Information on EC 2.4.2.31 - NAD+-protein-arginine ADP-ribosyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, dsDNA viruses, no RNA stage

EC NUMBER
COMMENTARY
2.4.2.31
-
RECOMMENDED NAME
GeneOntology No.
NAD+-protein-arginine ADP-ribosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
NAD+ + protein L-arginine = nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
show the reaction diagram
rapid equilibrium random sequential mechanism
-
NAD+ + protein L-arginine = nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
NAD+:protein-L-arginine ADP-D-ribosyltransferase
Protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in the regulation of cellular activities [4]. Arginine residues in proteins act as acceptors. Free arginine, agmatine [(4-aminobutyl)guanidine], arginine methyl ester and guanidine can also do so. The enzyme from some, but not all, species can also use NADP+ as acceptor (giving rise to Nomega-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine as the product), but more slowly [1,5]. The enzyme catalyses the NAD+-dependent activation of EC 4.6.1.1, adenylate cyclase. Some bacterial enterotoxins possess similar enzymic activities. (cf. EC 2.4.2.36 NAD+---diphthamide ADP-ribosyltransferase).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-arginine
-
-
-
-
ADP-ribosyltransferase
-
-
-
-
ADP-ribosyltransferase
-
-
ADP-ribosyltransferase
-
-
ADP-ribosyltransferase-2
-
-
ADPRT
-
-
-
-
alloantigen Rt6.1
-
-
-
-
alloantigen Rt6.2
-
-
-
-
arginine specific ADP-ribosyltransferase
-
-
-
-
arginine specific mono-ADP-ribosyltransferase
-
-
-
-
arginine-specific ADP-ribosyltransferase
-
-
arginine-specific mono-ADP-ribosyltransferase
-
-
-
-
arginine-specific mono-ADP-ribosyltransferase
B6RDZ5
-
arginine-specific mono-ADP-ribosyltransferase
-
-
arginine-specific mono-ADP-ribosyltransferase A
Meleagris sp.
-
-
ART
-
-
-
-
ART
Q49L19, Q49L21
-
ART1
-
-
ART2
-
-
ART3
-
-
ART4
B6RDZ5
-
ART4
-
-
ART5
-
-
Art7.1
-
-
Art7.2
-
-
ARTD15
Q8N5Y8
-
ARTD15/PARP16
Q8N5Y8
-
asparagine-specific ADP-ribosyltransferase
-
-
AT1
-
-
-
-
AT2
-
-
-
-
cARTC2.1
-
bi-functional: NAD-glycohydrolase and arginine-specific ADP-ribosyltransferase activities
cholera toxin
-
-
Dombrock blood group carrier molecule
-
-
-
-
exoenzyme C3
-
-
glycosylphosphatidylinositol-anchored arginine-specific ADP-ribosyltransferase7.1
-
-
MART-A
Meleagris sp.
-
-
mono(ADP-ribosyl)transferase
-
-
-
-
mono-ADP-ribosyltransferase
Q5J1L0, Q5J1P0, Q5J1P8
-
mono-ADP-ribosyltransferase
-
-
mono-ADP-ribosyltransferase A
Meleagris sp.
-
-
NAD(P)+-arginine ADP-ribosyltransferase
-
-
-
-
NAD+:arginine ADP-ribosyltransferase
-
-
-
-
NAD+:arginine ecto-mono(ADP-ribosyl)transferase
-
-
-
-
NAD+:L-arginine ADP-D-ribosyltransferase
-
-
-
-
NAD-arginine ADP-ribosyltransferase
-
-
-
-
NAD-arginine mono-ADP-ribosyltransferase B
-
-
-
-
NAD-dependent ADPribosyltransferase
-
-
-
-
NAD:arginine ADP-ribosyltransferase
-
-
NAD:arginine ADP-ribosyltransferase B
-
-
-
-
PARP16/ARTD15
Q8N5Y8
-
RT6
-
-
-
-
RT6.1
-
-
-
-
RT6.2
-
-
-
-
T-cell surface protein Rt6.1
-
-
-
-
T-cell surface protein Rt6.2
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
81457-93-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Coturnix sp.
-
-
-
Manually annotated by BRENDA team
Escherichia coli B/r infected with phage T4
-
-
Manually annotated by BRENDA team
2 enzyme forms: AT1 and AT2
-
-
Manually annotated by BRENDA team
isoform Art1
Swissprot
Manually annotated by BRENDA team
isoform Art2
Swissprot
Manually annotated by BRENDA team
ART3, fragment; gene ART3, two splicing variants different in the 5'-UTR
SwissProt
Manually annotated by BRENDA team
ART3, fragments; gene ART3, two splicing variants different in the 5'-UTR
SwissProt
Manually annotated by BRENDA team
isozymes ART1, ART3, ART4, and ART5
-
-
Manually annotated by BRENDA team
Meleagris sp.
