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Information on EC 2.4.2.30 - NAD+ ADP-ribosyltransferase
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2.4.2.30 NAD+ ADP-ribosyltransferaseIUBMB 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.
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Word Map
- 2.4.2.30
-
polyadp-ribose
- caspase-3
- bcl-2
- breast
- ovarian
- necrosis
-
pro-apoptotic
-
annexin
- cyclin
- chromatin
- strand
-
anti-apoptotic
-
polyadp-ribosylation
- prostate
- leukemia
- mapks
-
tunel
-
adp-ribosylation
-
apoptosis-inducing
- cisplatin
- jnk
- histone
-
checkpoint
- rad51
-
caspase-dependent
- xiap
-
dna-damaging
- aif
-
apoptosis-related
- z-vad-fmk
- survivin
-
ladder
-
germline
-
triple-negative
-
sub-g1
-
antiproliferative
- polymerases
-
brca1/2
- analysis
- dna-pk
- molecular biology
-
lc3-ii
- h2ax
- botulinum
-
trail-induced
-
mitochondria-mediated
- chk1
-
platinum-based
-
mitochondria-dependent
- drug development
- pharmacology
-
pan-caspase
- xrcc1
- temozolomide
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
parp, parp-1, poly(adp-ribose) polymerase, parp1, poly (adp-ribose) polymerase, poly(adp-ribose) polymerase-1, c3 exoenzyme, adprt, exoenzyme s, poly (adp-ribose) polymerase-1, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADP-ribosylating thermozyme
ADP-ribosyltransferase
ADP-ribosyltransferase C3cer
ADP-ribosyltransferase-1
ADPr
ADPRT
ART
ARTD10
C3larvin toxin
exoenzyme C3
exoenzyme S
ExoS
ExoT
exotoxin-S
ModA
ModB
mono-ADP-ribosyltransferase
NarE
PAR polymerase
PARP
PARP-1
PARPss
poly(ADP-ribose) polymerase
poly(ADP-ribose) polymerase-1
scabin
TTS-ExoS
additional information
exoenzyme S
-
-
ExoS
-
-
ExoS
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bifunctional type-III cytotoxin with an N-terminal RhoGAP domain and and C-terminal ADP-ribosylation domain
ExoS
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bifunctional type-III cytotoxin. Residues 96–233 comprise the Rho GTPase-activating protein domain, while residues 234–453 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
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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
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
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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+
E219 and Gln217 of the ARTT-motif, i.e. ADP-ribosylating turn-turn motif, are essential for activity
-
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+
mechanism and physiological function, overview
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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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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.
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CAS REGISTRY NUMBER
COMMENTARY
58319-92-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NAD+ + (ADP-D-ribosyl)n-(EF-2)
nicotinamide + (ADP-D-ribosyl)n+1-(EF-2)
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-actin
nicotinamide + (ADP-D-ribosyl)n+1-actin
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
-
?
NAD+ + (ADP-D-ribosyl)n-apolipoprotein
nicotinamide + (ADP-D-ribosyl)n+1-apolipoprotein
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-aryl hydrocarbon receptor
nicotinamide + (ADP-D-ribosyl)n+1-aryl hydrocarbon receptor + H+
-
-
?
NAD+ + (ADP-D-ribosyl)n-Crk-I
nicotinamide + (ADP-D-ribosyl)n+1-Crk-I
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-Crk-II
nicotinamide + (ADP-D-ribosyl)n+1-Crk-II
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-His6HRas
nicotinamide + (ADP-D-ribosyl)n+1-His6HRas
-
the enzyme preferentially ADP-ribosylates membrane-associated His6HRas relative to its cytosolic His6HRasDELTACAAX with a C-terminal deletion
-
?
NAD+ + (ADP-D-ribosyl)n-immunoglobulin A
nicotinamide + (ADP-D-ribosyl)n+1-immunoglobulin A
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-immunoglobulin G
nicotinamide + (ADP-D-ribosyl)n+1-immunoglobulin G
-
preferentially IgG3
-
?
NAD+ + (ADP-D-ribosyl)n-NEMO protein
nicotinamide + (ADP-D-ribosyl)n+1-NEMO protein + H+
the enzyme prevents poly-ubiquitination of NEMO protein
-
?
NAD+ + (ADP-D-ribosyl)n-P2X7 ion channel
nicotinamide + (ADP-D-ribosyl)n+1-P2X7 ion channel + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-peptide LL-37
nicotinamide + (ADP-D-ribosyl)n+1-peptide LL-37 + H+
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
-
?
