase, controls ADP-ribosyltransferase-2-catalyzed ADP-ribosylation of T cell surface proteins, overview, the enzyme is a a GPI-anchored, toxin-related ADP-ribosylating ectoenzyme, ART2 can sense and translate the local concentration of ecto-NAD into corresponding levels of ADP-ribosylated cell surface proteins, whereas CD38 controls the level of cell surface protein ADP-ribosylation by limiting the substrate availability for ART2
-
-
?
additional information
?
-
-
substrate specificity, human neutrophil peptide-1 is a poor substrate of isozymes ART2.2 and ART5, overview
-
-
?
additional information
?
-
-
among the three ARTs being expressed at the myotube stage ADP-ribosylation of surface proteins can only be attributed to ART1
-
-
?
additional information
?
-
-
NarE undergoes auto-ADP-ribosylation
-
-
?
additional information
?
-
the enzyme can perform auto-ADP-ribosylation. The auto-ADP-ribosylation site occurs preferentially on the R7 residue
-
-
?
additional information
?
-
-
the enzyme can perform auto-ADP-ribosylation. The auto-ADP-ribosylation site occurs preferentially on the R7 residue
-
-
?
additional information
?
-
the enzyme also exhibits NADase activity which produces free ADP-ribose that can covalently bind to lysine
-
-
?
additional information
?
-
-
the enzyme also exhibits NADase activity which produces free ADP-ribose that can covalently bind to lysine
-
-
?
additional information
?
-
-
enzyme is involved in posttranslational modification of proteins
-
-
?
additional information
?
-
the enzyme also shows auto-ADP-ribosylation activity
-
-
?
additional information
additional information
-
-
a large isoform of cyclophilin A, the multi-domain enzyme cyclophilin 40 (Cyp40), binds to the enzyme
-
-
?
additional information
additional information
-
-
a large isoform of cyclophilin A, the multi-domain enzyme cyclophilin 40, binds to the enzyme
-
-
?
additional information
additional information
-
-
a large isoform of cyclophilin A, the multi-domain enzyme cyclophilin 40 (Cyp40), binds to the enzyme
-
-
?
additional information
additional information
-
-
actin with substitution of Asp179 (but not Arg177 and less Glu270) is sensitive towards the toxic action of the enzyme
-
-
?
RNA polymerase + NAD+
additional information
-
Tequatrovirus T4
-
E. coli RNA polymerase
-
-
?
RNA polymerase + NAD+
additional information
-
Tequatrovirus T4
-
alpha-subunit of RNA polymerase
the amino acid carrying the ADP-ribosyl residue appears to be arginine
ir
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E301A
-
no NADase activity detected
E378S
mutation eliminates ADP-ribosylation activity and reduces the weak NAD+ glycohydrolase activity in absence of actin to 50%
E380A
mutation eliminates both ADP-ribosylation activity and the weak NAD+ glycohydrolase activity in absence of actin
E380S
mutation eliminates both ADP-ribosylation activity and the weak NAD+ glycohydrolase activity in absence of actin
F349A
-
the ratio of turnover-number to Km-value in the NADase reaction is 1% of the wild-type ratio. The ratio of turnover-number to Km-value in the ADP-ribosyltransferase activity is 1.9% of the wild-type ratio with rabbit muscle actin as substrate and 4% of the wild-type ratio with non-muscle actin from human platelets as substrate
F349Y
-
the ratio of turnover-number to Km-value in the NADase reaction is 110% of the wild-type ratio
N255A
-
the ratio of turnover-number to Km-value in the NADase reaction is 90% of the wild-type ratio. The ratio of turnover-number to Km-value in the ADP-ribosyltransferase activity is 20% of the wild-type ratio with rabbit muscle actin as substrate and 77% of the wild-type ratio with non-muscle actin from human platelets as substrate
Y246A
-
the ratio of turnover-number to Km-value in the NADase reaction is 90% of the wild-type ratio. The ratio of turnover-number to Km-value in the ADP-ribosyltransferase activity is 1.9% of the wild-type ratio with rabbit muscle actin as substrate and 19% of the wild-type ratio with non-muscle actin from human platelets as substrate
Y251A
-
the ratio of turnover-number to Km-value in the NADase reaction is 10% of the wild-type ratio
Y251F
-
the ratio of turnover-number to Km-value in the NADase reaction is 40% of the wild-type ratio
E207G/E209G
-
abolished ADP-ribosyltransferase activity. Mutated protein localises to the plasma membrane
E209G
-
single point mutant of cARTC2.1 cannot hydrolyse NAD+, although it retains low arginine-specific ADP-ribosyltransferase activity. Mutated protein localises to the plasma membrane
E219Q
-
site-directed mutagenesis, almost inactive mutant
Q217E
-
site-directed mutagenesis, the mutation results in inhibition of the enzyme's ADP-ribosyltransferase activity toward RhoA, the mutant protein is still capable of NAD+-binding and possesses NAD+ glycohydrolase activity, the mutant is capable of ADP-ribosylation of poly-arginine but not poly-asparagine
R151A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R61A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R86A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
