Any feedback?
No. of entries
Information on EC 2.4.2.30 - NAD+ ADP-ribosyltransferase
for references in articles please use BRENDA:EC2.4.2.30
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.2 Pentosyltransferases
2.4.2.30 NAD+ ADP-ribosyltransferase
IUBMB Comments
The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2′-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20–30 units.
The enzyme appears in viruses and cellular organisms
- 2.4.2.30
-
polyadp-ribose
- caspase-3
- agonist
- bcl-2
- camp
- cyclase
- g-proteins
-
adp-ribosylation
- phospholipase
- ovarian
- necrosis
- endothelial
-
toxin-sensitive
- leukemia
- adenylate
- cholera
- cyclin
-
gtp-binding
- inositol
- bordetella
- guanine
-
annexin
- gtp
- erk
-
pro-apoptotic
-
anti-apoptotic
- mapks
- chromatin
-
apoptosis-inducing
- phosphoinositide
-
muscarinic
-
tunel
-
phorbol
-
adenylyl
- forskolin
-
receptor-mediated
-
protein-coupled
- pkc
-
heterotrimeric
-
caspase-dependent
-
acellular
-
forskolin-stimulated
- survivin
- aif
-
sub-g1
- xiap
- rad51
- carbachol
-
brca1/2
- molecular biology
- drug development
- pharmacology
- toxoid
- analysis
Reaction Schemes
showSynonyms
parp, pertussis toxin, parp-1, poly(adp-ribose) polymerase, parp1, poly (adp-ribose) polymerase, poly(adp-ribose) polymerase-1, c3 exoenzyme, adprt, exoenzyme s, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-protein
-
-
-
-
193-kDa vault protein
-
-
-
-
adenosine diphosphate ribosyltransferase
-
-
-
-
ADP-ribosylating thermozyme
ADP-ribosyltransferase
ADP-ribosyltransferase (polymerizing)
-
-
-
-
ADP-ribosyltransferase C3cer
ADP-ribosyltransferase-1
ADPr
ADPRT
ADPRT
-
-
-
-
ART
ARTD10
AvrRpm1
C3 exoenzyme
-
-
-
-
C3-like toxin
C3larvin toxin
exoenzyme C3
exoenzyme S
ExoS
ExoT
exotoxin-S
HopF2
HopO1-1
HopU1
mART
ModA
ModB
mono-ADP-ribosyl transferase C3
mono-ADP-ribosyltransferase
msPARP
-
-
-
-
NAD(+) ADP-ribosyltransferase
-
-
-
-
NAD+:ADP-ribosyltransferase (polymerizing)
-
-
-
-
NAD-protein ADP-ribosyltransferase
-
-
-
-
NarE
pADPRT
-
-
-
-
PAR polymerase
PARP
PARP
-
-
-
-
PARP-1
PARP-related/IalphaI-related H5/proline-rich
-
-
-
-
PARP1
PARP13
PARP14
PARP15
PARP2
PARPss
pertussis toxin
PH5P
-
-
-
-
poly(ADP-ribose) polymerase
poly(ADP-ribose) polymerase-1
poly(ADP-ribose) synthase
-
-
-
-
poly(ADP-ribose) transferase
-
-
-
-
poly(ADP-ribosyl)transferase
-
-
-
-
poly[ADP-ribose] synthetase
-
-
-
-
PtxS1
scabin
SirTM
TANK1
-
-
-
-
TANK2
-
-
-
-
Tankyrase-like protein
-
-
-
-
Tankyrase-related protein
-
-
-
-
TRF1-interacting ankyrin-related ADP-ribose polymerase
-
-
-
-
TTS-ExoS
VPARP
-
-
-
-
additional information
ADP-ribosyltransferase
-
-
-
-
ADP-ribosyltransferase
-
-
exoenzyme C3
-
-
-
-
exoenzyme S
-
-
-
-
exoenzyme S
-
-
ExoS
-
-
ExoS
-
bifunctional type-III cytotoxin with an N-terminal RhoGAP domain and and C-terminal ADP-ribosylation domain
ExoS
-
bifunctional type-III cytotoxin. Residues 96233 comprise the Rho GTPase-activating protein domain, while residues 234453 comprise the 14-3-3-dependent ADP-ribosyltransferase domain
ExoS
-
bifunctional type-III cytotoxin with an N-terminal RhoGAP domain and and C-terminal ADP-ribosylation domain
-
ExoS
-
bifunctional type-III cytotoxin with an N-terminal RhoGAP domain and and C-terminal ADP-ribosylation domain
-
ExoT
-
bifunctional type-III cytotoxin with an N-terminal RhoGAP domain and and C-terminal ADP-ribosylation domain
ExoT
-
enzyme is comprised of an N-terminal domain with GTPase activating protein activity towards Rho family GTPases and a C-terminal ADP ribosyl-transferase (ADPRT) domain with minimal activity towards a synthetic substrate in vitro
ExoT
-
bifunctional type-III cytotoxin with an N-terminal RhoGAP domain and and C-terminal ADP-ribosylation domain
-
ExoT
-
bifunctional type-III cytotoxin with an N-terminal RhoGAP domain and and C-terminal ADP-ribosylation domain
-
poly(ADP-ribose) polymerase
-
-
-
-
additional information
the enzyme belongs to the family of PARP-like poly(ADP-ribosyl)transferases, pARTs
additional information
the enzyme belongs to the family of PARP-like poly(ADP-ribosyl)transferases, pARTs
additional information
the enzyme belongs to the family of PARP-like poly(ADP-ribosyl)transferases, pARTs
additional information
the enzyme belongs to the family of PARP-like poly(ADP-ribosyl)transferases, pARTs
additional information
the enzyme belongs to the family of PARP-like poly(ADP-ribosyl)transferases, pARTs
additional information
the enzyme belongs to the family of PARP-like poly(ADP-ribosyl)transferases, pARTs
additional information
the enzyme belongs to the family of PARP-like poly(ADP-ribosyl)transferases, pARTs
additional information
the enzyme belongs to the family of PARP-like poly(ADP-ribosyl)transferases, pARTs
additional information
the enzyme belongs to the family of PARP-like poly(ADP-ribosyl)transferases, pARTs
additional information
-
the enzyme belongs to the family of PARP-like poly(ADP-ribosyl)transferases, pARTs
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
-
NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the pART catalytic domain is found associated in Lego-like fashion with a variety of domains, including nucleic acid-binding, protein-protein interaction, and ubiquitylation domains
NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the pART catalytic domain is found associated in Lego-like fashion with a variety of domains, including nucleic acid-binding, protein-protein interaction, and ubiquitylation domains
-
NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
mechanism and physiological function, overview
-
NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
L428 is essential for activity
-
NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
E219 and Gln217 of the ARTT-motif, i.e. ADP-ribosylating turn-turn motif, are essential for activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
NAD+:poly(ADP-D-ribosyl)-acceptor ADP-D-ribosyl-transferase
The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20--30 units.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
58319-92-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-biotin-17-NAD+ + (ADP-D-ribosyl)n- inhibitory alpha-subunits of heterotrimeric G protein
?
biotin-NAD+ + (ADP-D-ribosyl)n-acceptor
biotin-nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n- inhibitory alpha-subunits of heterotrimeric G protein
nicotinamide + (ADP-D-ribosyl)n+1- inhibitory alpha-subunits of heterotrimeric G protein + H+
NAD+ + (ADP-D-ribosyl)n-(EF-2)
nicotinamide + (ADP-D-ribosyl)n+1-(EF-2)
-
Substrates: in native conformation, CRM66 shows limited ability to modify EF-2 covalently. Upon activation with urea and dithiothreitol CRM66 loses ADP-ribosylation activity entirely, yet it retains the ability to bind NAD+. Replacement of Tyr-426 with histidine in CRM66 completely restores cytotoxicity and ADP-ribosyltransferase activity
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-actin
nicotinamide + (ADP-D-ribosyl)n+1-actin
Substrates: VahC is shown to ADP-ribosylate Arg-177 of actin. VahC activity causes depolymerization of actin filaments, which induces caspase-mediated apoptosis in HeLa Tet-Off cells
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-apolipoprotein
nicotinamide + (ADP-D-ribosyl)n+1-apolipoprotein
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-aryl hydrocarbon receptor
nicotinamide + (ADP-D-ribosyl)n+1-aryl hydrocarbon receptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-beta-transducin repeat-containing protein
nicotinamide + (ADP-D-ribosyl)n+1-beta-transducin repeat-containing protein + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-Crk-I
nicotinamide + (ADP-D-ribosyl)n+1-Crk-I
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-Crk-II
nicotinamide + (ADP-D-ribosyl)n+1-Crk-II
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-double-stranded DNA
nicotinamide + (ADP-D-ribosyl)n+1-double-stranded DNA + H+
NAD+ + (ADP-D-ribosyl)n-His6HRas
nicotinamide + (ADP-D-ribosyl)n+1-His6HRas
-
Substrates: the enzyme preferentially ADP-ribosylates membrane-associated His6HRas relative to its cytosolic His6HRasDELTACAAX with a C-terminal deletion
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-immunoglobulin A
nicotinamide + (ADP-D-ribosyl)n+1-immunoglobulin A
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-immunoglobulin G
nicotinamide + (ADP-D-ribosyl)n+1-immunoglobulin G
-
Substrates: preferentially IgG3
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-NEMO protein
nicotinamide + (ADP-D-ribosyl)n+1-NEMO protein + H+
Substrates: the enzyme prevents poly-ubiquitination of NEMO protein
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-P2X7 ion channel
nicotinamide + (ADP-D-ribosyl)n+1-P2X7 ion channel + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-peptide LL-37
nicotinamide + (ADP-D-ribosyl)n+1-peptide LL-37 + H+
Substrates: up to four of the five arginine residues present in peptide LL-37 can be ADP-ribosylated on the same peptide when incubated at a high NAD concentration
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-Rab2
nicotinamide + (ADP-D-ribosyl)n+1-Rab2
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-Rab3
nicotinamide + (ADP-D-ribosyl)n+1-Rab3
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5 + H+
-
Substrates: the enzyme ADP-ribosylates Rab5 at Gln79
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-Rap1A
nicotinamide + (ADP-D-ribosyl)n+1-Rap1A
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-Ras protein
nicotinamide + (ADP-D-ribosyl)n+1-Ras protein
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-serine/arginine-rich protein-specific kinase 2
nicotinamide + (ADP-D-ribosyl)n+1-serine/arginine-rich protein-specific kinase 2 + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-single-stranded DNA
nicotinamide + (ADP-D-ribosyl)n+1-single-stranded DNA + H+
NAD+ + (ADP-D-ribosyl)n-single-stranded RNA
nicotinamide + (ADP-D-ribosyl)n+1-single-stranded RNA + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-soybean trypsin inhibitor
nicotinamide + (ADP-D-ribosyl)n+1-soybean trypsin inhibitor
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-soybean-trypsin-inhibitor
nicotinamide + (ADP-D-ribosyl)n+1-soybean-trypsin-inhibitor
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Btk
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Btk + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Csk
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Csk + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Hck
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Hck + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Lyn
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Lyn + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Src
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Src + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Syk
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Syk + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Tec
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Tec + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Yes1
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Yes1 + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + 4-nitrobenzylidine aminoguanidine
?
-
Substrates: -
Products: -
Products: -
?
NAD+ + Galphai3C20
nicotinamide + N-(ADP-D-ribosyl)-Galphai3C20
-
Substrates: -
Products: -
Products: -
?
NAD+ + GTPase RhoA
nicotinamide + (ADP-D-ribosyl)-GTPase RhoA
-
Substrates: the exoenzyme modifies the low-molecular-mass GTPases RhoA, B, and C specifically at Asn41
Products: -
Products: -
?
NAD+ + GTPase RhoB
nicotinamide + (ADP-D-ribosyl)-GTPase RhoB
-
Substrates: the exoenzyme modifies the low-molecular-mass GTPases RhoA, B, and C specifically at Asn41
Products: -
Products: -
?
NAD+ + GTPase RhoC
nicotinamide + (ADP-D-ribosyl)-GTPase RhoC
-
Substrates: the exoenzyme modifies the low-molecular-mass GTPases RhoA, B, and C specifically at Asn41
Products: -
Products: -
?
NAD+ + histone H1
nicotinamide + (ADP-D-ribosyl)-histone H1
-
Substrates: -
Products: -
Products: -
?
NAD+ + lymphocyte function-associated antigen LFA-1
nicotinamide + ?
-
Substrates: -
Products: -
Products: -
?