NAD+ + (ADP-D-ribosyl)n-Rab2
nicotinamide + (ADP-D-ribosyl)n+1-Rab2
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-Rab3
nicotinamide + (ADP-D-ribosyl)n+1-Rab3
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-Rap1A
nicotinamide + (ADP-D-ribosyl)n+1-Rap1A
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-Ras protein
nicotinamide + (ADP-D-ribosyl)n+1-Ras protein
-
-
-
?
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+
-
-
?
NAD+ + (ADP-D-ribosyl)n-soybean trypsin inhibitor
nicotinamide + (ADP-D-ribosyl)n+1-soybean trypsin inhibitor
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-soybean-trypsin-inhibitor
nicotinamide + (ADP-D-ribosyl)n+1-soybean-trypsin-inhibitor
-
-
-
?
NAD+ + GTPase RhoA
nicotinamide + (ADP-D-ribosyl)-GTPase RhoA
-
the exoenzyme modifies the low-molecular-mass GTPases RhoA, B, and C specifically at Asn41
-
?
NAD+ + GTPase RhoB
nicotinamide + (ADP-D-ribosyl)-GTPase RhoB
-
the exoenzyme modifies the low-molecular-mass GTPases RhoA, B, and C specifically at Asn41
-
?
NAD+ + GTPase RhoC
nicotinamide + (ADP-D-ribosyl)-GTPase RhoC
-
the exoenzyme modifies the low-molecular-mass GTPases RhoA, B, and C specifically at Asn41
-
?
NAD+ + poly(ADP-ribose) polymerase-1
nicotinamide + (ADP-ribosyl)-poly(ADP-ribose) polymerase-1
-
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
-
?
NAD+ + Ras
nicotinamide + (ADP-D-ribosyl)-Ras
-
interaction requires residue Leu428
-
?
NAD+ + Ras2p
nicotinamide + (ADP-D-ribosyl)-Ras2p + H+
-
Ras2p is a yeast protein, activity absolutely requires the yeast protein Bmh1p
-
?
NAD+ + soybean trypsin inhibitor
nicotinamide + (ADP-D-ribosyl)-soybean trypsin inhibitor
-
the exoenzyme modifies the substrate at an arginine residue
-
?
NAD+ + wild-type exoenzyme C3
nicotinamide + (ADP-D-ribosyl)-wild-type exoenzyme C3
-
activity of the recombinant mutant Q217E exoenzyme C3, modification at Arg86
-
?
nicotinamide 1,N6-ethenoadenine dinucleotide + (ADP-D-ribosyl)n-vH-Ras protein
nicotinamide + ?
integrin alpha7 + NAD+
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
-
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
-
?
integrin alpha7 + NAD+
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of histone H1
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
the enzyme is a DNA repair enzyme
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of 21000-24000 Da platelet membrane proteins
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
Cryptothecodinium cohnii
-
poly(ADP-ribosyl)ation of histone
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of histone H1
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of histone
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of topoisomerase I
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
auto-poly(ADP-ribosyl)ation
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of high mobility group proteins
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of DNA ligase
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of endonuclease
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of topoisomerase II
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of terminal deoxynucleotidyltransferase
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of histone H1
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of histone
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
catalyzes poly(ADP-ribosyl)ation of the synthetase itself, automodification
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of ADP-ribosyltransferase
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
agmatine as ADPribose acceptor is used
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ADPRT domain of ExoT is active in vivo and contributes to the pathogenesis of Pseudomonas aeruginosa infections
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
intracellular Ras is modified by bacterially translocated ExoS, inhibition of target cell proliferation correlates with the efficiency of Ras modification
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoT ADP-ribosylates a restricted subset of host proteins including the Crk proteins
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoT ADP-ribosylates a restricted subset of host proteins including the Crk proteins
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoT ADP-ribosylates a restricted subset of host proteins including the Crk proteins
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
?
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+
-
-
?
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+
-
-
-
?
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+
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
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
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Saccharolobus solfataricus MT-4 / DSM 5833
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Saccharolobus solfataricus MT-4 / DSM 5833
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
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
-
?
NAD+ + (ADP-D-ribosyl)n-biotin
nicotinamide + (ADP-D-ribosyl)n+1-biotin + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-biotin
nicotinamide + (ADP-D-ribosyl)n+1-biotin + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-p21ras
nicotinamide + (ADP-D-ribosyl)n+1-p21ras
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-p21ras
nicotinamide + (ADP-D-ribosyl)n+1-p21ras
-
ADP-ribosylation of p21ras does not alter interactions with guanidine nucleotides. Possible function of the enzyme in pathogenesis
-
?
NAD+ + (ADP-D-ribosyl)n-rab4
nicotinamide + (ADP-D-ribosyl)n+1-rab4
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-rab4
nicotinamide + (ADP-D-ribosyl)n+1-rab4
-
ADP-ribosylation affects Rab4 function in membrane recycling
-
?