-
-
-
Manually annotated by BRENDA team
BALB/c and C57BL/6 mice, isozyme ART2
-
-
Manually annotated by BRENDA team
isozyme ART2
-
-
Manually annotated by BRENDA team
isozymes ART1, ART2.2, and ART5
-
-
Manually annotated by BRENDA team
2 enzyme forms: enzyme type alpha and enzyme type beta
-
-
Manually annotated by BRENDA team
isoforms ART2a and ART2b, expression in rat mammary adenocarcinoma cells
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
B6RDZ5
avian orthologue of the acatalytic mammalian ART4 is a mono-ADP-ribosyltransferase with enzymatic activity comparable to that of other, catalytically active and glycosyl-phosphatidylinositol-anchored members of the mammalian ART family
physiological function
-
in contrast to its avian orthologue the mammalian ART4 is a acatalytic mono-ADP-ribosyltransferase
physiological function
-
expression of Art7.1 molecules on B-cells can modulate the B cell receptor signalling and direct the B-cell fate to maturation
physiological function
-
ADP-ribosylation of the P2X7(k) but not the P2X7(a) variant induces stable Ca2+ signals
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
A1 peptide of cholera toxin + NAD+
nicotinamide + ?
show the reaction diagram
-
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 + ?
show the reaction diagram
-
no activity with the enzyme from skeletal muscle sarcoplasmic reticulum
-
-
-
actin + NAD+
nicotinamide + ?
show the reaction diagram
-
non-muscle beta/gamma actin, skeletal muscle alpha actin, smooth muscle gamma actin
-
-
?
actin + NAD+
nicotinamide + ?
show the reaction diagram
-
alpha-actin and beta/gamma-actin
-
-
?
actin + NAD+
nicotinamide + ?
show the reaction diagram
-
the ADP ribosylation of actin in the heterophils may be involved in the cellular processes such as phagocytosis, secretion and migration
-
-
-
actin + NAD+
nicotinamide + ?
show the reaction diagram
Q49L19, Q49L21
2% of the activity with p33
-
-
?
actin + NAD+
nicotinamide + ?
show the reaction diagram
Q49L19, Q49L21
3% of the activity with p33
-
-
?
agmatine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
-
agmatine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
-
agmatine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
agmatine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
agmatine + NAD+
nicotinamide + ?
show the reaction diagram
P70352
-
-
-
-
agmatine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
-
agmatine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
-
agmatine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
arginine + NAD+
nicotinamide + ADP-ribose-L-arginine
show the reaction diagram
-
-
-
-
?
arginine methyl ester + NAD+
nicotinamide + N2-(ADP-D-ribosyl)-L-arginine
show the reaction diagram
-
-
-
?
arginine methyl ester + NAD+
nicotinamide + N2-(ADP-D-ribosyl)-L-arginine
show the reaction diagram
-
-
-
-
?
arginine methyl ester + NADP+
nicotinamide phosphate + N2-(ADP-D-ribosyl)-L-arginine
show the reaction diagram
-
-
-
-
?
basic fibroblast growth factor FGF-2 + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
beta-lactoglobulin + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
bovine plasma albumin + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
bovine serum albumin + NAD+
nicotinamide + ?
show the reaction diagram
-
poor ADP-ribose acceptor
-
-
?
casein + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
casein + NAD+
nicotinamide + ?
show the reaction diagram
Q49L19, Q49L21
8% of the activity with p33
-
-
?
diethylamino-(benzylidineamino)guanidine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
DNase I + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
FGF-2 + NAD+
?
show the reaction diagram
-
ADP-ribosylation of FGF-2 may provide an additional level of control of FGF-2 activity
-
-
-
guanidine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
guanidinobutyrate + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
guanidinopropionate + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
histone + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
-
histone + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
histone + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
histone + NAD+
nicotinamide + ?
show the reaction diagram
Q49L19, Q49L21
130% of the activity with p33
-
-
?
histone + NAD+
nicotinamide + ?
show the reaction diagram
Q49L19, Q49L21
67% of the activity with p33
-
-
?
histone + NAD+
Nomega-[(2'-phospho-ADP)-D-ribosyl]-histone-L-arginine + nicotinamide + H+
show the reaction diagram
-
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 + ?
show the reaction diagram
-
-
-
-
?
histone f2a + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
histone f2b + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
histone f3 + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
histone H2B + NAD+
Nomega-[(2'-phospho-ADP)-D-ribosyl]-histone H2B-L-arginine + nicotinamide
show the reaction diagram
Meleagris sp.