NAD+ + poly(ADP-ribose) polymerase-1
nicotinamide + (ADP-ribosyl)-poly(ADP-ribose) polymerase-1
-
Substrates: the 40 kDa CD fragment of avian PARP-1 efficiently catalyzes a covalent auto-poly-(ADP-ribosyl)ation reaction via an intermolecular mechanism that is completely independent of DNA
Products: -
Products: -
?
NAD+ + Rab31
nicotinamide + (ADP-D-ribosyl)-Rab31 + H+
-
Substrates: the enzyme ADP-ribosylates Rab31 at Gln64
Products: -
Products: -
?
NAD+ + Ras
nicotinamide + (ADP-D-ribosyl)-Ras
-
Substrates: interaction requires residue Leu428
Products: -
Products: -
?
NAD+ + Ras GTPase
nicotinamide + (ADP-D-ribosyl)-Ras GTPase
-
Substrates: -
Products: -
Products: -
?
NAD+ + Ras2p
nicotinamide + (ADP-D-ribosyl)-Ras2p + H+
-
Substrates: Ras2p is a yeast protein, activity absolutely requires the yeast protein Bmh1p
Products: -
Products: -
?
NAD+ + soybean trypsin inhibitor
nicotinamide + (ADP-D-ribosyl)-soybean trypsin inhibitor
-
Substrates: the exoenzyme modifies the substrate at an arginine residue
Products: -
Products: -
?
NAD+ + vimentin
nicotinamide + (ADP-D-ribosyl)-vimentin
-
Substrates: -
Products: -
Products: -
?
NAD+ + wild-type exoenzyme C3
nicotinamide + (ADP-D-ribosyl)-wild-type exoenzyme C3
-
Substrates: activity of the recombinant mutant Q217E exoenzyme C3, modification at Arg86
Products: -
Products: -
?
nicotinamide + (ADP-D-ribosyl)n+1-single-stranded DNA + H+
NAD+ + (ADP-D-ribosyl)n-single-stranded DNA
-
Substrates: reaction of DarG
Products: -
Products: -
ir
nicotinamide 1,N6-ethenoadenine dinucleotide + (ADP-D-ribosyl)n-vH-Ras protein
nicotinamide + ?
6-biotin-17-NAD+ + (ADP-D-ribosyl)n- inhibitory alpha-subunits of heterotrimeric G protein
?
Substrates: -
Products: -
Products: -
?
6-biotin-17-NAD+ + (ADP-D-ribosyl)n- inhibitory alpha-subunits of heterotrimeric G protein
?
Substrates: -
Products: -
Products: -
?
beta-benzamide amino adenine dinucleotide + (ADP-D-ribosyl)n-acceptor
?
Substrates: -
Products: -
Products: -
?
beta-benzamide amino adenine dinucleotide + (ADP-D-ribosyl)n-acceptor
?
Substrates: -
Products: -
Products: -
?
beta-carba-NAD+ + (ADP-D-ribosyl)n-acceptor
?
Substrates: -
Products: -
Products: -
?
beta-carba-NAD+ + (ADP-D-ribosyl)n-acceptor
?
Substrates: -
Products: -
Products: -
?
integrin alpha7 + NAD+
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
-
Substrates: the extracellular domain of integrin alpha7 is ADP-ribosylated by an arginine-specific ecto-ADP-ribosyltransferase after adding exogenous NAD+ to intact C2C12 muscle cells, integrin alpha7 N-terminal ADP-ribosylation inhibits the binding of integrin alpha7beta1 to laminin activation status of integrin alpha7beta1 in intact myotubes, overview
Products: -
Products: -
?
integrin alpha7 + NAD+
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
-
Substrates: the extracellular domain of integrin alpha7 is ADP-ribosylated by an arginine-specific ecto-ADP-ribosyltransferase after adding exogenous NAD+ to intact C2C12 muscle cells, integrin alpha7 ADP-ribosylation inhibits the binding of integrin alpha7beta1 to laminin, binding site, overview
Products: -
Products: -
?
isoindolone amine adenine dinucleotide + (ADP-D-ribosyl)n-acceptor
?
Substrates: -
Products: -
Products: -
?
isoindolone amine adenine dinucleotide + (ADP-D-ribosyl)n-acceptor
?
Substrates: -
Products: -
Products: -
?
isoquinolinone amine adenine dinucleotide + (ADP-D-ribosyl)n-acceptor
?
Substrates: -
Products: -
Products: -
?
isoquinolinone amine adenine dinucleotide + (ADP-D-ribosyl)n-acceptor
?
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n- inhibitory alpha-subunits of heterotrimeric G protein
nicotinamide + (ADP-D-ribosyl)n+1- inhibitory alpha-subunits of heterotrimeric G protein + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n- inhibitory alpha-subunits of heterotrimeric G protein
nicotinamide + (ADP-D-ribosyl)n+1- inhibitory alpha-subunits of heterotrimeric G protein + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation of histone H1
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: the enzyme is a DNA repair enzyme
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation of 21000-24000 Da platelet membrane proteins
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
Cryptothecodinium cohnii
-
Substrates: poly(ADP-ribosyl)ation of histone
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation of histone H1
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation, i.e. PARylation, plays diverse roles in many molecular and cellular processes, including DNA damage detection and repair, chromatin modification, transcription, cell death pathways, insulator function, and mitotic apparatus function, connections between nuclear NAD+ metabolism and nuclear signaling through PARP-1, physiologic functions, detailed overview, synthesis and degradation of PAR on an acceptor protein, pathway overview, the enzyme is involved in regulation of the steady-state levels of PAR
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: linking a long negatively charged polymer to a protein, PARP catalyzes the polymerization of ADP-ribose units from donor NAD+ molecules on target proteins, resulting in the attachment of PAR, each residue in PAR contains an adenine moiety capable of base stacking and hydrogen bonding, as well as two phosphate groups that carry negative charges, substrate structure, overview
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation of histone
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation of topoisomerase I
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: auto-poly(ADP-ribosyl)ation
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation of high mobility group proteins
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation of DNA ligase
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation of endonuclease
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation of topoisomerase II
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation of terminal deoxynucleotidyltransferase
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation of histone H1
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation of histone
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: catalyzes poly(ADP-ribosyl)ation of the synthetase itself, automodification
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation of ADP-ribosyltransferase
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation, i.e. PARylation, plays diverse roles in many molecular and cellular processes, including DNA damage detection and repair, chromatin modification, transcription, cell death pathways, insulator function, and mitotic apparatus function, connections between nuclear NAD+ metabolism and nuclear signaling through PARP-1, physiologic functions, detailed overview, synthesis and degradation of PAR on an acceptor protein, pathway overview, the enzyme is involved in regulation of the steady-state levels of PAR
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: linking a long negatively charged polymer to a protein, PARP-1 catalyzes the polymerization of ADP-ribose units from donor NAD+ molecules on target proteins, resulting in the attachment of PAR, each residue in PAR contains an adenine moiety capable of base stacking and hydrogen bonding, as well as two phosphate groups that carry negative charges, substrate structure, overview
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: agmatine as ADPribose acceptor is used
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: ExoS can modify multiple GTPases of the Ras superfamily in vivo. ExoS modulates the activity of several of GTP-binding proteins, such as Ras, Rap1, Rap2, Ral, Rac1, RhoA and Cdc42. It is suggested that ExoS is the major ADP-ribosyltransferase protein modulating small GTPase function encoded by Pseudomonas aeruginosa
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: intracellular expression of the amino terminus of ExoS in eukaryotic cells stimulates actin reorganization without cytotoxicity, which involves small-molecular-weight GTPases of the Rho subfamily
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: intracellular Ras is modified by bacterially translocated ExoS, inhibition of target cell proliferation correlates with the efficiency of Ras modification
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: exoenzyme S is an ADP-ribosyltransferase produced and directly translocated into eukaryotic cells by the opportunistic pathogen Pseudomonas aeruginosa. Factors expressed by growing epithelial cells are required for the bacterial contact-dependent translocation of ExoS. As normal epithelial cells differentiate into polarized confluent monolayers, expression of these factors is altered, and cells in turn become more resistant to the effects of ExoS
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: ExoT modifies and inactivates host cell proteins involved in maintaining the actin cytoskeleton in vivo by two independent mechanisms. ADP-ribosylation activity of ExoT induces an irreversible disruption of actin microfilaments of infected Hela cells
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: ADPRT domain of ExoT is active in vivo and contributes to the pathogenesis of Pseudomonas aeruginosa infections
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: ExoS has polysubstrate specificity and can ADP-ribosylate numerous host proteins, e.g. monomeric GTPase or vimentin. ExoS also undergoes auto-ADP-ribosylation. Ras has multiple alternative sites for ADP-ribosylation
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: ExoT ADP-ribosylates a restricted subset of host proteins including the Crk proteins
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: ExoS is a type III cytotoxin which modulates two eukaryotic signalling pathways. The N-terminus (residues 1-234) is a GTPase activating protein for RhoGTPases, while the C-terminus (residues 232-453) encodes an ADP-ribosyltransferase
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: ExoS has polysubstrate specificity and can ADP-ribosylate numerous host proteins, e.g. monomeric GTPase or vimentin. ExoS also undergoes auto-ADP-ribosylation. Ras has multiple alternative sites for ADP-ribosylation
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: ExoT ADP-ribosylates a restricted subset of host proteins including the Crk proteins
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: ExoS has polysubstrate specificity and can ADP-ribosylate numerous host proteins, e.g. monomeric GTPase or vimentin. ExoS also undergoes auto-ADP-ribosylation. Ras has multiple alternative sites for ADP-ribosylation
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: ExoT ADP-ribosylates a restricted subset of host proteins including the Crk proteins
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
W2E3J5
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
W2E3J5
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: the emzyme protects homologous DNA against thermal denaturation by lowering the amount of melted DNA and increasing melting temperature. The archaeal protein induces structural changes of the nucleic acid by modifying the dichroic spectra towards a shape typical of condensing DNA
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Saccharolobus solfataricus MT-4 / DSM 5833
Substrates: the emzyme protects homologous DNA against thermal denaturation by lowering the amount of melted DNA and increasing melting temperature. The archaeal protein induces structural changes of the nucleic acid by modifying the dichroic spectra towards a shape typical of condensing DNA
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Saccharolobus solfataricus MT-4 / DSM 5833
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-biotin
nicotinamide + (ADP-D-ribosyl)n+1-biotin + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-biotin
nicotinamide + (ADP-D-ribosyl)n+1-biotin + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-double-stranded DNA
nicotinamide + (ADP-D-ribosyl)n+1-double-stranded DNA + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-double-stranded DNA
nicotinamide + (ADP-D-ribosyl)n+1-double-stranded DNA + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-p21ras
nicotinamide + (ADP-D-ribosyl)n+1-p21ras
-
Substrates: ADP-ribosylation of p21ras does not alter interactions with guanidine nucleotides. Possible function of the enzyme in pathogenesis
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-p21ras
nicotinamide + (ADP-D-ribosyl)n+1-p21ras
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-rab4
nicotinamide + (ADP-D-ribosyl)n+1-rab4
-
Substrates: ADP-ribosylation affects Rab4 function in membrane recycling
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-rab4
nicotinamide + (ADP-D-ribosyl)n+1-rab4
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5
-
Substrates: ADP-ribosylation of Rab5 by ExoS affects endocytosis. Interaction of Rab5 with endosome antigen 1 is markedly diminished after Rab5 ADP-ribosylation by ExoS
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-RalA
nicotinamide + (ADP-D-ribosyl)n+1-RalA
-
Substrates: ADP-ribosylation of RalA by ExoS interferes with RalA activation and binding to its downstream effector in J774A.1 macrophages and suggests the potential of ExoS ADPRT activity to interfere with filiopodium formation through the inactivation of RalA and downstream effects mediated through the exocyst complex
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-RalA
nicotinamide + (ADP-D-ribosyl)n+1-RalA
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-Ras
nicotinamide + (ADP-D-ribosyl)n+1-Ras
-
Substrates: ADP-ribosylation of Ras at Arg41 disrupts Ras-Cdc25 interactions, which inhibits the rate-limiting step in Ras signal transduction, the activation of Ras by its guanine nucleotide exchange factor
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-Ras
nicotinamide + (ADP-D-ribosyl)n+1-Ras
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
W2E3J5
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
W2E3J5
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-single-stranded DNA
nicotinamide + (ADP-D-ribosyl)n+1-single-stranded DNA + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-single-stranded DNA
nicotinamide + (ADP-D-ribosyl)n+1-single-stranded DNA + H+
-
Substrates: -
Products: -
Products: -
ir
NAD+ + (ADP-D-ribosyl)n-single-stranded DNA
nicotinamide + (ADP-D-ribosyl)n+1-single-stranded DNA + H+
-
Substrates: reaction of DarT
Products: -
Products: -
ir
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
Substrates: cytosolic protein of several human epithelial cells, modification at Arg55 and Arg69 of cyclophilin A, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, overview
Products: -
Products: -
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
Substrates: a non-G-protein substrate with peptidyl-prolyl isomerase activity, from several human epithelial cells, modification at Arg55 and Arg69, but not at Arg148, of cyclophilin A, i.e. CpA, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, activity with CpA mutants, overview
Products: -
Products: -
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
Substrates: cytosolic protein of several human epithelial cells, modification at Arg55 and Arg69 of cyclophilin A, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, overview
Products: -
Products: -
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
Substrates: a non-G-protein substrate with peptidyl-prolyl isomerase activity, from several human epithelial cells, modification at Arg55 and Arg69, but not at Arg148, of cyclophilin A, i.e. CpA, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, activity with CpA mutants, overview
Products: -
Products: -
?