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5
-
ADP-ribosylation of Rab5 by ExoS affects endocytosis. Interaction of Rab5 with endosome antigen 1 is markedly diminished after Rab5 ADP-ribosylation by ExoS
-
?
NAD+ + (ADP-D-ribosyl)n-RalA
nicotinamide + (ADP-D-ribosyl)n+1-RalA
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-RalA
nicotinamide + (ADP-D-ribosyl)n+1-RalA
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-Ras
nicotinamide + (ADP-D-ribosyl)n+1-Ras
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-Ras
nicotinamide + (ADP-D-ribosyl)n+1-Ras
-
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
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
-
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
-
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
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
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
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
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
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
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
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
-
?
NAD+ + histone H2A
nicotinamide + (ADP-D-ribosyl)-histone H2A
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
-
?
NAD+ + histone H2A
nicotinamide + (ADP-D-ribosyl)-histone H2A
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B
-
?
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
-
?
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B
-
?
NAD+ + moesin
nicotinamide + (ADP-D-ribosyl)-moesin
-
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
-
?
NAD+ + moesin
nicotinamide + (ADP-D-ribosyl)-moesin
-
modification of Arg553, Arg560 and Arg563, activity with wild-type and mutant moesins, overview
-
?
NAD+ + p53
nicotinamide + (ADP-D-ribosyl)-p53
-
PARP-1 interacts with and poly(ADP-ribosyl)ates p53, which participates in DNA recombination
-
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Rab5 mediates entry of the EGFR into early endosomes
-
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Rab5 mediates entry of the EGFR into early endosomes
-
?
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
-
-
-
?
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
-
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
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
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
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
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
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
-
?
NAD+ + topoisomerase I
nicotinamide + (ADP-D-ribosyl)-topoisomerase I
-
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
-
?
nicotinamide 1,N6-ethenoadenine dinucleotide + (ADP-D-ribosyl)n-vH-Ras protein
nicotinamide + ?
-
-
-
?
nicotinamide 1,N6-ethenoadenine dinucleotide + (ADP-D-ribosyl)n-vH-Ras protein
nicotinamide + ?
-
-
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
the enzyme modifies eukaryotic 21000-24000 Da GTP-binding proteins
-
?
additional information
?
-
-
transcriptional regulation mechanism, overview
-
?
additional information
?
-
-
the enzyme also shows NAD+-hydrolase activity
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
the enzyme is involved in pathogenesis of Parkinson's disease, analysis of polymorphisms, overview
-
?
additional information
?
-
-
the enzyme shows DNA-binding activity, and is physically associated with the transcription factor tonicity-responsive enhancer/osmotic response element-binding protein, TonEBP/OREBP
-
?
additional information
?
-
-
the enzyme has the ability to ADP-ribosylate itself
-
?
additional information
?
-
-
raft association focuses ART2.2 on specific targets that constitutively or inducibly assoiate with lipid rafts
-
?
additional information
?
-
-
PARP-1 is involved in modulation of NO-derived injury and response to genotoxic damage
-
?
additional information
?
-
-
PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
the enzyme is involved in endothelial cell dysfunction
-
?
additional information
?
-
-
transcriptional regulation mechanism, overview
-
?
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, DNA binding by PARP-1 triggers its activity and it adds poly(ADP-ribose) polymers to itself and to surrounding histones, overview
-
?
additional information
?
-
-
the enzyme itself is a target for P2X7-triggered ectodomain shedding at F239/S240
-
?
additional information
?
-
-
the enzyme is involved in endothelial cell dysfunction
-
?
additional information
?
-
-
PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
-
?
additional information
?
-
-
narE possesses ADP-ribosylating and NAD-glycohydrolase activities
-
?
additional information
?
-
-
exoenzyme S and 14-3-3 interact in a direct fashion, interaction involves the conserved amphiphatic groove of 14-3-3
-
?
additional information
?
-
-
exoenzyme S is an important adhesin
-
?
additional information
?
-
-
ExoS is a virulence factor of the pathogen
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
exoenzyme S is a bifunctional type III secretion, TTS, effector protein, with GTPase-activating and ADP-ribosyltransferase activities
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
ExoS is a bi-functional type III cytotoxin that possesses Rho GTPase activating protein and ADP-ribosyltransferase activities, no activity with Rab4 protein, overview
-
?
additional information
?
-
-
exoenzyme S is a bifunctional type III secretion, TTS, effector protein, with GTPase-activating and ADP-ribosyltransferase activities
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
ExoS is a bi-functional type III cytotoxin that possesses Rho GTPase activating protein and ADP-ribosyltransferase activities, no activity with Rab4 protein, overview
-
?
additional information
?
-
the enzyme also targets deoxyguanosine
-
?
additional information
?