-
-
-
-
?
human alpha-defensin-1 + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
human alpha-defensin-1 + NAD+
nicotinamide + ?
show the reaction diagram
-
poorly recognised substrate
-
-
?
human alpha-globulin + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
human beta-defensin-1 + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
human beta-globulin + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
human gamma-globulin + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
human neutrophil peptide-1 + NAD+
Nomega-(ADP-D-ribosyl)-L-arginine-human neutrophil peptide-1 + nicotinamide
show the reaction diagram
-
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
show the reaction diagram
-
human neutrophil peptide-1, HNP-1, from neutrophil cell surface, isozyme ART1 is active on Arg14 and Arg24
-
-
?
human neutrophil peptide-1 + NAD+
Nomega-(ADP-D-ribosyl)-L-arginine-human neutrophil peptide-1 + nicotinamide
show the reaction diagram
-
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
-
-
?
karyopherin-beta1 + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
lysozyme + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
show the reaction diagram
-
agmatine as ADPribose acceptor is used
-
-
?
ovalbumin + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
ovalbumin + NAD+
nicotinamide + ?
show the reaction diagram
-
poor ADP-ribose acceptor
-
-
?
p-nitrobenzylidine aminoguanidine + NAD+
nicotinamide + mono-ADP-ribosylated p-nitrobenzylidine aminoguanidine
show the reaction diagram
-
-
-
?
P2X7 purinoceptor protein + NAD+
Nomega-[(2'-phospho-ADP)-D-ribosyl]-P2X7 purinoceptor protein-L-arginine + nicotinamide
show the reaction diagram
-
isozyme ART2
-
-
?
P2X7(k) + NAD+
nicotinamide + ?
show the reaction diagram
-
the P2X7(k) variant is sensitive to activation by ADP-ribosylation whereas the P2X7(a) variant is insensitive
-
-
?
P33 + NAD+
nicotinamide + ?
show the reaction diagram
-
preferential endogenous acceptor
-
-
?
P33 + NAD+
nicotinamide + ?
show the reaction diagram
-
no activity with the enzyme from skeletal muscle sarcoplasmic reticulum
-
-
-
p33 protein + NAD+
nicotinamide + ?
show the reaction diagram
Q49L19, Q49L21
-
-
-
?
polyarginine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
-
polyarginine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
polyarginine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
polyarginine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
ir
polyarginine + NAD+
nicotinamide + ?
show the reaction diagram
B6RDZ5
in contrast to its mammalian orthologues, the chicken protein contains an intact R-S-EXE motif
-
-
?
polylysine + NAD+
nicotinamide + ?
show the reaction diagram
-
poor ADP-ribose acceptor
-
-
?
Ras + NAD+
nicotinamide + ?
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme modifies the low-molecular-mass GTPase RhoA specifically at Asn41
-
-
?
RhoB + NAD+
Nomega-(ADP-D-ribosyl)-L-asparagine41-RhoB + nicotinamide
show the reaction diagram
-
the enzyme modifies the low-molecular-mass GTPase RhoB specifically at Asn41
-
-
?
soy bean trypsin inhibitor + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
soybean trypsin inhibitor + NAD+
Nomega-(ADP-D-ribosyl)-L-arginine-soybean trypsin inhibitor + nicotinamide
show the reaction diagram
-
-
-
-
?
trypsin inhibitor + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
wild-type exoenzyme C3 + NAD+
Nomega-(ADP-D-ribosyl)-L-arginine86-wild-type exoenzyme C3 + nicotinamide
show the reaction diagram
-
the recombinant mutant Q217E enzyme modifies the recombinant wild-type enzyme at Arg86
-
-
?
lysozyme + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
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, 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, beta-defensin-1 is a poor substrate, overview
-
-
-
additional information
?
-
-
substrate specificity, human neutrophil peptide-1 is a poor substrate of isozymes ART2.2 and ART5, overview
-
-
-
additional information
?
-
-
the enzyme exhibits ADP-ribosyltransferase and NAD+ glycohydrolase activity, modeling of interaction od substrate and catalytic residues, overview
-
-
-
additional information
?
-
Meleagris sp.
-
the enzyme is involved in signal transduction and cytoskeletal realignment
-
-
-
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
?
-
-
no activity with NAD+ as substrate
-
-
-
additional information
?
-
-
NarE undergoes auto-ADP-ribosylation
-
-
-
RhoC + NAD+
Nomega-(ADP-D-ribosyl)-L-asparagine41-RhoC + nicotinamide
show the reaction diagram
-
the enzyme modifies the low-molecular-mass GTPase RhoC specifically at Asn41
-
-
?