NAD+ + Galphai
nicotinamide + (ADP-D-ribosyl)-Galphai + H+
Substrates: -
Products: -
Products: -
?
NAD+ + Galphai
nicotinamide + (ADP-D-ribosyl)-Galphai + H+
Substrates: -
Products: -
Products: -
?
NAD+ + histone H2A
nicotinamide + (ADP-D-ribosyl)-histone H2A
-
Substrates: the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
Products: -
Products: -
?
NAD+ + histone H2A
nicotinamide + (ADP-D-ribosyl)-histone H2A
-
Substrates: the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B
Products: -
Products: -
?
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
-
Substrates: -
Products: -
Products: -
?
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
-
Substrates: the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
Products: -
Products: -
?
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
-
Substrates: the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B
Products: -
Products: -
?
NAD+ + moesin
nicotinamide + (ADP-D-ribosyl)-moesin
-
Substrates: ADP-ribosylated-moesin is a poor target for phosphorylation by protein kinase C and Rho kinase, which shows that ADP-ribosylation directly inhibits ERM phosphorylation
Products: -
Products: -
?
NAD+ + moesin
nicotinamide + (ADP-D-ribosyl)-moesin
-
Substrates: modification of Arg553, Arg560 and Arg563, activity with wild-type and mutant moesins, overview
Products: -
Products: -
?
NAD+ + p53
nicotinamide + (ADP-D-ribosyl)-p53
-
Substrates: PARP-1 interacts with and poly(ADP-ribosyl)ates p53, which participates in DNA recombination
Products: -
Products: -
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Substrates: Rab5 mediates entry of the EGFR into early endosomes
Products: -
Products: -
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Substrates: Rab5 mediates entry of the EGFR into early endosomes
Products: -
Products: -
?
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + RhoA
nicotinamide (ADP-D-ribosyl)-RhoA
-
Substrates: -
Products: -
Products: -
?
NAD+ + RhoB
nicotinamide (ADP-D-ribosyl)-RhoB
-
Substrates: -
Products: -
Products: -
?
NAD+ + RhoC
nicotinamide (ADP-D-ribosyl)-RhoC
-
Substrates: weak activity
Products: -
Products: -
?
NAD+ + RhoC
nicotinamide (ADP-D-ribosyl)-RhoC
-
Substrates: weak activity
Products: -
Products: -
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Substrates: three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
Products: -
Products: -
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Substrates: -
Products: -
Products: -
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4 ModA
Substrates: three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
Products: -
Products: -
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4 ModA
Substrates: -
Products: -
Products: -
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4 ModB
Substrates: three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
Products: -
Products: -
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4 ModB
Substrates: -
Products: -
Products: -
?
NAD+ + topoisomerase I
nicotinamide + (ADP-D-ribosyl)-topoisomerase I
-
Substrates: -
Products: -
Products: -
?
NAD+ + topoisomerase I
nicotinamide + (ADP-D-ribosyl)-topoisomerase I
-
Substrates: PARP-1 interacts with and poly(ADP-ribosyl)ates topoisomerase I, which participates in DNA recombination, I-SceI-meganuclease-mediated cleavage terminates the interaction, overview
Products: -
Products: -
?
nicotinamide 1,N6-ethenoadenine dinucleotide + (ADP-D-ribosyl)n-vH-Ras protein
nicotinamide + ?
-
Substrates: -
Products: -
Products: -
?
nicotinamide 1,N6-ethenoadenine dinucleotide + (ADP-D-ribosyl)n-vH-Ras protein
nicotinamide + ?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: cuts produced in vivo on DNA during DNA repair activate the enzyme, which then synthesiszes poly(ADP-ribose) on histone H1, in particular, and contributes to the opening of the 25 nm chromatin fiber, resulting in the increased accessibility of DNA to excision repair enzymes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme modifies eukaryotic 21000-24000 Da GTP-binding proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: transcriptional regulation mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also shows NAD+-hydrolase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: ADP-ribosylation seems to be involved in regulation of differentiation, the enzyme may be centrally involved in tumorigenic cell transformation, the enzyme appears to be a central controller of cell processes: higher activities shift the cell towards proliferation, low activities shift the cell towards differentiation, role of the enzyme in DNA repair
Products: -
Products: -
?
additional information
?
-
-
Substrates: role of the enzyme in DNA repair, the unmodified polymerase molecules bind tightly to DNA strand breaks: auto-poly(ADP-ribosyl)ation of the protein then effects its release and allows access to lesions for DNA repair enzymes
Products: -
Products: -
?
additional information
?
-
-
Substrates: mechanistic basis for the physiological function of PARP-1 in the dynamics of the local modulation of chromatin structure. PARP-1 activation upon binding to base-unpaired regions and stem-loops structures in DNA leads to a local PAR modification of histones and non-histone proteins at genomic sites where such DNA structures are formed. Subsequent PARP-1 automodification results in its dissociation from DNA leading to an enzymatic self-inactivation thus ensuring a transient character of chromatin ADP-ribosylation. In combination with the PAR-glycohydrolase degradation of ADP-ribose polymers on acceptor proteins, PARP-1 interaction with DNA secondary structures provides a mechanism for local and transient chromatin modification by PAR during physiological nuclear processes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in pathogenesis of Parkinson's disease, analysis of polymorphisms, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: PARP-1 inhibits the transcription factor tonicity-responsive enhancer/osmotic response element-binding protein, TonEBP/OREBP. Inhibition of TonEBP/OREBP transcriptional activity by PARP-1 does not require PARP-1 catalytic activity, functional interaction anaylsis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows DNA-binding activity, and is physically associated with the transcription factor tonicity-responsive enhancer/osmotic response element-binding protein, TonEBP/OREBP
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the ability to ADP-ribosylate itself
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform PARP14 does not show activity on 5'-phosphorylated RNA
Products: -
Products: -
-
additional information
?
-
Substrates: isoform PARP14 does not show activity on 5'-phosphorylated RNA
Products: -
Products: -
-
additional information
?
-
Substrates: isoform PARP14 does not show activity on 5'-phosphorylated RNA
Products: -
Products: -
-
additional information
?
-
Substrates: isoform PARP14 does not show activity on 5'-phosphorylated RNA
Products: -
Products: -
-
additional information
?
-
Substrates: isoform PARP14 does not show activity on 5'-phosphorylated RNA
Products: -
Products: -
-
additional information
?
-
-
Substrates: isoform PARP13 does not show activity on 5'-phosphorylated RNA
Products: -
Products: -
-
additional information
?
-
Substrates: isoform PARP13 does not show activity on 5'-phosphorylated RNA
Products: -
Products: -
-
additional information
?
-
Substrates: isoform PARP13 does not show activity on 5'-phosphorylated RNA
Products: -
Products: -
-
additional information
?
-
Substrates: isoform PARP13 does not show activity on 5'-phosphorylated RNA
Products: -
Products: -
-
additional information
?
-
Substrates: isoform PARP13 does not show activity on 5'-phosphorylated RNA
Products: -
Products: -
-
additional information
?
-
-
Substrates: raft association focuses ART2.2 on specific targets that constitutively or inducibly assoiate with lipid rafts
Products: -
Products: -
?
additional information
?
-
-
Substrates: ART1 is an arginine-specific transferase
Products: -
Products: -
?
additional information
?
-
-
Substrates: PARP-1 responds to DNA damage by transferring 50 to 200 molecules of ADP-ribose to various nuclear proteins, including transcription factors, histones and PARP-1 itself, interaction between ATM and PARP-1 in response to DNA damage and sensitization of ATM deficient cells through PARP inhibition, ATM and PARP-1 are two of the most important players in the cell's response to DNA damage, PARP-1 is needed for optimal activation of ATM, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: role for PARP-1 in DNA double-strand break repair, the enzyme is not required for homologous recombination itself, it regulates the process through its involvement in the repair of DNA single-strand breaks, PARP-1 binds to DNA breaks to facilitate DNA repair, but the role of PARP-1 in DNA repair appears to not be critical since PARP-1 knockout mice are viable, fertile and do not develop early onset tumors, DNA binding and auto-modification of PARP-1 attracts the DNA repair proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: transcriptional regulation mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in endothelial cell dysfunction
Products: -
Products: -
?
additional information
?
-
-
Substrates: PARP-1 is involved in modulation of NO-derived injury and response to genotoxic damage
Products: -
Products: -
?
additional information
?
-
-
Substrates: PARP-1 plays fundamental roles in the recruitment and modulation of enzymatic and regulatory factors involved in transcription, DNA replication, repair and recombination, the enzyme antagonizes topoisomerase I-dependent recombination stimulation by P53
Products: -
Products: -
?
additional information
?
-
-
Substrates: PARP-1 protein has an N-terminal DNA binding domain containing two large zinc fingers that bind to both DNA single-strand breaks and DNA double-strand breaks, DNA binding by PARP-1 triggers its activity and it adds poly(ADP-ribose) polymers to itself and to surrounding histones, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme itself is a target for P2X7-triggered ectodomain shedding at F239/S240
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in endothelial cell dysfunction
Products: -
Products: -
?
additional information
?
-
-
Substrates: PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: narE possesses ADP-ribosylating and NAD-glycohydrolase activities
Products: -
Products: -
?
additional information
?
-
-
Substrates: exoenzyme S is an important adhesin
Products: -
Products: -
?
additional information
?
-
-
Substrates: exoenzyme S and 14-3-3 interact in a direct fashion, interaction involves the conserved amphiphatic groove of 14-3-3
Products: -
Products: -
?
additional information
?
-
-
Substrates: ExoS is a virulence factor of the pathogen
Products: -
Products: -
?
additional information
?
-
-
Substrates: the bacterial enzyme shows the ability to mediate cell death in the host and is a toxin, residues 426-428 are required for this activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: Pseudomonas aeruginosa inhibits mammalian cytokinesis in a type III secretion system and exotoxin T-dependent manner, the ADP-ribosyl transferase domain inhibits late steps of cytokinesis by blocking syntaxin-2 localization to the midbody, an event essential for completion of cytokinesis, e.g. in Madin-Darby canine kidney cells, mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: ExoS is a bifunctional toxin with an N-terminal Rho GTPase activating protein, GAP, domain, and a C-terminal ADP-ribosyltransferase domain which transfers ADP-ribose from NAD onto substrates such as the Ras GTPases and vimentin
Products: -
Products: -
?
additional information
?
-
-
Substrates: ExoT is a bifunctional type III secretion system effector protein that contains an N-terminal GTPase-activating protein domain and a C-terminal ADP-ribosyl transferase domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: exoenzyme S is a bifunctional type III secretion, TTS, effector protein, with GTPase-activating and ADP-ribosyltransferase activities
Products: -
Products: -
?
additional information
?
-
-
Substrates: ExoS is a toxin playing a pivotal role during Pseudomonas aeruginosa infections, it is a virulence factor causing growth inhibition in Saccharomyces cerevisiae. Exoenzyme S ADP-ribosylates identical targets in both human and yeast
Products: -
Products: -
?
additional information
?