-
-
the enzyme also targets deoxyguanosine
-
?
additional information
?
-
the enzyme also targets deoxyguanosine
-
?
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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
integrin alpha7 + NAD+
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
-
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
-
-
?
NAD+ + (ADP-D-ribosyl)n-aryl hydrocarbon receptor
nicotinamide + (ADP-D-ribosyl)n+1-aryl hydrocarbon receptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-NEMO protein
nicotinamide + (ADP-D-ribosyl)n+1-NEMO protein + H+
the enzyme prevents poly-ubiquitination of NEMO protein
-
-
?
NAD+ + (ADP-D-ribosyl)n-p21ras
nicotinamide + (ADP-D-ribosyl)n+1-p21ras
-
ADP-ribosylation of p21ras does not alter interactions with guanidine nucleotides. Possible function of the enzyme in pathogenesis
-
-
?
NAD+ + (ADP-D-ribosyl)n-P2X7 ion channel
nicotinamide + (ADP-D-ribosyl)n+1-P2X7 ion channel + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-rab4
nicotinamide + (ADP-D-ribosyl)n+1-rab4
-
ADP-ribosylation affects Rab4 function in membrane recycling
-
-
?
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5
-
ADP-ribosylation of Rab5 by ExoS affects endocytosis. Interaction of Rab5 with endosome antigen 1 is markedly diminished after Rab5 ADP-ribosylation by ExoS
-
-
?
NAD+ + (ADP-D-ribosyl)n-RalA
nicotinamide + (ADP-D-ribosyl)n+1-RalA
-
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
-
-
?
NAD+ + (ADP-D-ribosyl)n-Ras
nicotinamide + (ADP-D-ribosyl)n+1-Ras
-
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
-
-
?
NAD+ + histone H2A
nicotinamide + (ADP-D-ribosyl)-histone H2A
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
-
-
?
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
-
-
?
NAD+ + moesin
nicotinamide + (ADP-D-ribosyl)-moesin
-
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
-
-
?
NAD+ + Ras
nicotinamide + (ADP-D-ribosyl)-Ras
-
interaction requires residue Leu428
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
the enzyme is a DNA repair enzyme
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ADPRT domain of ExoT is active in vivo and contributes to the pathogenesis of Pseudomonas aeruginosa infections
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
intracellular Ras is modified by bacterially translocated ExoS, inhibition of target cell proliferation correlates with the efficiency of Ras modification
-
-
?
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+
-
-
-
?
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+
-
-
-
-
?
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 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
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Saccharolobus solfataricus MT-4 / DSM 5833
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
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
-
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
-
-
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
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
-
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
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
-
-
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Rab5 mediates entry of the EGFR into early endosomes
-
-
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Rab5 mediates entry of the EGFR into early endosomes
-
-
?
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
-
-
-
-
?
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
-
-
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
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
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
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
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme modifies eukaryotic 21000-24000 Da GTP-binding proteins
-
-
?
additional information
?
-
-
transcriptional regulation mechanism, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme is involved in pathogenesis of Parkinson's disease, analysis of polymorphisms, overview
-
-
?
additional information
?
-
-
the enzyme has the ability to ADP-ribosylate itself
-
-
?
additional information
?
-
-
raft association focuses ART2.2 on specific targets that constitutively or inducibly assoiate with lipid rafts
-
-
?
additional information
?
-
-
PARP-1 is involved in modulation of NO-derived injury and response to genotoxic damage
-
-
?
additional information
?
-
-
PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme is involved in endothelial cell dysfunction
-
-
?
additional information
?
-
-
transcriptional regulation mechanism, overview
-
-
?
additional information
?
-
-
the enzyme itself is a target for P2X7-triggered ectodomain shedding at F239/S240
-
-
?
additional information
?
-
-
the enzyme is involved in endothelial cell dysfunction
-
-
?
additional information
?
-
-
PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
-
-
?
additional information
?
-
-
exoenzyme S and 14-3-3 interact in a direct fashion, interaction involves the conserved amphiphatic groove of 14-3-3
-
-
?
additional information
?
-
-
exoenzyme S is an important adhesin
-
-
?
additional information
?
-
-
ExoS is a virulence factor of the pathogen
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
Bmh1p, a yeast homologue of the human FAS, acts as an ExoS cofactor, overview
-
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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-[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-(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
-
novobiocin
-
IC50: 2.2 mM, 5 mM, 90% inhibition in presence of Mg2+, 59% inhibition in absence of Mg2+
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
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
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
-
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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
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.017
(ADP-D-ribosyl)n-RhoA protein
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
0.012
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
additional information
additional information
-
kinetics for NAD+ utilization are not Michaelis-Menten type
-
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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
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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
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
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.0249
4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
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
0.000925
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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
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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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
80
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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