RNA polymerase + NAD+
additional information
-
-
E. coli RNA polymerase
-
-
-
RNA polymerase + NAD+
additional information
-
-
alpha-subunit of RNA polymerase
the amino acid carrying the ADP-ribosyl residue appears to be arginine
ir
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
actin + NAD+
nicotinamide + ?
show the reaction diagram
-
the ADP ribosylation of actin in the heterophils may be involved in the cellular processes such as phagocytosis, secretion and migration
-
-
-
FGF-2 + NAD+
?
show the reaction diagram
-
ADP-ribosylation of FGF-2 may provide an additional level of control of FGF-2 activity
-
-
-
histone + NAD+
Nomega-[(2'-phospho-ADP)-D-ribosyl]-histone-L-arginine + nicotinamide + H+
show the reaction diagram
-
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
-
-
?
human neutrophil peptide-1 + NAD+
Nomega-(ADP-D-ribosyl)-L-arginine-human neutrophil peptide-1 + nicotinamide
show the reaction diagram
-
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
-
-
?
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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
-
NAD+ is preferred over NADP+, NAD:arginine ADP-ribosyltransferase A
NADP+
-
NAD+ is preferred over NADP+, NAD:arginine ADP-ribosyltransferase A
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe2+
-
enzyme binds iron through a Fe-S center, which is crucial for the catalytic activity
NaCl
-
activates AT2 transferase
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,2-naphthoquinone
-
-
1,4-Naphthoquinone
-
-
2-mercaptoethanol
-
marked decrease in activity, NAD+ and dithiothreitol protects
3-amino-1,4-dimethyl-5H-pyrido[4,3-b]indole
Meleagris sp.
-
i.e. Trp-P-1, 53% inhibition at 5 mM, IC50: 2.8 mM
4-amino-1-naphthol
-
-
5,8-Dihydroxy-1,4-naphthoquinone
-
-
ADP-ribose
-
partial competitive inhibition
AMP
-
7.8 mM, decreases activity to 78% of the uninhibited control
beta-NMN
Q49L19, Q49L21
50% inhibition at 0.021 mM; 50% inhibition at 0.35 mM
beta-NMN
-
specific Art7.2 inhibitor, beta-NMN does not inhibit Art activities on both thymocytes and bursal cells by the addition of 0.1 mM, thus expressed Art proteins on these cells are Art7.1
CD38
-
CD38, a potent ecto-NAD-glycohydrolase, controls ADP-ribosyltransferase-2-catalyzed ADP-ribosylation of T cell surface proteins, CD38 decreases ART2-catalyzed ADP-ribosylation in trans by reducing the amount of ART substrate NAD+
-
dithiothreitol
-
20% inhibition by 5 mM, 25% inhibition by 10 mM
human alpha-defensin-1
-
-
-
human neutrophil peptide-1
-
substrate inhibition of isozymes ART1 and ART5
-
human neutrophil peptide-1
-
substrate inhibition of isozyme ART5
-
K2HPO4
-
IC50: 50 mM
NaCl
-
inhibits AT1 transferase
NaCl
-
IC50: 50 mM
NaCl
-
IC50: 100 mM
NaCl
Q49L19, Q49L21
50% inhibition at 125 mM; 50% inhibition at 278 mM
NEM
-
inhibition of RT6.1, no affect on Rt6.2 and Glu207 mutant of RR6.1
novobiocin
-
IC50: 0.2 mM
novobiocin
-
IC50: 0.4 mM
Triton X-100
-
detergent solubilization of cell membranes specifically abolishes ADP-ribosylation of high MW histones
K2HPO4
-
IC50: 40 mM
additional information
-
activation of enzyme by proteolytic cleaveage releasing the active enzyme, amino acids 30-264, and a 70 kDa C-terminal fragment. In solution, the fragment is still a potent inhibitor of enzyme activity. Amino acids D273 and D275 are essential for inhibitory effect. Peptide 265-285 increases the Km-value for NAD. Two-site binding model for inhibition
-
additional information
Meleagris sp.
-
comparison of the effects of heterocyclic amines acting as potent carcinogens on poly(ADP-ribose) polymerase-1, PARP-1, EC 2.4.2.30, and the arginine-specific mono-ADP-ribosyltransferase A, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
required by AT1 transferase, activates AT2 transferase
3-amino-1-methyl-5H-pyrido[4,3-b]indole
Meleagris sp.