-
-
Substrates: ExoS is a type III cytotoxin, that ADP-ribosylates Rab GTPases to inhibit host cell vesicle trafficking pathways by modulating HeLa host cell endocytosis, wild-type ExoS uncouples Rab5-early endosome antigen 1 interaction and inhibits fluid phase uptake, as well as Pseudomonas aeruginosa internalization, RhoGAP, but not ADPr, the ADPr domain is dispensable for anti-internalization function, but is required for inhibition of EGF-activated EGFR degradation in HeLa cells, mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: ExoS is a bi-functional type III cytotoxin that possesses Rho GTPase activating protein and ADP-ribosyltransferase activities, no activity with Rab4 protein, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: exoenzyme S is a bifunctional type III secretion, TTS, effector protein, with GTPase-activating and ADP-ribosyltransferase activities
Products: -
Products: -
?
additional information
?
-
-
Substrates: ExoS is a type III cytotoxin, that ADP-ribosylates Rab GTPases to inhibit host cell vesicle trafficking pathways by modulating HeLa host cell endocytosis, wild-type ExoS uncouples Rab5-early endosome antigen 1 interaction and inhibits fluid phase uptake, as well as Pseudomonas aeruginosa internalization, RhoGAP, but not ADPr, the ADPr domain is dispensable for anti-internalization function, but is required for inhibition of EGF-activated EGFR degradation in HeLa cells, mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: ExoS is a bi-functional type III cytotoxin that possesses Rho GTPase activating protein and ADP-ribosyltransferase activities, no activity with Rab4 protein, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme also targets deoxyguanosine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also targets deoxyguanosine
Products: -
Products: -
?
additional information
?
-
-
Substrates: scabin specifically targets the exocyclic NH2 of guanosine residuesin DNA, RNA and in small molecules such as cGMP and GDP. The enzyme exhibits higher in vitro activity against potato (Solanum tuberosum) genomic DNA than against genomic DNA from either Streptomyces scabiei or Pseudomonas aeruginosa
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme also targets deoxyguanosine
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
integrin alpha7 + NAD+
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
-
Substrates: the extracellular domain of integrin alpha7 is ADP-ribosylated by an arginine-specific ecto-ADP-ribosyltransferase after adding exogenous NAD+ to intact C2C12 muscle cells, integrin alpha7 N-terminal ADP-ribosylation inhibits the binding of integrin alpha7beta1 to laminin activation status of integrin alpha7beta1 in intact myotubes, overview
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n- inhibitory alpha-subunits of heterotrimeric G protein
nicotinamide + (ADP-D-ribosyl)n+1- inhibitory alpha-subunits of heterotrimeric G protein + H+
NAD+ + (ADP-D-ribosyl)n-aryl hydrocarbon receptor
nicotinamide + (ADP-D-ribosyl)n+1-aryl hydrocarbon receptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-beta-transducin repeat-containing protein
nicotinamide + (ADP-D-ribosyl)n+1-beta-transducin repeat-containing protein + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-NEMO protein
nicotinamide + (ADP-D-ribosyl)n+1-NEMO protein + H+
Substrates: the enzyme prevents poly-ubiquitination of NEMO protein
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-p21ras
nicotinamide + (ADP-D-ribosyl)n+1-p21ras
-
Substrates: ADP-ribosylation of p21ras does not alter interactions with guanidine nucleotides. Possible function of the enzyme in pathogenesis
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-P2X7 ion channel
nicotinamide + (ADP-D-ribosyl)n+1-P2X7 ion channel + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-rab4
nicotinamide + (ADP-D-ribosyl)n+1-rab4
-
Substrates: ADP-ribosylation affects Rab4 function in membrane recycling
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5
-
Substrates: ADP-ribosylation of Rab5 by ExoS affects endocytosis. Interaction of Rab5 with endosome antigen 1 is markedly diminished after Rab5 ADP-ribosylation by ExoS
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5 + H+
-
Substrates: the enzyme ADP-ribosylates Rab5 at Gln79
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-RalA
nicotinamide + (ADP-D-ribosyl)n+1-RalA
-
Substrates: ADP-ribosylation of RalA by ExoS interferes with RalA activation and binding to its downstream effector in J774A.1 macrophages and suggests the potential of ExoS ADPRT activity to interfere with filiopodium formation through the inactivation of RalA and downstream effects mediated through the exocyst complex
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-Ras
nicotinamide + (ADP-D-ribosyl)n+1-Ras
-
Substrates: ADP-ribosylation of Ras at Arg41 disrupts Ras-Cdc25 interactions, which inhibits the rate-limiting step in Ras signal transduction, the activation of Ras by its guanine nucleotide exchange factor
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Btk
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Btk + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Csk
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Csk + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Hck
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Hck + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Lyn
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Lyn + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Src
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Src + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Syk
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Syk + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Tec
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Tec + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Yes1
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Yes1 + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + histone H2A
nicotinamide + (ADP-D-ribosyl)-histone H2A
-
Substrates: the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
Products: -
Products: -
?
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
-
Substrates: the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
Products: -
Products: -
?
NAD+ + moesin
nicotinamide + (ADP-D-ribosyl)-moesin
-
Substrates: ADP-ribosylated-moesin is a poor target for phosphorylation by protein kinase C and Rho kinase, which shows that ADP-ribosylation directly inhibits ERM phosphorylation
Products: -
Products: -
?
NAD+ + Rab31
nicotinamide + (ADP-D-ribosyl)-Rab31 + H+
-
Substrates: the enzyme ADP-ribosylates Rab31 at Gln64
Products: -
Products: -
?
NAD+ + Ras
nicotinamide + (ADP-D-ribosyl)-Ras
-
Substrates: interaction requires residue Leu428
Products: -
Products: -
?
NAD+ + Ras GTPase
nicotinamide + (ADP-D-ribosyl)-Ras GTPase
-
Substrates: -
Products: -
Products: -
?
NAD+ + topoisomerase I
nicotinamide + (ADP-D-ribosyl)-topoisomerase I
-
Substrates: -
Products: -
Products: -
?
NAD+ + vimentin
nicotinamide + (ADP-D-ribosyl)-vimentin
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n- inhibitory alpha-subunits of heterotrimeric G protein
nicotinamide + (ADP-D-ribosyl)n+1- inhibitory alpha-subunits of heterotrimeric G protein + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n- inhibitory alpha-subunits of heterotrimeric G protein
nicotinamide + (ADP-D-ribosyl)n+1- inhibitory alpha-subunits of heterotrimeric G protein + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: the enzyme is a DNA repair enzyme
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation, i.e. PARylation, plays diverse roles in many molecular and cellular processes, including DNA damage detection and repair, chromatin modification, transcription, cell death pathways, insulator function, and mitotic apparatus function, connections between nuclear NAD+ metabolism and nuclear signaling through PARP-1, physiologic functions, detailed overview, synthesis and degradation of PAR on an acceptor protein, pathway overview, the enzyme is involved in regulation of the steady-state levels of PAR
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: poly(ADP-ribosyl)ation, i.e. PARylation, plays diverse roles in many molecular and cellular processes, including DNA damage detection and repair, chromatin modification, transcription, cell death pathways, insulator function, and mitotic apparatus function, connections between nuclear NAD+ metabolism and nuclear signaling through PARP-1, physiologic functions, detailed overview, synthesis and degradation of PAR on an acceptor protein, pathway overview, the enzyme is involved in regulation of the steady-state levels of PAR
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: ExoS can modify multiple GTPases of the Ras superfamily in vivo. ExoS modulates the activity of several of GTP-binding proteins, such as Ras, Rap1, Rap2, Ral, Rac1, RhoA and Cdc42. It is suggested that ExoS is the major ADP-ribosyltransferase protein modulating small GTPase function encoded by Pseudomonas aeruginosa
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: intracellular expression of the amino terminus of ExoS in eukaryotic cells stimulates actin reorganization without cytotoxicity, which involves small-molecular-weight GTPases of the Rho subfamily
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: intracellular Ras is modified by bacterially translocated ExoS, inhibition of target cell proliferation correlates with the efficiency of Ras modification
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: exoenzyme S is an ADP-ribosyltransferase produced and directly translocated into eukaryotic cells by the opportunistic pathogen Pseudomonas aeruginosa. Factors expressed by growing epithelial cells are required for the bacterial contact-dependent translocation of ExoS. As normal epithelial cells differentiate into polarized confluent monolayers, expression of these factors is altered, and cells in turn become more resistant to the effects of ExoS
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: ExoT modifies and inactivates host cell proteins involved in maintaining the actin cytoskeleton in vivo by two independent mechanisms. ADP-ribosylation activity of ExoT induces an irreversible disruption of actin microfilaments of infected Hela cells
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: ADPRT domain of ExoT is active in vivo and contributes to the pathogenesis of Pseudomonas aeruginosa infections
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
W2E3J5
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
W2E3J5
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: the emzyme protects homologous DNA against thermal denaturation by lowering the amount of melted DNA and increasing melting temperature. The archaeal protein induces structural changes of the nucleic acid by modifying the dichroic spectra towards a shape typical of condensing DNA
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Saccharolobus solfataricus MT-4 / DSM 5833
Substrates: the emzyme protects homologous DNA against thermal denaturation by lowering the amount of melted DNA and increasing melting temperature. The archaeal protein induces structural changes of the nucleic acid by modifying the dichroic spectra towards a shape typical of condensing DNA
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Substrates: the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
W2E3J5
Substrates: -
Products: -
Products: -
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
W2E3J5
Substrates: -
Products: -
Products: -
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
Substrates: cytosolic protein of several human epithelial cells, modification at Arg55 and Arg69 of cyclophilin A, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, overview
Products: -
Products: -
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
Substrates: cytosolic protein of several human epithelial cells, modification at Arg55 and Arg69 of cyclophilin A, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, overview
Products: -
Products: -
?
NAD+ + Galphai
nicotinamide + (ADP-D-ribosyl)-Galphai + H+
Substrates: -
Products: -
Products: -
?
NAD+ + Galphai
nicotinamide + (ADP-D-ribosyl)-Galphai + H+
Substrates: -
Products: -
Products: -
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Substrates: Rab5 mediates entry of the EGFR into early endosomes
Products: -
Products: -
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Substrates: Rab5 mediates entry of the EGFR into early endosomes
Products: -
Products: -
?
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
-
Substrates: -
Products: -
Products: -
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Substrates: three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
Products: -
Products: -
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4 ModA
Substrates: three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
Products: -
Products: -
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4 ModB
Substrates: three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
Products: -
Products: -
?
additional information
?
-
-
Substrates: cuts produced in vivo on DNA during DNA repair activate the enzyme, which then synthesiszes poly(ADP-ribose) on histone H1, in particular, and contributes to the opening of the 25 nm chromatin fiber, resulting in the increased accessibility of DNA to excision repair enzymes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme modifies eukaryotic 21000-24000 Da GTP-binding proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: transcriptional regulation mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: ADP-ribosylation seems to be involved in regulation of differentiation, the enzyme may be centrally involved in tumorigenic cell transformation, the enzyme appears to be a central controller of cell processes: higher activities shift the cell towards proliferation, low activities shift the cell towards differentiation, role of the enzyme in DNA repair
Products: -
Products: -
?
additional information
?
-
-
Substrates: role of the enzyme in DNA repair, the unmodified polymerase molecules bind tightly to DNA strand breaks: auto-poly(ADP-ribosyl)ation of the protein then effects its release and allows access to lesions for DNA repair enzymes
Products: -
Products: -
?
additional information
?
-
-
Substrates: mechanistic basis for the physiological function of PARP-1 in the dynamics of the local modulation of chromatin structure. PARP-1 activation upon binding to base-unpaired regions and stem-loops structures in DNA leads to a local PAR modification of histones and non-histone proteins at genomic sites where such DNA structures are formed. Subsequent PARP-1 automodification results in its dissociation from DNA leading to an enzymatic self-inactivation thus ensuring a transient character of chromatin ADP-ribosylation. In combination with the PAR-glycohydrolase degradation of ADP-ribose polymers on acceptor proteins, PARP-1 interaction with DNA secondary structures provides a mechanism for local and transient chromatin modification by PAR during physiological nuclear processes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in pathogenesis of Parkinson's disease, analysis of polymorphisms, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: PARP-1 inhibits the transcription factor tonicity-responsive enhancer/osmotic response element-binding protein, TonEBP/OREBP. Inhibition of TonEBP/OREBP transcriptional activity by PARP-1 does not require PARP-1 catalytic activity, functional interaction anaylsis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the ability to ADP-ribosylate itself
Products: -
Products: -
?
additional information
?
-
-
Substrates: raft association focuses ART2.2 on specific targets that constitutively or inducibly assoiate with lipid rafts
Products: -
Products: -
?
additional information
?