DELTA278-322
a deletion mutant lacking the region encompassing the putative transmembrane domain (aminoacids 278-322) shows a diffuse, cytosolic localization compared with full length ARTD15
K242E
-
displays no activity
Y187R
-
displays no activity
Y187R/K242E
-
double mutant contains the R-S-EXE motif, but displays no activity, thus additional residues besides the intact R-S-EXE motif are involved in catalyzing the enzymatic reaction
C201F
-
mutant enzyme of RT6.1, mutant enzyme loses thiol-dependency
C80S
-
mutant enzyme of RT6.1 remains thiol-dependent
C11S
the mutation results in an auto-ADP-ribosylation comparable to the wild type enzyme
C128S
the mutant does not have a stable Fe-S cluster and reduced auto-ADP-ribosylation activity
C130S
the mutation results in an auto-ADP-ribosylation comparable to the wild type enzyme
C67S
the mutant does not have a stable Fe-S cluster and reduced auto-ADP-ribosylation activity
E109D
the mutation results in an auto-ADP-ribosylation comparable to the wild type enzyme
R204E
-
isoform ART2b, no auto-ADP-ribosylation
R204K
-
isoform ART2b, no auto-ADP-ribosylation
R204Y
-
isoform ART2b, no auto-ADP-ribosylation
Y204R
-
isoform ART2a, unlike wild-type, is autoribosylated and has increased enzymic activity
E579Q
the mutant shows reduced biotinylation intensity compared to the wild type enzyme
E581Q
the mutant exhibits strongly reduced biotinylation intensity compared to the wild type enzyme
R426A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R426K/R451K/R473K/R479K/R506K/R519K/R522K/R525K/R535K/R540K/R543K/R566K/R629K
the mutant shows no auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R451K/R473K/R479K/R506K/R519K/R522K/R535K/R540K/R543K/R566K/R629K
the mutant shows no auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R451K/R473K/R506K/R519K/R522K/R525K/R535K/R540K/R543K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and severely reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R451K/R473K/R506K/R519K/R522K/R535K/R540K/R543K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R451K/R473K/R506K/R519K/R522K/R540K/R543K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R473K/R479K/R506K/R519K/R522K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R473K/R506K/R519K/R522K/R540K/R543K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R473K/R506K/R519K/R522K/R540K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R473K/R506K/R519K/R522K/R543K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R473K/R506K/R519K/R522K/R566K/R629K
the mutant shows increased auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R473K/R506K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R451A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R473A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R479A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R506A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R506K
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R506K/R566K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R506Q
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R519A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R522A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R525A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R525K
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R525Q
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R530A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R535A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R540A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R543A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R566A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R629A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
Y493A/E579Q/E581Q
inactive
R352A
-
no ADP-ribosyltransferase activity with rabbit muscle actin and non-muscle actin from human platelets
R352A
-
the ratio of turnover-number to Km-value in the NADase reaction is 2% of the wild-type ratio, no activity
E111D
-
catalytic activity close to wild-type
E111D
the mutation results in an auto-ADP-ribosylation comparable to the wild type enzyme
E120D
-
catalytic activity highly decreased
E120D
the mutant has no auto-ADP-ribosylation ability
R7K
-
catalytic activity highly decreased
R7K
the mutant has no auto-ADP-ribosylation ability
additional information
-
engineering strategy for the creation of a plant-tolerated, zymogen-like form of an otherwise toxic protein. Engineering of a random propeptide library at the C-terminal end of ADP-ribosyltranferase Vip2 and selecting for malfunctional enzyme variants in yeast leads to a proenzyme proVip2 which possesses reduced enzymatic activity as compared with the wild-type Vip2 protein, but remains a potent toxin toward rootworm larvae. The zymogenized Vip2 can be proteolytically activated by rootworm digestive enzyme machinery
additional information
-
depletion of CD38 cells results in enhanced levels of cell surface etheno-ADP-ribosylation on CD38 T cells
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Moss, J.; Stanley, S.J.; Oppenheimer, N.J.
Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes
J. Biol. Chem.
254
8891-8894
1979
Meleagris gallopavo
brenda
Moss, J.; Stanley, S.J.; Watkins, P.A.
Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes
J. Biol. Chem.
255
5838-5840
1980
Meleagris gallopavo
brenda
Yost, D.A.; Moss, J.
Amino acid-specific ADP-ribosylation. Evidence for two distinct NAD:arginine ADP-ribosyltransferases in turkey erythrocytes
J. Biol. Chem.
258
4926-4929
1983
Meleagris gallopavo
brenda
Moss, J.; Vaughan, M.
NAD: arginine mono-ADP-ribosyltransferases from animal cells
Methods Enzymol.
106
430-437
1984
Meleagris gallopavo
brenda
Terashima, M.; Mishima, K.; Yamada, K.; Wakutani, T.; Shimoyama, M.
ADP-ribosylation of actins by arginine-specific ADP-ribosyltransferase purified from chicken heterophils
Eur. J. Biochem.
204
305-311
1992
Gallus gallus
brenda
Watkins, P.A.; Moss, J.
Effects of nucleotides on activity of a purified ADP-ribosyltransferase from turkey erythrocytes
Arch. Biochem. Biophys.
216
74-80
1982
Meleagris gallopavo
brenda
Moss, J.; Osborne, J.C.; Stanley, S.J.
Activation of an erythrocyte NAD:arginine ADP-ribosyltransferase by lysolecithin and nonionic and zwitterionic detergents
Biochemistry
23
1353-1357
1984
Meleagris gallopavo
brenda
Osborne, J.C.; Stanley, S.J.; Moss, J.
Kinetic mechanisms of two NAD:arginine ADP-ribosyltransferases: the soluble, salt-stimulated transferase from turkey erythrocytes and choleragen, a toxin from Vibrio cholerae
Biochemistry
24
5235-5240
1985
Meleagris gallopavo
brenda
West, R.E.; Moss, J.
Amino acid specific ADP-ribosylation: specific NAD: arginine mono-ADP-ribosyltransferases associated with turkey erythrocyte nuclei and plasma membranes
Biochemistry
25
8057-8062
1986
Meleagris gallopavo
brenda
Taniguchi, M.; Tanigawa, Y.; Tsuchiya, M.; Mishima, K.; Obara, S.; Yamada, K.; Shimoyama, M.
Arginine-specific ADP-ribosyltransferase from rabbit skeletal muscle sarcoplasmic reticulum is solubilized as the active form with trypsin: partial purification and characterization
Biochem. Biophys. Res. Commun.
164
128-133
1989
Oryctolagus cuniculus
brenda
Peterson, J.E.; Larew, J.S.A.; Graves, D.J.
Purification and partial characterization of arginine-specific ADP-ribosyltransferase from skeletal muscle microsomal membranes
J. Biol. Chem.
265
17062-17069
1990
Oryctolagus cuniculus
brenda
Zolkiewska, A.; Nightingale M.S.; Moss, J.
Molecular characterization of NAD:arginine ADP-ribosyltransferase from rabbit skeletal muscle
Proc. Natl. Acad. Sci. USA
89
11352-11356
1992
Oryctolagus cuniculus
brenda
Skorko, R.; Zillig, W.; Rohrer, H.; Mailhammer, R.
Purification and properties of the NAD+: protein ADP-ribosyltransferase responsible for the T4-phage-induced modification of the alpha subunit of DNA-dependent RNA polymerase of Escherichia coli
Eur. J. Biochem.
79
55-66
1977
Tequatrovirus T4
brenda
Goff, C.G.
Coliphage-induced ADP-ribosylation of Escherichia coli RNA polymerase
Methods Enzymol.
106
418-429
1984
Tequatrovirus T4
brenda
Soman, G.; Miller, J.F.; Graves, D.
Use of guanylhydrazones as substrates for guanidine-specific mono-ADP-ribosyltransferases
Methods Enzymol.
106
403-410
1984
Oryctolagus cuniculus, Meleagris gallopavo
brenda
McMahon, K.K.; Piron, K.J.; Ha, V.T.; Fullerton, A.T.