-
i.e. Trp-P-2, 71% activation at 3 mM
App(NH)p
-
10 mM, stimulates
ATP
-
half-maximal stimulation with 2.5 mM
Br-
-
activates NAD:arginine ADP-ribosyltransferase A
CHAPS
-
activates; enhances activity
Cl-
-
activates NAD:arginine ADP-ribosyltransferase A, NaCl is maximally effective at 250 mM
dithiothreitol
-
activity of RT6.1 increases fivefold, no effect on activity of RT6.2. Cys201 confers thiol sensitivity
DNA
-
enhances activity
DTT
-
dependent on, the DTT cencentration influences the target specificity of ART2
F-
-
activates NAD:arginine ADP-ribosyltransferase A
GTP
-
10 mM, stimulates
Histone
-
increases activity in absence of salt
human alpha-defensin-1
-
strongly influences NarE by inhibiting its transferase activity while enhancing its auto-ADP-ribosylation
-
lysolecithin
-
stimulates 4-6fold in the order of declining effectiveness: C14, C12, C10, C8
PO43-
-
activates NAD:arginine ADP-ribosyltransferase A
SCN-
-
activates NAD:arginine ADP-ribosyltransferase A, NaSCN is maximally effective at 100 mM
Tetrapolyphosphate
-
10 mM, stimulates
tripolyphosphate
-
10 mM, stimulates
Triton X-100
-
enhances activity
Triton X-114
-
enhances activity
Triton X-305
-
enhances activity
-
Tween 20
-
enhances activity
lysophosphatidylcholine
-
increases activity in the order of declining effectiveness C18, C16, C14, C12, C10, C8, NAD:arginine ADP-ribosyltransferase A
additional information
-
more than 85% of the enzyme activity is lost within 1 min Vortex-mixing at room temperature of dilute enzyme. When the less-active form of the enzyme is treated with 10 mM dithiothreitol plus 0.2 M NaCl under anaerobic conditions, more than 50% of the enzyme activity is restored
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.26
-
1-(4-aminobutyl)guanidine
-
-
15
-
1-(4-aminobutyl)guanidine
-
enzyme Yac-2
2
-
agmatine
-
NAD:arginine ADP-ribosyltransferase A
9.4
-
agmatine
-
enzyme Yac-1
0.0025
-
alpha-Actin
-
-
-
1.3
-
Arginine methyl ester
-
in presence of 250 mM NaCl, NAD:arginine ADP-ribosyltransferase A
3
-
Arginine methyl ester
-
-
3
-
Arginine methyl ester
-
NAD:arginine ADP-ribosyltransferase B
0.015
-
beta/gamma-actin
-
-
-
0.01
-
gamma-actin
-
-
-
0.0007
-
NAD+
B6RDZ5
recombinant ART4, in the presence of PNGase F
0.001
-
NAD+
B6RDZ5
recombinant ART4
0.014
-
NAD+
-
in presence of lysolecithin
0.015
-
NAD+
-
NAD:arginine ADP-ribosyltransferase A
0.015
-
NAD+
-
NAD:arginine ADP-ribosyltransferase C
0.02
-
NAD+
-
reaction with gamma-actin
0.025
-
NAD+
-
in presence of NaCl
0.03
-
NAD+
-
reaction with beta/gamma-actin
0.035
-
NAD+
-
reaction with alpha-actin
0.036
-
NAD+
-
NAD:arginine ADP-ribosyltransferase B
0.0403
-
NAD+
-
pH 7.4, absence of peptide 265-285
0.1
-
NAD+
-
-
0.118
-
NAD+
-
reaction with 20 mM agmatine, enzyme Yac-1
0.13
-
NAD+
-
-
0.142
-
NAD+
-
reaction with 20 mM agmatine, enzyme Yac-2
0.267
-
NAD+
-
pH and temperature not specified in the publication
0.29
-
NAD+
-
37C, pH not specified in the publication
1.133
-
NAD+
-
pH 7.4, presence of peptide 265-285
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6.2
-
NAD+
-
pH 7.4, absence of peptide 265-285
10.6
-
NAD+
-
pH 7.4, presence of peptide 265-285
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0049
-
1,4-Naphthoquinone
-
-
0.37
-
Nicotinamide
-
-
4
-
Nicotinamide
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.8
-
3-amino-1,4-dimethyl-5H-pyrido[4,3-b]indole
Meleagris sp.
-
i.e. Trp-P-1, 53% inhibition at 5 mM, IC50: 2.8 mM
40
-
K2HPO4
-
IC50: 40 mM
50
-
K2HPO4
-
IC50: 50 mM
50
-
NaCl
-
IC50: 50 mM
100
-
NaCl
-
IC50: 100 mM
0.2
-
novobiocin
-
IC50: 0.2 mM
0.4
-
novobiocin
-
IC50: 0.4 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.6
-
-
NAD:arginine ADP-ribosyltransferase C
53
-
-
NAD:arginine ADP-ribosyltransferase B
353
-
-
NAD:arginine ADP-ribosyltransferase A
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
easy assay procedure
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
8.5
Coturnix sp.