-
-
Substrates: PARP-1 responds to DNA damage by transferring 50 to 200 molecules of ADP-ribose to various nuclear proteins, including transcription factors, histones and PARP-1 itself, interaction between ATM and PARP-1 in response to DNA damage and sensitization of ATM deficient cells through PARP inhibition, ATM and PARP-1 are two of the most important players in the cell's response to DNA damage, PARP-1 is needed for optimal activation of ATM, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: role for PARP-1 in DNA double-strand break repair, the enzyme is not required for homologous recombination itself, it regulates the process through its involvement in the repair of DNA single-strand breaks, PARP-1 binds to DNA breaks to facilitate DNA repair, but the role of PARP-1 in DNA repair appears to not be critical since PARP-1 knockout mice are viable, fertile and do not develop early onset tumors, DNA binding and auto-modification of PARP-1 attracts the DNA repair proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: transcriptional regulation mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in endothelial cell dysfunction
Products: -
Products: -
?
additional information
?
-
-
Substrates: PARP-1 is involved in modulation of NO-derived injury and response to genotoxic damage
Products: -
Products: -
?
additional information
?
-
-
Substrates: PARP-1 plays fundamental roles in the recruitment and modulation of enzymatic and regulatory factors involved in transcription, DNA replication, repair and recombination, the enzyme antagonizes topoisomerase I-dependent recombination stimulation by P53
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme itself is a target for P2X7-triggered ectodomain shedding at F239/S240
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in endothelial cell dysfunction
Products: -
Products: -
?
additional information
?
-
-
Substrates: PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: exoenzyme S is an important adhesin
Products: -
Products: -
?
additional information
?
-
-
Substrates: exoenzyme S and 14-3-3 interact in a direct fashion, interaction involves the conserved amphiphatic groove of 14-3-3
Products: -
Products: -
?
additional information
?
-
-
Substrates: ExoS is a virulence factor of the pathogen
Products: -
Products: -
?
additional information
?
-
-
Substrates: the bacterial enzyme shows the ability to mediate cell death in the host and is a toxin, residues 426-428 are required for this activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: Pseudomonas aeruginosa inhibits mammalian cytokinesis in a type III secretion system and exotoxin T-dependent manner, the ADP-ribosyl transferase domain inhibits late steps of cytokinesis by blocking syntaxin-2 localization to the midbody, an event essential for completion of cytokinesis, e.g. in Madin-Darby canine kidney cells, mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: ExoS is a toxin playing a pivotal role during Pseudomonas aeruginosa infections, it is a virulence factor causing growth inhibition in Saccharomyces cerevisiae. Exoenzyme S ADP-ribosylates identical targets in both human and yeast
Products: -
Products: -
?
additional information
?
-
-
Substrates: ExoS is a type III cytotoxin, that ADP-ribosylates Rab GTPases to inhibit host cell vesicle trafficking pathways by modulating HeLa host cell endocytosis, wild-type ExoS uncouples Rab5-early endosome antigen 1 interaction and inhibits fluid phase uptake, as well as Pseudomonas aeruginosa internalization, RhoGAP, but not ADPr, the ADPr domain is dispensable for anti-internalization function, but is required for inhibition of EGF-activated EGFR degradation in HeLa cells, mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: ExoS is a type III cytotoxin, that ADP-ribosylates Rab GTPases to inhibit host cell vesicle trafficking pathways by modulating HeLa host cell endocytosis, wild-type ExoS uncouples Rab5-early endosome antigen 1 interaction and inhibits fluid phase uptake, as well as Pseudomonas aeruginosa internalization, RhoGAP, but not ADPr, the ADPr domain is dispensable for anti-internalization function, but is required for inhibition of EGF-activated EGFR degradation in HeLa cells, mechanism, overview
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
Bmh1p, a yeast homologue of the human FAS, acts as an ExoS cofactor, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
-
enzyme binds iron through a Fe-S center, which is crucial for the catalytic activity
Mg2+
Mn2+
Mg2+
-
enhances both the automodification and poly(ADP-ribosyl)ation of histone H1
Mg2+
-
divalent cation required, Mg2+ preferred to Mn2+, optimal concentration 5 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanamide
-
(beta,beta-dimethylacryl)shikonin
64% inhibition at 0.01 mM; 64% inhibition at 0.01 mM
2,3-dihydro-5-hydroxy-1,4-phthalazinedione
-
0.001 mM, 95% inhibition of the 116000 Da enzyme
2-(3-hydroxypropyl)-3,5,6,7-tetrahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-4-one
-
-
2-(3-hydroxypropyl)-5,6,7,8-tetrahydro[1]benzothieno[2,3-d]pyrimidin-4(3H)-one
-
-
2-(4-[4-[(2,4-dimethoxyphenyl)amino]quinazolin-2-yl]piperazin-1-yl)ethanol
-
2-[[3-(dimethylamino)-2-oxopropyl]amino]-5,6-dihydrophenanthridin-6-one
potent inhibitor
3-(4-methoxy-6,7-dihydro-5H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-2-yl)propanoic acid
-
-
3-(4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl)propanoic acid
-
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-(pyridin-2-yl)ethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-(pyridin-2-yl)ethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylpropyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[1-(4-sulfamoylphenyl)ethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[1-(pyridin-2-yl)ethyl]propanamide
-
3-(4-oxo-3,5,6,7-tetrahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-2-yl)propanoic acid
-
inhibitor with micromolar potency
3-amino-1,4-dimethyl-5H-pyrido[4,3-b]indole
-
i.e. Trp-P-1, 94% inhibition at 5 mM, IC50: 0.22 mM
3-amino-1-methyl-5H-pyrido[4,3-b]indole
-
i.e. Trp-P-2, 34% activation at 1 mM, 7% inhibition at 5 mM, IC50: 2.2 mM
3-Guanidinobenzamide
-
0.1 mM, 71% inhibition of the 116000 Da enzyme
4-nitro-7-[(1-oxo-1lambda(5)-pyridin-2-yl)sulfanyl]-2,1,3-benzoxadiazole
i.e. NSC228155
4-[8-fluoro-6-oxo-1H,2H,3H,4H,5H,6H-benzo[c]1,6-naphthyridin-2-yl]butanoic acid
-
4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4,6,7-hexahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]-N,N-dimethylpiperidine-1-carboxamide
-
activates in presence of Mg2+, inhibits in absence of Mg2+
8-fluoro-2-[3-(piperidin-1-yl)propanesulfonyl]-1H,2H,3H,4H,5H,6H-benzo[c]1,6-naphthyridin-6-one
-
8-fluoro-2-[3-(piperidin-1-yl)propyl]-1H,2H,3H,4H,5H,6H-benzo[c]1,6-naphthyridin-6-one
-
Alpha-NAD+
-
0.5 mM, 40% inhibition of the 116000 Da enzyme, 44% inhibition of the 90000 Da enzyme
carsalam
-
5 mM, 88% inhibition in presence of Mg2+, 68% inhibition in absence of Mg2+
deoxyshikonin
67% inhibition at 0.01 mM; 67% inhibition at 0.01 mM
DMSO
at 2% (v/v) DMSO isoform ARTD10 loses more than half of its activity; at 2% (v/v) DMSO isoform ARTD7 loses its activity completely
EB-47
i.e. 5'-deoxy-5'-[4-[2-[(2,3-dihydro-1-oxo-1H-isoindol-4-yl)amino]-2-oxoethyl]-1-piperazinyl]-5'-oxoadenosine dihydrochloride; i.e. 5'-deoxy-5'-[4-[2-[(2,3-dihydro-1-oxo-1H-isoindol-4-yl)amino]-2-oxoethyl]-1-piperazinyl]-5'-oxoadenosine dihydrochloride
exosin
-
a small molecule inhibitor, that modulates ExoS ADP-ribosyltransferase activity in vitro, suggesting the inhibition is direct. Exosin and two of its analogues display a significant protective effect against Pseudomonas infection in vivo, competitive against NAD+
gambogic acid
75% inhibition at 0.01 mM; 75% inhibition at 0.01 mM
Isoquinoline
-
5 mM, 47% inhibition in presence of Mg2+, 34% inhibition in absence of Mg2+
methyl (2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanoate
-
N-(5,6-dihydro-6-oxo-2-phenanthridinyl)-2-(dimethylamino)acetamide
PJ34, millimolar inhibitor
-
N-(6-oxo-5,6-dihydrophenanthrolin-2-yl)-(N,N-dimethylamino)acetamide
-
0.1 mM, remaining activity: 36.2%
N-[(1R)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(1S)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(2S)-1-hydroxy-3-phenylpropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(2S)-1-hydroxybutan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(2S)-1-hydroxypropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[1-[4-(1H-imidazol-1-yl)phenyl]ethyl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[2-oxo-4-(phenylamino)-3,8a-dihydro-2H-chromen-3-yl]acetamide
-
N-[[1-(1H-pyrazolo[3,4-d]pyrimidin-4-yl)piperidin-3-yl]methyl]methanesulfonamide
W2E3J5
-
novobiocin
-
IC50: 2.2 mM, 5 mM, 90% inhibition in presence of Mg2+, 59% inhibition in absence of Mg2+
phenantridinone
i.e. 6(5H)-phenantridinone; i.e. 6(5H)-phenantridinone
Phthalazine
-
5 mM, 91% inhibition in presence of Mg2+, 79% inhibition in absence of Mg2+
Quinazoline
-
5 mM, 63% inhibition in presence of Mg2+, 50% inhibition in absence of Mg2+
TIQ-A
i.e. 4H-thieno[2,3-c]isoquinolin-5-one; i.e. 4H-thieno[2,3-c]isoquinolin-5-one
trimethylpsoralen
61% inhibition at 0.01 mM; 61% inhibition at 0.01 mM
xanthurenic acid
-
5 mM, 88% inhibition in presence of Mg2+, 65% inhibition in absence of Mg2+
3-aminobenzamide
10 mM, 47% inhibition; 10 mM, 47% inhibition
3-Aminophthalhydrazide
-
0.1 mM, 98% inhibition of the 116000 Da enzyme
3-Methoxybenzamide
-
0.01 mM, 85% inhibition of the 116000 Da enzyme, 84% inhibition of the 90000 Da enzyme; 1 mM, 96% inhibition of the 116000 Da enzyme, 95% inhibition of the 90000 Da enzyme
Caffeine
-
1 mM, 86% inhibition of the 116000 Da enzyme, 57% inhibition of the 90000 Da enzyme
nicotinamide
-
1 mM, 96% inhibition of the 116000 Da enzyme, 95% inhibition of the 90000 Da enzyme
olaparib
i.e. 4-[(3-[(4-cyclopropylcarbonyl)piperazin-4-yl]carbonyl)-4-fluorophenyl]methyl(2H)phthalazin-1-one; i.e. 4-[(3-[(4-cyclopropylcarbonyl)piperazin-4-yl]carbonyl)-4-fluorophenyl]methyl(2H)phthalazin-1-one
theophylline
-
1 mM, 68% inhibition of the 116000 Da enzyme, 39% inhibition of the 90000 Da enzyme
thymidine
-
1 mM, 94% inhibition of the 116000 Da enzyme, 88% inhibition of the 90000 Da enzyme
additional information
-
comparison of the effects of heterocyclic amines acting as potent carcinogens on PARP-1 and the arginine-specific mono-ADP-ribosyltransferase A, MART-A, EC 2.4.2.31, overview
-
additional information
-
PARP inhibitors promote ATM activation through induction of double strand breaks
-
additional information
-
identification of small molecule inhibitors of Pseudomonas aeruginosa exoenzyme S using a yeast phenotypic screening, overview
-
additional information
-
phenanthroline has no or a slightly activating effect
-
additional information
phenanthroline has no or a slightly activating effect
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-amino-1-methyl-5H-pyrido[4,3-b]indole
-
i.e. Trp-P-2, 34% activation at 1 mM, 7% inhibition at 5 mM, IC50: 2.2 mM
4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4,6,7-hexahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]-N,N-dimethylpiperidine-1-carboxamide
-
activates in presence of Mg2+, inhibits in absence of Mg2+
Bmh1p
-
a yeast homologue of the human FAS, acts as an activating ExoS cofactor, overview
-
FAS
-
exoenzyme S absolutely requires a soluble eukaryotic protein, named FAS (Factor Activating exoenzyme E), in order to ADP-ribosylate all substrates. In the presence of FAS, exoenzyme S ADP-ribosylates several proteins in lysates of Pseudomonas aeruginosa. Purification and characterization of FAS
-
harmaline hydrochloride
-
activates more strongly in absence of Mg2+ than in presence of Mg2+
oligodeoxyribonucleotides
slightly enhance enzyme activity with the maximal increase of 50% as compared to the control
Phthalic acid
-
activates more strongly in absence of Mg2+ than in presence of Mg2+
DNA
-
the enzyme is completely dependent on the presence of DNA containing single or double stranded breaks. Activation results in a decondensation of chromatin superstructure in vitro, which is caused mainly by hyper(ADP-ribosyl)ation of histone H1
protein 14-3-3
-
required, interaction analysis, interaction equires residues L426, D427, and L428, overview, binding study of mutant enzymes, overview
-
additional information
-
stable expression of the transcription factor tonicity-responsive enhancer/osmotic response element-binding protein, TonEBP/OREBP, clone KIAA0827/amino acids 1-547, in HEK-293 cells increases the expression of the enzyme
-
additional information