Developmental and biochemical characteristics of the cardiac membrane-bound arginine-specific mono-ADP-ribosyltransferase
Biochem. J.
293
789-793
1993
Canis sp., Coturnix sp., Oryctolagus cuniculus, Mus musculus, Rattus norvegicus, Sus scrofa
-
brenda
Shimoyama, M.; Tsuchiya, M.; Hara, N.; Yamada, K.; Osago, H.
Molecular cloning and characterization of arginine-specific ADP-ribosyltransferases from chicken bone marrow cells
Adv. Exp. Med. Biol.
419
137-144
1997
Gallus gallus
brenda
Kanaitsuka, T.; Bortell, R.; Stevens, L.A.; Moss, J.; Sardinha, D.; Rajan, T.V.; Zipris, D.; Mordes, J.P.; Greiner, D.L.; Rossini, A.A.
Expression in BALB/c and C57BL/6 mice of Rt6-1 and Rt6-2 ADP-ribosyltransferases that differ in enzymic activity
J. Immunol.
159
2741-2749
1997
Mus musculus, Rattus norvegicus
brenda
Rigby, M.R.; Bortell, R.; Stevens, L.A.; Moss, J.; Kanaitsuka, T.; Shigeta, H.; Mordes, J.P.; Greiner, D.L.; Rossini, A.A.
Rat RT6.2 and mouse Rt6 locus 1 are NAD+:arginine ADP ribosyltransferases with auto-ADP ribosylation activity
J. Immunol.
156
4259-4265
1996
Mus musculus, Rattus norvegicus
brenda
Braren, R.; Glowacki, G.; Nissen, M.; Haag, F.; Koch-Nolte, F.
Molecular characterization and expression of the gene for mouse NAD+:arginine ecto-mono(ADP-ribosyl)transferase, Art1
Biochem. J.
336
561-568
1998
Mus musculus
-
brenda
Ganesan, A.K.; Mende-Mueller, L.; Selzer, J.; Barbieri, J.T.
Pseudomonas aeruginosa exoenzyme S, a double ADP-ribosyltransferase, resembles vertebrate mono-ADP-ribosyltransferases
J. Biol. Chem.
274
9503-9508
1999
Pseudomonas aeruginosa
brenda
Okazaki, I.J.; Kim, H.J.; Moss, J.
Cloning and characterization of a novel membrane-associated lymphocyte NAD:arginine ADP-ribosyltransferase
J. Biol. Chem.
271
22052-22057
1996
Gallus gallus, Oryctolagus cuniculus, Homo sapiens, Mus musculus (P70352), Mus musculus
brenda
Jones, E.M.; Baird, A.
Cell-surface ADP-ribosylation of fibroblast growth factor-2 by an arginine-specific ADP-ribosyltransferase
Biochem. J.
323
173-177
1997
Bos taurus, Homo sapiens
-
brenda
Donnelly, L.E.; Rendell, N.B.; Murray, S.; Allport, J.R.; Lo, G.; Kefalas, P.; Taylor, G.W.; MacDermot, J.
Arginine-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leukocytes
Biochem. J.
315
635-641
1996
Homo sapiens
-
brenda
Ohno, T.; Badruzzaman, M.; Nishikori, Y.; Tsuchiya, M.; Jidoi, J.; Shimoyama, M.
vortex-mixing-induced inactivation of arginine-specific ADP-ribosyltransferase activity and re-activation of the less-active form by dithiothreitol plus NaCl under anaerobic conditions
Biochem. Mol. Biol. Int.
32
213-220
1994
Gallus gallus
brenda
Terashima, M.; Shimoyama, M.
ADP-ribosylation of A1 peptide of cholera toxin by chicken arginine-specific ADP-ribosyltransferase with a concomitant increase in ADP-ribosyltransferase activity of the peptide
Biomed. Res.
14
329-335
1993
Gallus gallus
-
brenda
Moss, J.; Balducci, E.; Cavanaugh, E.; Kim, H.J.; Konczalik, P.; Lesma, E.A.; Okazaki, I.J.; Park, M.; Shoemaker, M.; Stevens, L.A.; Zolkiewska, A.
Characterization of NAD:arginine ADP-ribosyltransferases
Mol. Cell. Biochem.
193
109-113
1999
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Davis, T.; Sabir, J.S.M.; Tavassoli, M.; Shall, S.