-
-
7
-
Meleagris sp.
-
assay at
7.4
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.6
-
-
assay at
8.5
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
pH 6: about 50% of maximal activity, pH 9: about 80% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
37
-
assay at
30
-
-
assay at
30
-
Meleagris sp.
-
assay at
30
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
37
-
20C: optimum, 37C: about 35% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
aortic arch endothelium
Manually annotated by BRENDA team
Q49L19, Q49L21
predominantly
Manually annotated by BRENDA team
B6RDZ5
high level
Manually annotated by BRENDA team
B6RDZ5
very low level
Manually annotated by BRENDA team
-
Art7.1, but not Art7.2, is predominant on the surface of B-cells from the bursa of Fabricius as a glycosylphosphatidylinositol-anchored form
Manually annotated by BRENDA team
-
ART1, ART3 and ART5 present in myotubes, absent, with the exception of ART3, from myoblasts
Manually annotated by BRENDA team
-
ART1, ART3 and ART5 present in myotubes. Absent from mesenchymal progenitor cells and, with the exception of ART3, in myoblasts
Manually annotated by BRENDA team
-
epithelial cells lining human airways and cells, isozyme ART1, bronchoalveolar lavage fluid
Manually annotated by BRENDA team
-
very low activity
Manually annotated by BRENDA team
Meleagris sp.
-
-
Manually annotated by BRENDA team
-
low level
Manually annotated by BRENDA team
-
peripheral polymorphonuclear
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
Q49L19, Q49L21
;
Manually annotated by BRENDA team
Q5J1L0, Q5J1P0, Q5J1P8
-
Manually annotated by BRENDA team
-
Art7.1 and Art7.2
Manually annotated by BRENDA team
Q49L19, Q49L21
-
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
-
low level
Manually annotated by BRENDA team
B6RDZ5
high level
Manually annotated by BRENDA team
-
low level
Manually annotated by BRENDA team
Q49L19, Q49L21
predominantly
Manually annotated by BRENDA team
-
Art7.1 and Art7.2
Manually annotated by BRENDA team
Q49L19, Q49L21
-
Manually annotated by BRENDA team
Q5J1L0, Q5J1P0, Q5J1P8
-
Manually annotated by BRENDA team
-
low level
Manually annotated by BRENDA team
Q49L19, Q49L21
predominantly
Manually annotated by BRENDA team
B6RDZ5
high level
Manually annotated by BRENDA team
-
from BALB/c mouse
Manually annotated by BRENDA team
-
surface of mature T-lymphocytes
Manually annotated by BRENDA team
-
splenic lymphocyte subpopulations, ART2 is a T-cell-specific transferase, expression of CD38 and ART2 is inversely correlated on murine lymphocytes
Manually annotated by BRENDA team
-
ART2 is a T-cell-specific transferase
Manually annotated by BRENDA team
-
Art7.1, but not Art7.2, is predominant on T-cells
Manually annotated by BRENDA team
B6RDZ5
very low level
Manually annotated by BRENDA team
Q5J1L0, Q5J1P0, Q5J1P8
-
Manually annotated by BRENDA team
Q5J1L0, Q5J1P0, Q5J1P8
-
Manually annotated by BRENDA team
additional information
Q5J1L0, Q5J1P0, Q5J1P8
tissue distribution and expression pattern; tissue distribution and expression pattern; tissue distribution and expression pattern
Manually annotated by BRENDA team
additional information
B6RDZ5
very low level in caecum, absent from lung
Manually annotated by BRENDA team
additional information
-
very low level of Art7.1 in DT40 cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
on epithelial cells lining human airways and cells, isozyme ART1
Manually annotated by BRENDA team
-
ART2 is attached to the cell surface by a glycosylphosphatidylinositol anchor in T-cells
Manually annotated by BRENDA team
-
anchored to membranes by glycosylphosphatidylinositol
Manually annotated by BRENDA team
-
glycosylphosphatidylinositol-anchored membrane protein
Manually annotated by BRENDA team
P70352
glycosylphosphatidylinositol-anchored membrane protein; Yac-2 enzyme is membrane-bound but appears not to be glycosylphosphatidylinositol-anchored
Manually annotated by BRENDA team
-
glycosylphosphatidylinositol-anchored membrane protein
Manually annotated by BRENDA team
-
the enzyme is likely to be linked to the cell surface via a glycosylphosphatidylinositol
Manually annotated by BRENDA team
-
anchored to membranes by glycosylphosphatidylinositol
Manually annotated by BRENDA team
-
anchored to membranes by glycosylphosphatidylinositol
Manually annotated by BRENDA team
-
anchored to membranes by glycosylphosphatidylinositol; Yac-1 enzyme is anchored to membranes by glycosylphosphatidylinositol; Yac-2 enzyme is membrane-bound but appears not to be glycosylphosphatidylinositol-anchored