-
DNA binding by PARP-1 triggers its activity and it adds poly(ADP-ribose) polymers to itself and to surrounding histones, overview
-
additional information
-
PARP-1 is activated in response to DNA damage and participates in DNA repair, genomic integrity and cell death
-
additional information
-
in native conformation, CRM66 shows limited ability to modify EF-2 covalently. Upon activation with urea and dithiothreitol CRM66 loses ADP-ribosylation activity entirely, yet it retains the ability to bind NAD+. Replacement of Tyr-426 with histidine in CRM66 completely restores cytotoxicity and ADP-ribosyltransferase activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.017
(ADP-D-ribosyl)n-RhoA protein
W2E3J5
at pH 7.4 and 37°C
-
0.011
(ADP-D-ribosyl)n-actin
mutant N86A, 25°C, pH not specified in the publication
0.02
(ADP-D-ribosyl)n-actin
mutant E213A, 25°C, pH not specified in the publication
0.023
(ADP-D-ribosyl)n-actin
mutant E215A, 25°C, pH not specified in the publication
0.024
(ADP-D-ribosyl)n-actin
wild-type, 25°C, pH not specified in the publication
0.033
(ADP-D-ribosyl)n-actin
mutant S178A, 25°C, pH not specified in the publication
0.035
(ADP-D-ribosyl)n-actin
mutant Y82A, 25°C, pH not specified in the publication
0.037
(ADP-D-ribosyl)n-actin
mutant Y77A, 25°C, pH not specified in the publication
0.03
(ADP-D-ribosyl)n-soybean-trypsin-inhibitor
-
recombinant full-length enzyme
-
0.037
(ADP-D-ribosyl)n-soybean-trypsin-inhibitor
-
recombinant DELTAN222
-
0.004
NAD+
mutant N86A, 25°C, pH not specified in the publication
0.005
NAD+
mutant E213A, 25°C, pH not specified in the publication
0.008
NAD+
mutant Y77A, 25°C, pH not specified in the publication
0.011
NAD+
pH and temperature not specified in the publication
0.012
NAD+
mutant Y82A, 25°C, pH not specified in the publication
0.014
NAD+
mutant E215A, 25°C, pH not specified in the publication
0.018
NAD+
mutant S178A, 25°C, pH not specified in the publication
0.031
NAD+
pH and temperature not specified in the publication
0.035
NAD+
pH and temperature not specified in the publication
0.159
NAD+
pH and temperature not specified in the publication
0.251
NAD+
pH and temperature not specified in the publication
additional information
additional information
-
kinetics for NAD+ utilization are not Michaelis-Menten type
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
(ADP-D-ribosyl)n-actin
mutant E215A, co-substrate: NAD+, 25°C, pH not specified in the publication
0.11
(ADP-D-ribosyl)n-actin
mutant E213A, co-substrate: NAD+, 25°C, pH not specified in the publication
0.65
(ADP-D-ribosyl)n-actin
mutant Y82A, co-substrate: NAD+, 25°C, pH not specified in the publication
1.3
(ADP-D-ribosyl)n-actin
mutant Y77A, co-substrate: NAD+, 25°C, pH not specified in the publication
1.38
(ADP-D-ribosyl)n-actin
mutant S178A, co-substrate: NAD+, 25°C, pH not specified in the publication
9.35
(ADP-D-ribosyl)n-actin
mutant N86A, co-substrate: NAD+, 25°C, pH not specified in the publication
22
(ADP-D-ribosyl)n-actin
wild-type, co-substrate: NAD+, 25°C, pH not specified in the publication
0.0031
(ADP-D-ribosyl)n-soybean-trypsin-inhibitor
-
recombinant DELTAN222
-
0.008
(ADP-D-ribosyl)n-soybean-trypsin-inhibitor
-
recombinant full-length enzyme
-
0.05
NAD+
mutant E215A, co-substrate: (ADP-D-ribosyl)n-actin, 25°C, pH not specified in the publication
0.11
NAD+
mutant E213A, co-substrate: (ADP-D-ribosyl)n-actin, 25°C, pH not specified in the publication
0.65
NAD+
mutant Y82A, co-substrate: (ADP-D-ribosyl)n-actin, 25°C, pH not specified in the publication
1.3
NAD+
mutant Y77A, co-substrate: (ADP-D-ribosyl)n-actin, 25°C, pH not specified in the publication
1.38
NAD+
mutant S178, co-substrate: (ADP-D-ribosyl)n-actin, 25°C, pH not specified in the publication
9.35
NAD+
mutant N86A, co-substrate: (ADP-D-ribosyl)n-actin, 25°C, pH not specified in the publication
22
NAD+
wild-type, co-substrate: (ADP-D-ribosyl)n-actin, 25°C, pH not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0075
2-(4-[4-[(2,4-dimethoxyphenyl)amino]quinazolin-2-yl]piperazin-1-yl)ethanol
25°C, pH not specified in the publication
0.003
2-[[3-(dimethylamino)-2-oxopropyl]amino]-5,6-dihydrophenanthridin-6-one
wild type enzyme, at pH 7.9 and 22°C
0.00862
3-(4-oxo-3,5,6,7-tetrahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-2-yl)propanoic acid
-
at pH 7.5 and 22°C
0.018 - 0.024
4-[8-fluoro-6-oxo-1H,2H,3H,4H,5H,6H-benzo[c]1,6-naphthyridin-2-yl]butanoic acid
0.007
8-fluoro-2-[3-(piperidin-1-yl)propanesulfonyl]-1H,2H,3H,4H,5H,6H-benzo[c]1,6-naphthyridin-6-one
wild type enzyme, at pH 7.9 and 22°C
0.019
8-fluoro-2-[3-(piperidin-1-yl)propyl]-1H,2H,3H,4H,5H,6H-benzo[c]1,6-naphthyridin-6-one
wild type enzyme, at pH 7.9 and 22°C
0.0041
N-(acridin-9-yl)-4-nitrobenzamide
25°C, pH not specified in the publication
0.0041
N-[2-oxo-4-(phenylamino)-3,8a-dihydro-2H-chromen-3-yl]acetamide
25°C, pH not specified in the publication
0.011
N-[[1-(1H-pyrazolo[3,4-d]pyrimidin-4-yl)piperidin-3-yl]methyl]methanesulfonamide
W2E3J5
at pH 7.4 and 37°C
0.018
4-[8-fluoro-6-oxo-1H,2H,3H,4H,5H,6H-benzo[c]1,6-naphthyridin-2-yl]butanoic acid
wild type enzyme, at pH 7.9 and 22°C
0.024
4-[8-fluoro-6-oxo-1H,2H,3H,4H,5H,6H-benzo[c]1,6-naphthyridin-2-yl]butanoic acid
wild type enzyme, at pH 7.9 and 22°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
(1E,4E)-1,5-di(pyridin-3-yl)penta-1,4-dien-3-one
Bordetella pertussis
at pH 7.5 and 25°C
0.0038
(2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanamide
Homo sapiens
pH and temperature not specified in the publication
0.0524
2-(3-hydroxypropyl)-3,5,6,7-tetrahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-4-one
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.169
2-(3-hydroxypropyl)-5,6,7,8-tetrahydro[1]benzothieno[2,3-d]pyrimidin-4(3H)-one
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.294
3-(4-methoxy-6,7-dihydro-5H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-2-yl)propanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.0479
3-(4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl)propanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.1
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-(pyridin-2-yl)ethyl]propanamide
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.0152
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-phenylethyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0013
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-(pyridin-2-yl)ethyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0009
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylethyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0022
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylpropyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0144
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[1-(4-sulfamoylphenyl)ethyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.135
3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.019
3-(4-oxo-3,5,6,7-tetrahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-2-yl)propanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.22
3-amino-1,4-dimethyl-5H-pyrido[4,3-b]indole
Bos taurus
-
i.e. Trp-P-1, 94% inhibition at 5 mM, IC50: 0.22 mM
2.2
3-amino-1-methyl-5H-pyrido[4,3-b]indole
Bos taurus
-
i.e. Trp-P-2, 34% activation at 1 mM, 7% inhibition at 5 mM, IC50: 2.2 mM
0.0068
4,5,7,9-tetrahydro-2H-purine-2,8(3H)-dithione
Bordetella pertussis
at pH 7.5 and 25°C
0.0017
4-(2-fluorophenoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0019
4-(2-phenoxyethoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0013
4-(4-aminophenoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00018
4-(4-carbamoylphenoxy)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00071
4-(4-formylphenoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0018
4-(4-hydroxyphenoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0014
4-(4-methoxyphenoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0249
4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.0014
4-(benzyloxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00072
4-butoxybenzamide
Homo sapiens
pH and temperature not specified in the publication
0.0073
4-carbamoylphenyl benzoate
Homo sapiens
pH and temperature not specified in the publication
0.0035
4-ethoxybenzamide
Homo sapiens
pH and temperature not specified in the publication
0.003
4-nitro-7-[(1-oxo-1lambda(5)-pyridin-2-yl)sulfanyl]-2,1,3-benzoxadiazole
Bordetella pertussis
at pH 7.5 and 25°C
0.0011
4-phenoxybenzamide
Homo sapiens
pH and temperature not specified in the publication
0.0038
4-[(2-bromophenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00023
4-[(2-fluorophenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0045
4-[(3,5-dimethylphenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0022
4-[(3-bromophenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0033
4-[(3-fluorophenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0079
4-[(4-fluorophenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0093
4-[(4-methylphenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0014
4-[(naphthalen-1-yl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0013
4-[(propan-2-yl)oxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00135
4-[(pyridin-2-yl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.002
4-[[4-(aminocarbonyl)benzyl]oxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00118
EB-47
Homo sapiens
isoform ARDT10, pH and temperature not specified in the publication
0.0022
methyl (2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanoate
Homo sapiens
pH and temperature not specified in the publication
0.0858
N-(acridin-9-yl)-4-nitrobenzamide
Aeromonas hydrophila
25°C, pH not specified in the publication
0.1
N-[(1R)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.1
N-[(1S)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.001
N-[(2S)-1-hydroxy-3-phenylpropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0096
N-[(2S)-1-hydroxybutan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0111
N-[(2S)-1-hydroxypropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0132
N-[1-[4-(1H-imidazol-1-yl)phenyl]ethyl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.086
N-[2-oxo-4-(phenylamino)-3,8a-dihydro-2H-chromen-3-yl]acetamide
Aeromonas hydrophila
25°C, pH not specified in the publication
2.2
novobiocin
Bos taurus
-
IC50: 2.2 mM, 5 mM, 90% inhibition in presence of Mg2+, 59% inhibition in absence of Mg2+
0.000232
TIQ-A
Homo sapiens
isoform ARDT7, pH and temperature not specified in the publication
0.0028
4-methoxybenzamide
Homo sapiens
pH and temperature not specified in the publication
0.000329
4-[4-(1-aminoethenyl)phenoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00033
4-[4-(1-aminoethenyl)phenoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.000925
olaparib
Homo sapiens
isoform ARDT7, pH and temperature not specified in the publication
0.00204
olaparib
Homo sapiens
isoform ARDT10, pH and temperature not specified in the publication
0.000745
phenantridinone
Homo sapiens
isoform ARDT10, pH and temperature not specified in the publication
0.00114
phenantridinone
Homo sapiens
isoform ARDT7, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.5
-
pH 7.0: about 75% of maximal activity, pH 9.5: about 70% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
80
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.3
-
isoelectric focusing. ExoS shows pI heterogeneity, that is independent of a mass change and thus represents molecular charge conformers
5.5
-
isoelectric focusing. ExoS shows pI heterogeneity, that is independent of a mass change and thus represents molecular charge conformers
5.7
-
isoelectric focusing. ExoS shows pI heterogeneity, that is independent of a mass change and thus represents molecular charge conformers
5.9
-
isoelectric focusing. ExoS shows pI heterogeneity, that is independent of a mass change and thus represents molecular charge conformers
7 - 7.2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Saccharolobus solfataricus MT-4 / DSM 5833
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
transfectants expressing either ART2.2 with its native anchor (RT2.2-GPI) or ART2.2 with a grafted transmembrane anchor
brenda
-
PARP-1 in lung repair during recovery after hyperoxia, that is induced by 5-bromo-2-deoxyuridine, overview
brenda
-
PARP-1 in lung repair during recovery after hyperoxia, that is induced by 5-bromo-2-deoxyuridine, overview
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
TbSIR2RP1 is a nuclear protein that colocalizes with telomeric sequences and minichromosomes
brenda
-
localizes in eukaryotic cells to the perinuclear region