Purification, characterization, and molecular cloning of a chicken erythroblast mono(ADP-ribosyl)transferase
Adv. Exp. Med. Biol.
419
145-154
1997
Gallus gallus
brenda
Wang, J.; Nemoto, E.; Dennert, G.
Regulation of cytotoxic T cell functions by a GPI-anchored ecto-ADP-ribosyltransferase
Adv. Exp. Med. Biol.
419
191-201
1997
Mus musculus
brenda
Tsuchiya, M.; Osago, H.; Yamada, K.; Shimoyama, M.
A newly identified glycosylphosphatidylinositol-anchored arginine-specific ADP-ribosyltransferase in chicken spleen
Adv. Exp. Med. Biol.
419
245-248
1997
Gallus gallus
brenda
Okazaki, I.J.; Kim, H.J.; Moss, J.
Molecular cloning and characterization of lymphocyte and muscle ADP-ribosyltransferases
Adv. Exp. Med. Biol.
419
129-136
1997
Homo sapiens, Mus musculus, Oryctolagus cuniculus
brenda
Hara, N.; Badruzzaman, M.; Sugae, T.; Shimoyama, M.; Tsuchiya, M.
Mouse Rt6.1 is a thiol-dependent arginine-specific ADP-ribosyltransferase cysteine 201 confers thiol sensitivity on the enzyme
Eur. J. Biochem.
259
289-294
1999
Mus musculus
brenda
Taniguchi, M.; Tsuchiya, M.; Shimoyama, M.
Comparison of acceptor protein specificities on the formation of ADP-ribose.acceptor adducts by arginine-specific ADP-ribosyltransferase from rabbit skeletal muscle sarcoplasmic reticulum with those of the enzyme from chicken peripheral polymorphonuclear cells
Biochim. Biophys. Acta
1161
265-271
1993
Gallus gallus, Oryctolagus cuniculus
brenda
Sakurai, J.; Nagahama, M.; Hisatsune, J.; Katunuma, N.; Tsuge, H.
Clostridium perfringens i-toxin, ADP-ribosyltransferase: structure and mechanism of action
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43
361-377
2003
Clostridium perfringens
brenda
Terashima, M.; Osago, H.; Hara, N.; Tanigawa, Y.; Shimoyama, M.; Tsuchiya, M.
Purification, characterization and molecular cloning of glycosylphosphatidylinositol-anchored arginine-specific ADP-ribosyltransferases from chicken
Biochem. J.
389
853-861
2005
Gallus gallus (Q49L19), Gallus gallus (Q49L21)
brenda
Carpusca, I.; Schirmer, J.; Aktories, K.
Two-site autoinhibition of the ADP-ribosylating mosquitocidal toxin (MTX) from Bacillus sphaericus by its 70-kDa ricin-like binding domain
Biochemistry
43
12009-12019
2004
Lysinibacillus sphaericus
brenda
Stevens, L.A.; Bourgeois, C.; Bortell, R.; Moss, J.
Regulatory role of arginine 204 in the catalytic activity of rat alloantigens ART2a and ART2b
J. Biol. Chem.
278
19591-19596
2003
Rattus norvegicus
brenda
Krebs, C.; Adriouch, S.; Braasch, F.; Koestner, W.; Leiter, E.H.; Seman, M.; Lund, F.E.; Oppenheimer, N.; Haag, F.; Koch-Nolte, F.
CD38 controls ADP-ribosyltransferase-2-catalyzed ADP-ribosylation of T cell surface proteins
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174
3298-3305
2005
Mus musculus
brenda
Vogelsgesang, M.; Aktories, K.
Exchange of glutamine-217 to glutamate of Clostridium limosum exoenzyme C3 turns the asparagine-specific ADP-ribosyltransferase into an arginine-modifying enzyme
Biochemistry
45
1017-1025
2006
Hathewaya limosa
brenda
Friedrich, M.; Grahnert, A.; Klein, C.; Tschoep, K.; Engeland, K.; Hauschildt, S.
Genomic organization and expression of the human mono-ADP-ribosyltransferase ART3 gene
Biochim. Biophys. Acta
1759
270-280
2006
Homo sapiens (Q5J1L0), Homo sapiens (Q5J1P8), Homo sapiens (Q5J1Q0)
brenda
Paone, G.; Stevens, L.A.; Levine, R.L.; Bourgeois, C.; Steagall, W.K.; Gochuico, B.R.; Moss, J.