Manually annotated by BRENDA team
-
anchored to membranes by glycosylphosphatidylinositol
Manually annotated by BRENDA team
-
anchored to membranes by glycosylphosphatidylinositol
Manually annotated by BRENDA team
Q49L19, Q49L21
glycosyl-phosphatidylinositol-anchored protein; glycosyl-phosphatidylinositol-anchored protein
Manually annotated by BRENDA team
-
membranes of the nuclear envelope
Manually annotated by BRENDA team
-
98% of NAD:arginine ADP-ribosyltransferase A is located to the nucleus
Manually annotated by BRENDA team
-
NAD:arginine ADP-ribosyltransferase C is enriched 11fold in membranes over nuclei
Manually annotated by BRENDA team
additional information
P70352
Yac-1 enzyme may have a signal peptide and may be secreted
-
Manually annotated by BRENDA team
additional information
-
the enzyme displays a hydrophobic amino terminus consistent with a signal sequence, but lacks a hydrophobic signal sequence at its carboxyl terminus suggesting that the protein is destined for export
-
Manually annotated by BRENDA team
additional information
-
the membrane or solution environment of ART2 plays a pivotal role in determining its substrate specificity
-
Manually annotated by BRENDA team
additional information
B6RDZ5
upon ectopic expression in C-33A cells, recombinant chicken ART4 localizes at the cell surface as a glycosyl-phosphatidylinositol-anchored, highly glycosylated protein, which displays arginine-specific ART activity
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25300
-
-
NAD:arginine ADP-ribosyltransferase A, gel filtration
25500
-
-
NAD:arginine ADP-ribosyltransferase A, gel filtration
26000
-
-
NAD:arginine ADP-ribosyltransferase C, gel filtration
26000
-
-
gel filtration
27500
-
-
gel filtration
31000
-
-
calculated from cDNA
32000
-
-
gel filtration
50000
-
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 28300, SDS-PAGE
?
-
x * 32000, NAD:arginine ADP-ribosyltransferase B, SDS-PAGE
?
-
x * 38500, enzyme type beta, SDS-PAGE; x * 39000, enzyme type alpha, SDS-PSGE
?
-
x * 36134, calculation from nucleotide sequence
?
-
x * 32000, AT1 transferase, SDS-PAGE; x * 34000, AT2 transferase, SDS-PAGE; x * 35318, AT1 transferase, calculation from nucleotide sequence
?
-
x * 42000, SDS-PAGE under non-reducing conditions; x * 44000, SDS-PAGE under reducing conditions
?
-
x * 27500, SDS-PAGE; x * 40000, SDS-PAGE
?
Q49L19, Q49L21
x * 45000, SDS-PAGE; x * 45000, SDS-PAGE
?
-
x * 50000, SDS-PAGE
monomer
-
x * 32000, SDS-PAGE
monomer
-
1 * 28000, NAD:arginine ADP-ribosyltransferase A, SDS-PAGE
monomer
-
1 * 28000, SDS-PAGE
additional information
-
the enzyme contains an ADP-ribosylating turn-turn motif, i.e. ARTT-motif, with the key residue Q217, that is involved in substrate specificity and recognition
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
activation of enzyme by proteolytic cleavage releasing the active enzyme, amino acids 30-264, and a 70 kDa C-terminal inhibitory fragment
additional information
-
enzyme is glycosylphosphatidylinositol (GPI)-anchored
glycoprotein
-
N-glycosyl modification
additional information
Q49L19, Q49L21
glycosyl-phosphatidylinositol-anchored membrane protein; glycosyl-phosphatidylinositol-anchored membrane protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the crystal structure of human ARTD15/PARP16 is shown. ARTD15 features an alpha-helical domain that packs against its transferase domain without making direct contact with the NAD+-binding crevice or the donor loop
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
unstable during dialysis, loss of activity can be strongly reduced by using buffers containing 40% glycerol
-
more than 85% of the enzyme activity is lost within 1 min Vortex-mixing at room temperature of dilute enzyme. When the less-active form of the enzyme is treated with 10 mM dithiothreitol plus 0.2 M NaCl under anaerobic conditions, more than 50% of the enzyme activity is restored
-
both propylene glycol and NaCl stabilize
-
highly unstable both in routine storage and in assay, can be stabilized by addition of 30-50% glycerol to the storage buffer and by addition of nontransferase protein to the assay
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0-4C, 50 mM sodium phosphate, pH 7.1, 100 mM NaCl, NAD:arginine ADP-ribosyltransferase B, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli by glutathione affinity chromatography, the GST-tag is cleaved off by thrombin