-
brenda
-
despite the absence of a signal peptide, the protein is efficiently exported into periplasm
-
brenda
additional information
additional information
-
residues 52-72, membrane localization domain within the N-terminus of ExoS, is necessary and sufficient for membrane localization within eukaryotic cells, plays a role in targeting of ExoS to eukaryotic signalling factors
-
brenda
additional information
-
residues 5172 represent a membrane localization domain, which targets ExoS to perinuclear vesicles within mammalian cells
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
disruption of PARP1 enzymatic activity causes nucleolar disintegration and aberrant localization of nucleolar-specific proteins. PARP1 mutants have increased accumulation of rRNA intermediates and a decrease in ribosome levels
malfunction
-
enzyme loss induces higher levels of cytokine production and downregulates ex-vivo apoptosis of splenocytes
malfunction
-
enzyme deletion results in teratozoospermia and male infertility in mice due to the formation of abnormally shaped fertilization-incompetent sperm, despite normal testis weights and sperm counts
malfunction
enzyme knockdown results in genomic instability and DNA damage hypersensitivity
metabolism
-
the lowest PARP activity, as well as the lowest quantum yield of PSII linear electron transport (FPSII) and photochemical quenching (qP), is found in outdoor during winter plants. In outdoor spring plants the recovery of photochemical activity associated to a poly(ADP-ribose)polymerase activity increase of about 50%, as compared to greenhouse plants, is observed
metabolism
the enzyme inhibits the activation of NF-kappaB and downstream target genes in response to interleukin-1beta and tumour necrosis factor-alpha, dependent on catalytic activity and poly-ubiquitin binding
metabolism
-
enzyme-induced ADP-ribosylation regulates multiple nonreceptor tyrosine kinases in vivo
metabolism
-
the enzyme PARP14 is an important modulator of the response to ATR-CHK1 pathway inhibitors
physiological function
the enzyme is a transcriptional repressor of aryl hydrocarbon receptor
physiological function
enzyme binding to human epithelial cells leads to protein internalization, impairs human epithelial monolayer integrity, induces cell rounding, and impacts on actin cytoskeleton
physiological function
-
the enzyme displays functional relevance for nuclear envelope stability and nuclear reorganization during spermiogenesis and is important for proper sperm head shaping
physiological function
enzyme binding to proliferating cell nuclear antigen is required for translesion DNA synthesis. The enzyme is required for genomic stability, DNA damage tolerance and mutagenesis
physiological function
-
the enzyme regulates the host immune response in vivo by targeting its kinases
physiological function
-
the enzyme is a potent regulator of interferon-I antiviral efficacy. The enzyme inhibits the interferon-I-activated signalling pathway. Mono-ADP-ribosylation of beta-transducin repeat-containing protein promotes interferon alpha/beta receptor subunit 1 ubiquitination and degradation
physiological function
the enzyme plays a key role in suppressing pathogen-triggered immunity and/or effector-triggered immunity
physiological function
isoform PARP1 is involved in nuclear factor-kappaB, JAK/STAT, Wnt-beta-catenin, MAPK, and PI3K/AKT signaling pathways
physiological function
isoform PARP2 is involved in the PI3K/AKT signaling pathway
physiological function
-
the induction of the enzyme signals DNA damage to the repair machinery and triggers the SOS response
physiological function
isoform PARP5a is involved in Wnt-beta-catenin, MAPK, and PI3K/AKT signaling pathways
physiological function
isoform PARP5b is involved in the Wnt-beta-catenin signaling pathway
physiological function
isoform PARP1 plays a role in DNA damage repair, where it is responsible for the recruitment of numerous DNA repair factors upon activation and PAR chain synthesis. PARP1 is specifically linked to base excision repair and nucleotide excision repair where it produces poly-ADP-ribosyl chains as scaffold for the DNA repair machinery
physiological function
the inactive isoform PARP13 is involved in the nuclear factor-kappaB signaling pathway
physiological function
-
the enzyme preferentially modifies potato genomic DNA, suggesting that it may function in modulating host gene expression during pathogen infection
physiological function
the enzyme plays a key role in suppressing pathogen-triggered immunity and/or effector-triggered immunity
physiological function
the enzyme is a major virulence factor secreted by Bordetella pertussis
physiological function
the enzyme plays a key role in suppressing pathogen-triggered immunity and/or effector-triggered immunity
physiological function
-
the enzyme plays a key role in suppressing pathogen-triggered immunity and/or effector-triggered immunity
-
physiological function
-
the enzyme is a major virulence factor secreted by Bordetella pertussis
-
physiological function
-
the enzyme plays a key role in suppressing pathogen-triggered immunity and/or effector-triggered immunity
-
Show AA Sequence and Transmembrane Helices (2799 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
116000
22000
25000
30000
90000
-
1 * 90000, two active proteins are detected: MW 90000 Da and 116000 Da, SDS-PAGE
116000
-
1 * 116000, two active proteins are detected: MW 90000 Da and 116000 Da, SDS-PAGE
22000
W2E3J5
x * 22000, calculated from amino acid sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
monomer
additional information
?
-
1 * 90000, two active proteins are detected: MW 90000 Da and 116000 Da, SDS-PAGE
?
-
1 * 116000, two active proteins are detected: MW 90000 Da and 116000 Da, SDS-PAGE
?
-
exoenzyme S activity and 53000 Da and 49000 Da proteins cofractionate, SDS-PAGE
?
-
exoenzyme S activity and 53000 Da and 49000 Da proteins cofractionate, SDS-PAGE
-
monomer
1 * 23400, recombinant C-terminally truncated enzyme, SDS-PAGE
monomer
-
1 * 23400, recombinant C-terminally truncated enzyme, SDS-PAGE
-
additional information
-
PARP-1 protein has an N-terminal DNA binding domain containing two large zinc fingers that bind to both DNA single-strand breaks and DNA double-strand breaks
additional information
-
structural and functional organizations of PARP-1 and PARP-2, overview
additional information
-
the N-terminus with amino acids 96219 encodes a Rho GTPase activating protein domain, the C-terminus with amino acids 234453 encodes a 14-3-3-dependent ADP-ribosyltransferase domain
additional information
-
the bifunctional ExoT contains an N-terminal GTPase-activating protein domain, GAP domain, and a C-terminal ADP-ribosyl transferase domain, ADPRT domain
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the full-length form is processed to a soluble fragment, which possesses both the GAP and ADP-ribosyltransferase activities
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
S1 subunit of mutant C41S in complex with NAD+, ADP-ribose plus nicotinamide, PJ34, and 3-aminobenzamide plus NAD+, hanging drop vapor diffusion method, using 25% (w/v) PEG 3350, 0.2 M potassium iodide (NAD+), 0.5 M (NH4)2SO4 and 0.1 M HEPES, pH 7.0 (ADP-ribose plus nicotinamide), 0.15 M NaCl, 0.1 M Tris(hydroxymethyl)aminomethane, pH 8.0 and 8% (w/v) PEG 8000 (PJ34), 0.2 M LiCl and 14% (w/v) PEG 3350 (3-aminobenzamide plus NAD+)
hanging drop vapor diffusion method, using 28% (w/v) PEG 4000, 200 mM sodium acetate, and 100 mM Tris, pH 8.5
W2E3J5
structures of complexes between wild-type and two mutant enzymes (E189I and E189A) on the one hand and the substrate analogues beta-methylenethiazole-4-carboxamideadenine dinucleotide and NADH as well as the substrate NAD+ on the other
-
in complex with inhibitor PJ34 or P6, hanging drop vapor diffusion method, using 0.1 M MES, pH 6.5, and 15% (w/v) PEG 400
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E213A
kcat highly decreased compared to wild-type, Km similar to wild-type
E215A
kcat highly decreased compared to wild-type, Km (ADP-D-ribosyl)n-actin similar to wild-type, Km (NAD+) increased compared to wild-type
N86A
kcat moderately decreased compared to wild-type, Km decreased compared to wild-type
S178A
kcat decreased compared to wild-type, Km increased compared to wild-type
Y77A
kcat decreased compared to wild-type, Km increased compared to wild-type
Y82A
kcat decreased compared to wild-type, Km increased compared to wild-type
Q127D
the mutant shows about 50% activity compared to the wild type enzyme
Q127D/E129D
Y63A
the mutant shows 5% activity compared to the wild type enzyme
Q127D
-
the mutant shows about 50% activity compared to the wild type enzyme
-
Q127D/E129D
Y63A
-
the mutant shows 5% activity compared to the wild type enzyme
-
Q217E
-
site-directed mutagenesis, the point mutation alters the asparagine-specificity of the enzyme to an arginie-specificity, the mutant does not show ADP-ribosyltransferase activity towards RhoA, but is still capable of NAD-binding and possesses NAD+ glycohydrolase activity, the mutant exoenzyme C3 is capable of ADP-ribosylation of poly-arginine, but not poly-asparagine, and shows high activity with Arg residues of soybean trypsin inhibitor
R151A
-
site-directed mutagenesis, the mutation does not alter the enzyme activity or its potential as substrate for the C3 mutant Q217E
R61A
-
site-directed mutagenesis, the mutation does not alter the enzyme activity or its potential as substrate for the C3 mutant Q217E
R86A
-
site-directed mutagenesis, the mutation does not alter the enzyme activity but its potential as substrate for the C3 mutant Q217E, which cannot ADP-ribosylate this mutant
G888W
DELTA24288
-
signal sequences necessary for export from the ER (at the amino terminus) and addition of a GPI-anchor (at the carboxyl terminus) are deleted. The resulting mutants retain the catalytic properties of the mature wild-type ART1. Their NADase activities relative to transferase activities are very low, and nicotinamide release is enhanced in the presence of the ADP-ribose acceptor, agmatine
DELTA24293
-
signal sequences necessary for export from the ER (at the amino terminus) and addition of a GPI-anchor (at the carboxyl terminus) are deleted. The resulting mutants retain the catalytic properties of the mature wild-type ART1. Their NADase activities relative to transferase activities are very low, and nicotinamide release is enhanced in the presence of the ADP-ribose acceptor, agmatine
R7K
D424A/D427A
-
site-directed mutagenesis, reduced interaction with 14-3-3, phenotypic analysis
D424A/L426A/D427A/L428A
-
site-directed mutagenesis, the mutant shows a highly reduced expression level, phenotypic analysis
D427A
-
site-directed mutagenesis, the mutant shows a reduced expression level, phenotypic analysis
DELTAN222
DELTAN222/E381A
-
possesses 0.02% of the ADP-ribosyltransferase activity of DELTAN222. KM-value for (ADP-D-ribosyl)n-soybean-trypsin-inhibitor is 8.7fold higher than the KM-value for DELTAN222
DELTAN222/E381D
-
possesses 0.6% of the ADP-ribosyltransferase activity of DELTAN222. KM-value for (ADP-D-ribosyl)n-soybean-trypsin-inhibitor is 7.9fold higher than the KM-value for DELTAN222
DELTAN222/E381S
-
possesses 0.01% of the ADP-ribosyltransferase activity of DELTAN222. KM-value for (ADP-D-ribosyl)n-soybean-trypsin-inhibitor is 4.7fold higher than the KM-value for DELTAN222
DELTAN222/E387A
-
possesses 31% of the ADP-ribosyltransferase activity of DELTAN222
DELTAN222/E399A
-
possesses 28% of the ADP-ribosyltransferase activity of DELTAN222
DELTAN222/E414A
-
possesses 20% of the ADP-ribosyltransferase activity of DELTAN222
E379D
-
mutation inhibits expression of ADP-ribosyltransferase activity, but has little effect on the expression of NAD glycohydrolase activity
E381D
L426A/D427A
-
site-directed mutagenesis, the mutant shows a highly reduced expression level and slightly reduced cytotoxicity, no interaction with 14-3-3, phenotypic analysis
L426A/D427A/L428A
-
site-directed mutagenesis, the mutant shows a highly reduced expression level and cytotoxicity, no interaction with 14-3-3, phenotypic analysis
L428A
-
site-directed mutagenesis, reduced interaction with 14-3-3, the mutant shows highly reduced cytotoxicity, phenotypic analysis
R146K
-
site-directed mutagenesis, the mutation within the active site for the RhoGAP domain
R146K/E379/381D
-
inactive mutant, does not inhibit Pseudomonas aeruginosa internalization into ExoS-transfected HeLa cells in contrast to the wild-type enzyme
Y426H
-
