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

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.2.31
-
RECOMMENDED NAME
GeneOntology No.
NAD+-protein-arginine ADP-ribosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NAD+ + protein L-arginine = nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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).
CAS REGISTRY NUMBER
COMMENTARY hide
81457-93-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Clostridium limosum
-
-
-
Manually annotated by BRENDA team
Coturnix sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Meleagris sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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
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
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 + 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
diethylamino-(benzylidineamino)guanidine + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
DNase I + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
FGF-2 + NAD+
?
show the reaction diagram
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+
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-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
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
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
p33 protein + NAD+
nicotinamide + ?
show the reaction diagram
-
-
-
?
polyarginine + NAD+
nicotinamide + ?
show the reaction diagram
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
Clostridium limosum
-
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
Clostridium limosum
-
the enzyme modifies the low-molecular-mass GTPase RhoB specifically at Asn41
-
-
?
RhoC + NAD+
Nomega-(ADP-D-ribosyl)-L-asparagine41-RhoC + nicotinamide
show the reaction diagram
Clostridium limosum
-
the enzyme modifies the low-molecular-mass GTPase RhoC 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
Clostridium limosum
-
-
-
-
?
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
Clostridium limosum
-
the recombinant mutant Q217E enzyme modifies the recombinant wild-type enzyme at Arg86
-
-
?
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
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
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
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
enzyme binds iron through a Fe-S center, which is crucial for the catalytic activity
Mg2+
Clostridium limosum
-
-
NaCl
-
activates AT2 transferase
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
K2HPO4
NEM
-
inhibition of RT6.1, no affect on Rt6.2 and Glu207 mutant of RR6.1
nicotinamide
novobiocin
theophylline
-
-
thymidine
-
-
Triton X-100
-
detergent solubilization of cell membranes specifically abolishes ADP-ribosylation of high MW histones
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
heparin
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
lysophosphatidylcholine
-
increases activity in the order of declining effectiveness C18, C16, C14, C12, C10, C8, NAD:arginine ADP-ribosyltransferase A
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
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26 - 15
1-(4-aminobutyl)guanidine
1 - 9.4
agmatine
0.0025
alpha-Actin
-
-
-
1.3 - 3
Arginine methyl ester
0.015
beta/gamma-actin
-
-
-
0.01
gamma-actin
-
-
-
0.0007 - 1.133
NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.2 - 10.6
NAD+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0049
1,4-Naphthoquinone
-
-
0.37 - 4
nicotinamide
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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 - 50
K2HPO4
50 - 100
NaCl
0.2 - 0.4
novobiocin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
-
NAD:arginine ADP-ribosyltransferase C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.5
Coturnix sp.
-
-
7
Meleagris sp.
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assay at
7.4
Clostridium limosum
-
assay at
7.6
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
pH 6: about 50% of maximal activity, pH 9: about 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 37
Clostridium limosum
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 37
-
20C: optimum, 37C: about 35% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
aortic arch endothelium
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
-
low level
Manually annotated by BRENDA team
-
peripheral polymorphonuclear
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
-
from BALB/c mouse
Manually annotated by BRENDA team
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Art7.1, but not Art7.2, is predominant on T-cells
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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serum
-
Manually annotated by BRENDA team
-
98% of NAD:arginine ADP-ribosyltransferase A is located to the nucleus
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Salmonella typhimurium
Salmonella typhimurium
Streptomyces scabiei (strain 87.22)
Streptomyces scabiei (strain 87.22)
Vibrio splendidus (strain 12B01)
Vibrio splendidus (strain 12B01)
Vibrio splendidus (strain 12B01)
Vibrio splendidus (strain 12B01)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25300
-
NAD:arginine ADP-ribosyltransferase A, gel filtration
25500
-
NAD:arginine ADP-ribosyltransferase A, gel filtration
27500
-
gel filtration
31000
-
calculated from cDNA
32000
-
gel filtration
50000
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
Clostridium limosum
-
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
COMMENTARY hide
LITERATURE
glycoprotein
-
N-glycosyl modification
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
LITERATURE
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
-
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
-
unstable during dialysis, loss of activity can be strongly reduced by using buffers containing 40% glycerol
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-4C, 50 mM sodium phosphate, pH 7.1, 100 mM NaCl, NAD:arginine ADP-ribosyltransferase B, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography
enzyme type alpha and enzyme type beta
-
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 GST-tagged wild-type and mutant enzymes from Escherichia coli by glutathione affinity chromatography, the GST-tag is cleaved off by thrombin
Clostridium limosum
-
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
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
At6-1 and RT6-2 cDNA
-
expressed in Escherichia coli
expression Escherichia coli
-
expression in Escherichia coli
expression of Art 1 in 293T cells as a recombinant fusion protein with the Fc portion of human IgG1
-
expression of GST-tagged wild-type and mutant enzymes in Escherichia coli
Clostridium limosum
-
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, 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
-
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
-
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
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
-
mutated amplification products transformed into the Escherichia coli DH 5alpha strain. HEK 293-T cells stably transfected with ART1 or ART3
-
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
plasmid pcDNA3-Art7.1 transfected into chicken B cell lymphoma DT40 cells
-
wild-type and mutants cloned into the pcDNA3.1/Zeo (+) plasmid, expression in C-33A cells
-
Yac-1 and Yac-2 enzymes are expressed as glutathione S-transferase fusion proteins in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Art7.1, but not Art7.2, is predominantly expressed on immune cells
-
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
-
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E219Q
Clostridium limosum
-
site-directed mutagenesis, almost inactive mutant
Q217E
Clostridium limosum
-
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
Clostridium limosum
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R61A
Clostridium limosum
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R86A
Clostridium limosum
-
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
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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
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mutant enzyme of RT6.1, mutant enzyme loses thiol-dependency
C80S
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mutant enzyme of RT6.1 remains thiol-dependent
E111D
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catalytic activity close to wild-type
E120D
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catalytic activity highly decreased
R7K
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catalytic activity highly decreased
R204E
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isoform ART2b, no auto-ADP-ribosylation
R204K
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isoform ART2b, no auto-ADP-ribosylation
R204Y
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isoform ART2b, no auto-ADP-ribosylation
Y204R
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isoform ART2a, unlike wild-type, is autoribosylated and has increased enzymic activity
additional information
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depletion of CD38 cells results in enhanced levels of cell surface etheno-ADP-ribosylation on CD38 T cells
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