-
;
Q49L19, Q49L21
by affinity chromatography
B6RDZ5
NAD:arginine ADP-ribosyltransferase A; NAD:arginine ADP-ribosyltransferase B
-
NAD:arginine ADP-ribosyltransferase A; NAD:arginine ADP-ribosyltransferase C
-
NAD:arginine ADP-ribosyltransferase B
-
recombinant membrane-bound His-tagged ART2 maltose-binding fusion protein from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, anion echange chromatography, and amylose resin affnity chromataography, the maltose-binding protein is cleaved off
-
enzyme type alpha and enzyme type beta
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of GST-tagged wild-type and mutant enzymes in Escherichia coli
-
expression in Escherichia coli
-
in COS 7 cells transiently transfected with AT1 cDNA activity is detected in the culture medium. In COS 7 cells transfected with AT2 CDNA activity is found in both culture medium and cell lysate
-
N-terminal Flag-tagged ART4 (amino acids 20-270) cloned (Asp718I/XhoI) into the pSecTagB plasmid. HEK-293T cells stably transfected with the plasmid. C-33A cells stably transfected with an expression plasmid containing the sequence of ART4 encoding amino acids 20-289
B6RDZ5
plasmid pcDNA3-Art7.1 transfected into chicken B cell lymphoma DT40 cells
-
expressed in Escherichia coli
-
expression Escherichia coli
-
expression of isozymes ART1, ART3, ART4, ART5, ART2.2 in Escherichia coli, isozyme ART1synthesized in Escherichia coli, glycosylphosphatidylinositol-anchored ART1 released with phosphatidylinositol-specific phospholipase C from transfected NMU cells, or ART1 expressed endogenously on C2C12 myotubes modifiy arginine 14 on HNP-1 with a secondary site on arginine 24
-
gene ART3, DNA and amino acid sequence determination and analysis, structural analysis of the untranslated regions, splicing variants differing in the 5'-UTR, genomic organization, expression analysis, recombinant expression in HEK-293T cells; gene ART3, DNA and amino acid sequence determination and analysis, structural analysis of the untranslated regions, splicing variants differing in the 5'-UTR, genomic organization, expression analysis, recombinant expression in HEK-293T cells; gene ART3, DNA and amino acid sequence determination and analysis, structural analysis of the untranslated regions, splicing variants differing in the 5'-UTR, genomic organization, expression analysis, recombinant expression in HEK-293T cells
Q5J1L0, Q5J1P0, Q5J1P8
wild-type and mutants cloned into the pcDNA3.1/Zeo (+) plasmid, expression in C-33A cells
-
At6-1 and RT6-2 cDNA
-
expression of Art 1 in 293T cells as a recombinant fusion protein with the Fc portion of human IgG1
-
expression of His-tagged ART2 as maltose-binding fusion protein in Escherichia coli strain BL21(DE3), expression of the membrane-bound ART2 in COS1 cells
-
expression of isozymes ART1, ART5, ART2.2 in Escherichia coli, ART1 expressed endogenously on C2C12 myotubes modifies arginine 14 on HNP-1 with a secondary site on arginine 24
-
mutated amplification products transformed into the Escherichia coli DH 5alpha strain. HEK 293-T cells stably transfected with ART1 or ART3
-
Yac-1 and Yac-2 enzymes are expressed as glutathione S-transferase fusion proteins in Escherichia coli
P70352
expressed in Escherichia coli
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Art7.1, but not Art7.2, is predominantly expressed on immune cells
-
mutating the DNA consensus sequence of either the E box or the A/T-rich element results in a nearly complete loss of ART1 promoter inducibility
-
expression of ART1, ART3 and ART5 mRNA in myogenic cell lines during skeletal muscle differentiation in vitro. ART1 expression is restricted to myotube formation. ART5 similar to ART1 mRNA is strongly upregulated during muscle cell differentiation. Upregulation of ART3 mRNA only in C3H10T1/2 cells. Differentiation-dependent upregulation of ART1 mRNA is induced by the binding of myogenin to an E box and of MEF-2 to an A/T-rich element in the proximal promoter region of the ART1 gene
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
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
E111D
-
catalytic activity close to wild-type
E120D
-
catalytic activity highly decreased
R7K
-
catalytic activity highly decreased
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
C80S
-
mutant enzyme of RT6.1 remains thiol-dependent
additional information
-
depletion of CD38 cells results in enhanced levels of cell surface etheno-ADP-ribosylation on CD38 T cells