in native conformation, CRM66 shows limited ability to modify EF-2 covalently. Upon activation with urea and dithiothreitol CRM66 loses ADP-ribosylation activity entirely, yet it retains the ability to bind NAD+. Replacement of Tyr-426 with histidine in CRM66 completely restores cytotoxicity and ADP-ribosyltransferase activity
E381D
R146K
-
site-directed mutagenesis, the mutation within the active site for the RhoGAP domain
-
R146K/E379/381D
-
inactive mutant, does not inhibit Pseudomonas aeruginosa internalization into ExoS-transfected HeLa cells in contrast to the wild-type enzyme
-
Q158A/E160A
E118A
mutation reduces the toxicity of the enzyme and still allows small colonies to grow
E171A
mutation reduces the toxicity of the enzyme and still allows small colonies to grow
F129A
I176A
mutation reduces the toxicity of the enzyme and still allows small colonies to grow
E165A
Tequatrovirus T4 ModA
-
mutation in ModA reduces the toxicity to colony growth
-
F127A
Tequatrovirus T4 ModA
-
mutation in ModA reduces the toxicity to colony growth
-
F129A
Tequatrovirus T4 ModA
-
mutation in ModA reduces the toxicity to colony growth
-
R72A
Tequatrovirus T4 ModA
-
mutation in ModA reduces the toxicity to colony growth
-
S109A
Tequatrovirus T4 ModA
-
mutation in ModA reduces the toxicity to colony growth
-
E165A
Tequatrovirus T4 ModB
-
mutation in ModA reduces the toxicity to colony growth
-
F127A
Tequatrovirus T4 ModB
-
mutation in ModA reduces the toxicity to colony growth
-
F129A
Tequatrovirus T4 ModB
-
mutation in ModA reduces the toxicity to colony growth
-
R72A
Tequatrovirus T4 ModB
-
mutation in ModA reduces the toxicity to colony growth
-
S109A
Tequatrovirus T4 ModB
-
mutation in ModA reduces the toxicity to colony growth
-
additional information
Q127D/E129D
the mutant shows drastically diminished activity compared to the wild type enzyme
Q127D/E129D
-
the mutant shows drastically diminished activity compared to the wild type enzyme
-
DELTAN222
-
carboxyl-terminal 222 amino acids of exoenzyme S, catalyzes the ADP-ribosylation of soybean trypsin inhibitor at a rate sixfold greater than rHisExoS. Relative to rHisExoS, DN222 has a similar affinity for NAD, a threefold greater affinity for soybean trypsin inhibitor, and a four- to eight-fold greater turnover number for the ADP-ribosylation of soybean trypsin inhibitor. DN222 does not chromatograph as an aggregate, which shows that the amino-terminal 99 amino acids of exoenzyme S are responsible for the aggregation phenotype
E381D
-
mutant deficient in ADP-ribosyltransferase activity, possesses pI heterogeneity that is different than that of auto-ADP-ribosylated wild-type ExoS
E381D
-
mutation inhibits expression of both ADP-ribosyltransferase activity and NAD glycohydrolase activity
E381D
-
site-directed mutagenesis, the mutation within the active site for the ADPr domain
E381D
-
mutant deficient in ADP-ribosyltransferase activity, possesses pI heterogeneity that is different than that of auto-ADP-ribosylated wild-type ExoS
-
E381D
-
site-directed mutagenesis, the mutation within the active site for the ADPr domain
-
Q158A/E160A
the mutant shows reduced activity compared to the wild type enzyme
Q158A/E160A
-
the mutant shows reduced activity compared to the wild type enzyme
-
additional information
-
phenotypes of isozyme-deficient mutant mice, overview
additional information
-
analysis of polymorphisms of PARP-1 promoter sequence in Parkinson patients, variations in the regulatory region are probably involved in increased risk for the disease, overview
additional information
-
stable expression of the transcription factor tonicity-responsive enhancer/osmotic response element-binding protein, TonEBP/OREBP, amino acids 1-547, in HEK-293 cells increases the expression of the enzyme
additional information
-
PARP-1 knockout mice are viable, fertile and do not develop early onset tumors, cells isolated from these mice show an increased level of homologous recombination
additional information
-
knockout mice show increased inflammatory response in PARP-1 -/- compared to wild-type animals, characterized by neutrophil infiltration and increased IL-6 levels in broncho-alveolar lavages, the lesions are reversible, since the extent of the hyperplastic regions is reduced after 21 days of recovery and do not result in fibrosis, phenotype, overview
additional information
-
establishment of an immortalized PARP-1-/- murine endothelial cell line HYKO6 by transfection of primary cells with a plasmid containing the SV40 genome, expression of epitopes for detection by antibodies, phenotype, overview
additional information
-
PARP-1 knockout mice are much less sensitive to inflammatory stress as a result of a diminished release of pro-inflammatory mediators, including nitric oxide, parp-1 knockout mice show reduced NO-induced oxidative injury and response to genotoxic damage during carcinogenesis and inflammation
additional information
-
downregulatory effect of PARP-1 on the p53-dependent regulation of recombination between SV40 minichromosomes in primate cell lines conditionally expressing exogenous PARP-1 in a wild-type p53-positive or -negative background, respectively, overview
additional information
-
effects of ADP-ribosylation of integrin alpha7 on the expression of the monoclonal anti-integrin antibody 9EG7 epitope in intact differentiated C2C12 cells in presence or absene of NAD+ and Mn2+, overview
additional information
-
establishment of an immortalized PARP-1-/- murine endothelial cell line HYKO6 by transfection of primary cells with a plasmid containing the SV40 genome, expression of epitopes for detection by antibodies, phenotype, overview
-
additional information
-
knockout mice show increased inflammatory response in PARP-1 -/- compared to wild-type animals, characterized by neutrophil infiltration and increased IL-6 levels in broncho-alveolar lavages, the lesions are reversible, since the extent of the hyperplastic regions is reduced after 21 days of recovery and do not result in fibrosis, phenotype, overview
-
additional information
-
the recombinant deletion protein N223-53 which contains the catalytic domain of Exo53, comprising its 223 carboxyl-terminal residues catalyzes the FAS-dependent ADP-ribosylation of soybean trypsin inhibitor at 0.4% and of the Ras protein at 1.0% of the rates of catalysis by N222-49 (a protein comprising the 222 carboxyl-terminal residues of ExoS, which represent its catalytic domain). N223-53 possesesses binding affinities for NAD+ and SBTI similar to those of N222-49 but shows a lower rate for the ADP-ribosylation of SBTI
additional information
-
enzyme is comprised of an N-terminal domain with GTPase activating protein activity towards Rho family GTPases and a C-terminal ADP ribosyl-transferase (ADPRT) domain with minimal activity towards a synthetic substrate in vitro. Deletion of a majority of the ADPRT domain (residues 234 to 438) or point mutations of the ADPRT catalytic site (residues 383 to 385) leads to distinct changes in host cell morphology and substantially reduces the ability of ExoT to inhibit in vitro epithelial wound healing over a 24-h period. In contrast, only subtle effects on the efficiency of ExoT-induced bacterial internalization are observed in the ADPRT mutant forms
additional information
-
the recombinant deletion protein N223-53 which contains the catalytic domain of Exo53, comprising its 223 carboxyl-terminal residues catalyzes the FAS-dependent ADP-ribosylation of soybean trypsin inhibitor at 0.4% and of the Ras protein at 1.0% of the rates of catalysis by N222-49 (a protein comprising the 222 carboxyl-terminal residues of ExoS, which represent its catalytic domain). N223-53 possesesses binding affinities for NAD+ and SBTI similar to those of N222-49 but shows a lower velocity rate for the ADP-ribosylation of SBTI
additional information
-
construction of a truncated ExoS mutant DELTA51-72
additional information
-
construction of an enzyme-deficient strain 388DELTAexoS
additional information
-
construction of an enzyme-deficient strain 388DELTAexoS
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap chelating Sepharose column chromatography and HiTrap Q-Sepharose column chromatography
HiTrap chelating Sepharose column chromatography, and Superdex 200 gel filtration
W2E3J5
Ni-NTA column chromatography, heparin column chromatography, and gel filtration
Ni2+ affinity resin column chromatography and Sephacryl S200 gel filtration
-
recombinant catalytic domain DELTAN22 and DELTAN222 mutants, expression in Escherichia coli
-
the membrane-binding domain (amino acids 51-72) is involved in membrane binding and aggregation, which complicates the purification schemes. Purification of recombinant forms of ExoS that lack the membrane binding domain, rExoS78-453 and rExoSDELTA51-72. Both forms possess Rho GAP activity and ADP ribosyltransferase activity comparable to wild-type ExoS
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
40 kDa carboxy-terminal catalytic fragment of PARP-1 comprising residues 6541014 is genetically expressed in insect cells (Spodoptera frugiperda, Sf9)
-
catalytic domain DELTAN22 and DELTAN222 mutants, expression in Escherichia coli
-
expressed in Escherichia coli as a soluble, cytosolic His function protein, rHisExoS
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta2 (DE3) cells
expression of ExoS in HeLa cells leads to a loss of phosphorylation of ERM proteins, overview, expression of wild-type and mutant ExoS in enzyme-deficient strain PA103, co-expression with 14-3-3
-
expression of ExoT and the isolated GAP and ADPRT enzyme domains, respectively, in A-549 cells
-
expression of the enzyme in HEK-293 cells using a luciferase reporter vector, PARP-1 expression analysis, overview
-
expression of various GST-fusion protein constructs of ExoS mutants in HeLa cells
-
expression of wild-type and mutant enzymes in Escherichia coli as GST-tagged proteins
-
gene PARP, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
-
gene parp-1, expression in LMV cells and subclones, derived from the parental line LLC-MK2 from rhesus monkey Macaca mulatta kidney, stably expressing the estradiol-inducible transcriptional transactivation factor Gal4ERVP
-
gene PARP1, chromosomal location 1q41-q42, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
gene PARP11, chromosomal location 12p13.3, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
gene PARP14, chromosomal location 3q21.1, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
gene PARP16, chromosomal location 15q22.2, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
gene PARP2, chromosomal location 14q11.2-q12, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
gene PARP3, chromosomal location 3p21.1-22.2, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
gene PARP4, chromosomal location 13q11, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
gene PARP6, chromosomal location 15q22.23, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
gene TNKS1, chromosomal location 8p23.1, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
PARP-1, DNA and amino acid sequence determination and analysis of wild-type and mutant genes
-
the ADP-ribosyltransferase domain of the protein is expressed in Saccharomyces cerevisiae strain MH272-3falpha and HeLa cells
-
trancriptional regulation, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is upregulated by virus infections, including vesicular stomatitis virus, herpes simplex virus-1 and influenza A virus, thus promoting ADP-ribosylation-mediated viral evasion
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
drug development
-
the enzyme can be a target for anti-bacterial treatment
molecular biology
pharmacology
-
the enzyme inhibition is a possible tool in cancer therapy both in prophylactic and therapeutic treatment, e.g. by targeting BRCA2 tumors with PARP inhibitors, overview
analysis
-
establishment of an immortalized PARP-1-/- murine endothelial cell line HYKO6 as a tool to study PARP-1-mediated endothelial cell dysfunction
analysis
-
establishment of an immortalized PARP-1-/- murine endothelial cell line HYKO6 as a tool to study PARP-1-mediated endothelial cell dysfunction
-
molecular biology
-
establishment of an immortalized PARP-1-/- murine endothelial cell line HYKO6 as a tool to study PARP-1-mediated endothelial cell dysfunction
molecular biology
-
establishment of an immortalized PARP-1-/- murine endothelial cell line HYKO6 as a tool to study PARP-1-mediated endothelial cell dysfunction
-
EXTERNAL LINKS (specific for EC-Number 2.4.2.30)
Transporter Classification Database (TCDB): 1.I.1.1.3
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