ADP-ribosyltransferase-specific modification of human neutrophil peptide-1
J. Biol. Chem.
281
17054-17060
2006
Homo sapiens, Mus musculus
brenda
Zheng, X.; Morrison, A.R.; Chung, A.S.; Moss, J.; Bortell, R.
Substrate specificity of soluble and membrane-associated ADP-ribosyltransferase ART2.1
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98
851-860
2006
Mus musculus
brenda
Banasik, M.; Stedeford, T.; Strosznajder, R.P.; Hsu, C.H.; Tanaka, S.; Ueda, K.
Differential effects of heterocyclic amines on poly(ADP-ribose) polymerase-1 and mono-ADP-ribosyltransferase A
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15-22
2006
Meleagris sp.
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The orthologue of the "acatalytic" mammalian ART4 in chicken is an arginine-specific mono-ADP-ribosyltransferase
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86
2008
Homo sapiens, Gallus gallus (B6RDZ5), Gallus gallus
brenda
Friedrich, M.; Boehlig, L.; Kirschner, R.D.; Engeland, K.; Hauschildt, S.
Identification of two regulatory binding sites which confer myotube specific expression of the mono-ADP-ribosyltransferase ART1 gene
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91
2008
Mus musculus
brenda
Terashima, M.; Takahashi, M.; Shimoyama, M.; Tanigawa, Y.; Urano, T.; Tsuchiya, M.
Glycosylphosphatidylinositol-anchored arginine-specific ADP-ribosyltransferase7.1 (Art7.1) on chicken B cells: the possible role of Art7 in B cell receptor signalling and proliferation
Mol. Cell. Biochem.
320
93-100
2009
Gallus gallus
brenda
Stilla, A.; Di Paola, S.; Dani, N.; Krebs, C.; Arrizza, A.; Corda, D.; Haag, F.; Koch-Nolte, F.; Di Girolamo, M.
Characterisation of a novel glycosylphosphatidylinositol-anchored mono-ADP-ribosyltransferase isoform in ovary cells
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90
665-677
2011
Cricetulus griseus
brenda
Koehler, C.; Carlier, L.; Veggi, D.; Balducci, E.; Di Marcello, F.; Ferrer-Navarro, M.; Pizza, M.; Daura, X.; Soriani, M.; Boelens, R.; Bonvin, A.M.
Structural and biochemical characterization of NarE, an iron-containing ADP-ribosyltransferase from Neisseria meningitidis
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286
14842-14851
2011
Neisseria meningitidis
brenda
Karlberg, T.; Thorsell, A.G.; Kallas, A.; Schueler, H.
Crystal structure of human ADP-ribose transferase ARTD15/PARP16 reveals a novel putative regulatory domain
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287
24077-24081
2012
Homo sapiens (Q8N5Y8), Homo sapiens
brenda
Di Paola, S.; Micaroni, M.; Di Tullio, G.; Buccione, R.; Di Girolamo, M.
PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-ss1
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7
e37352
2012
Homo sapiens (Q8N5Y8), Homo sapiens
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Schwarz, N.; Drouot, L.; Nicke, A.; Fliegert, R.; Boyer, O.; Guse, A.H.; Haag, F.; Adriouch, S.; Koch-Nolte, F.
Alternative splicing of the N-terminal cytosolic and transmembrane domains of P2X7 controls gating of the ion channel by ADP-ribosylation
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2012
Homo sapiens
brenda
Castagnini, M.; Picchianti, M.; Talluri, E.; Biagini, M.; Del Vecchio, M.; Di Procolo, P.; Norais, N.; Nardi-Dei, V.; Balducci, E.
Arginine-specific mono ADP-ribosylation in vitro of antimicrobial peptides by ADP-ribosylating toxins
PLoS ONE
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2012
Neisseria meningitidis, Vibrio cholerae serotype O1
brenda
Mauss, S.; Chaponnier, C.; Just, I.; Aktories, K.; Gabbiani, G.
ADP-ribosylation of actin isoforms by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin
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194
237-241
1990
Clostridium botulinum, Clostridium perfringens (Q46220), Clostridium perfringens
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Vandekerckhove, J.; Schering, B., Brmann, M.; Aktories, K.
Clostridium perfringens iota toxin ADP-ribosylates skeletal muscle actin in Arg-177
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225
48-52
1987
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Mus musculus
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