2.4.2.30 integrin alpha7 + NAD+ 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 Mus musculus (ADP-D-ribosyl)-integrin alpha7 + nicotinamide - ? 386509 2.4.2.30 integrin alpha7 + NAD+ 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 Mus musculus (ADP-D-ribosyl)-integrin alpha7 + nicotinamide - ? 386509 2.4.2.30 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 Homo sapiens ? - ? 89 2.4.2.30 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 Bos taurus ? - ? 89 2.4.2.30 additional information the enzyme modifies eukaryotic 21000-24000 Da GTP-binding proteins Clostridium botulinum ? - ? 89 2.4.2.30 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 Homo sapiens ? - ? 89 2.4.2.30 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 Homo sapiens ? - ? 89 2.4.2.30 additional information raft association focuses ART2.2 on specific targets that constitutively or inducibly assoiate with lipid rafts Mus musculus ? - ? 89 2.4.2.30 additional information ART1 is an arginine-specific transferase Mus musculus ? - ? 89 2.4.2.30 additional information narE possesses ADP-ribosylating and NAD-glycohydrolase activities Neisseria meningitidis ? - ? 89 2.4.2.30 additional information exoenzyme S and 14-3-3 interact in a direct fashion, interaction involves the conserved amphiphatic groove of 14-3-3 Pseudomonas aeruginosa ? - ? 89 2.4.2.30 additional information exoenzyme S is an important adhesin Pseudomonas aeruginosa ? - ? 89 2.4.2.30 additional information ExoS is a virulence factor of the pathogen Pseudomonas aeruginosa ? - ? 89 2.4.2.30 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 Homo sapiens ? - ? 89 2.4.2.30 additional information PARP-1 is involved in modulation of NO-derived injury and response to genotoxic damage Mus musculus ? - ? 89 2.4.2.30 additional information PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview Mus musculus ? - ? 89 2.4.2.30 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 Mus musculus ? - ? 89 2.4.2.30 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 Mus musculus ? - ? 89 2.4.2.30 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 Pseudomonas aeruginosa ? - ? 89 2.4.2.30 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 Mus musculus ? - ? 89 2.4.2.30 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 Pseudomonas aeruginosa ? - ? 89 2.4.2.30 additional information the enzyme is involved in endothelial cell dysfunction Mus musculus ? - ? 89 2.4.2.30 additional information the enzyme is involved in pathogenesis of Parkinson's disease, analysis of polymorphisms, overview Homo sapiens ? - ? 89 2.4.2.30 additional information transcriptional regulation mechanism, overview Drosophila melanogaster ? - ? 89 2.4.2.30 additional information transcriptional regulation mechanism, overview Mus musculus ? - ? 89 2.4.2.30 additional information exoenzyme S is a bifunctional type III secretion, TTS, effector protein, with GTPase-activating and ADP-ribosyltransferase activities Pseudomonas aeruginosa ? - ? 89 2.4.2.30 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 Pseudomonas aeruginosa ? - ? 89 2.4.2.30 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 Pseudomonas aeruginosa ? - ? 89 2.4.2.30 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 Mus musculus ? - ? 89 2.4.2.30 additional information the enzyme also shows NAD+-hydrolase activity Hathewaya limosa ? - ? 89 2.4.2.30 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 Homo sapiens ? - ? 89 2.4.2.30 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 Pseudomonas aeruginosa ? - ? 89 2.4.2.30 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 Pseudomonas aeruginosa ? - ? 89 2.4.2.30 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 Pseudomonas aeruginosa ? - ? 89 2.4.2.30 additional information the enzyme has the ability to ADP-ribosylate itself Homo sapiens ? - ? 89 2.4.2.30 additional information the enzyme itself is a target for P2X7-triggered ectodomain shedding at F239/S240 Mus musculus ? - ? 89 2.4.2.30 additional information the enzyme also targets deoxyguanosine Streptomyces scabiei ? - ? 89 2.4.2.30 additional information exoenzyme S is a bifunctional type III secretion, TTS, effector protein, with GTPase-activating and ADP-ribosyltransferase activities Pseudomonas aeruginosa 388 ? - ? 89 2.4.2.30 additional information the enzyme is involved in endothelial cell dysfunction Mus musculus 129/Sv x C57BL/6 ? - ? 89 2.4.2.30 additional information PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview Mus musculus Sv129 ? - ? 89 2.4.2.30 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 Pseudomonas aeruginosa PA103 ? - ? 89 2.4.2.30 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 Pseudomonas aeruginosa PA103 ? - ? 89 2.4.2.30 additional information the enzyme also targets deoxyguanosine Streptomyces scabiei 87.22 ? - ? 89 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-(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 Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-(EF-2) - ? 380102 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Mus musculus nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Bos taurus nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Mesocricetus auratus nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Saccharolobus solfataricus nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Hathewaya limosa nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of topoisomerase I Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor auto-poly(ADP-ribosyl)ation Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of high mobility group proteins Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of DNA ligase Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of endonuclease Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of topoisomerase II Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of terminal deoxynucleotidyltransferase Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of 21000-24000 Da platelet membrane proteins Clostridium botulinum nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of histone H1 Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of histone H1 Bos taurus nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of histone H1 Dictyostelium discoideum nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of histone Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of histone Helix pomatia nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of histone Cryptothecodinium cohnii nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor catalyzes poly(ADP-ribosyl)ation of the synthetase itself, automodification Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor poly(ADP-ribosyl)ation of ADP-ribosyltransferase Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor ADPRT domain of ExoT is active in vivo and contributes to the pathogenesis of Pseudomonas aeruginosa infections Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor intracellular Ras is modified by bacterially translocated ExoS, inhibition of target cell proliferation correlates with the efficiency of Ras modification Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor ExoT ADP-ribosylates a restricted subset of host proteins including the Crk proteins Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Drosophila melanogaster nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Mus musculus nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor the enzyme is a DNA repair enzyme Bos taurus nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Drosophila melanogaster nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Mus musculus nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor agmatine as ADPribose acceptor is used Neisseria meningitidis nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Pseudomonas aeruginosa ExoS nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor ExoT ADP-ribosylates a restricted subset of host proteins including the Crk proteins Pseudomonas aeruginosa ExoS nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Pseudomonas aeruginosa ExoT nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor ExoT ADP-ribosylates a restricted subset of host proteins including the Crk proteins Pseudomonas aeruginosa ExoT nicotinamide + (ADP-D-ribosyl)n+1-acceptor - ? 354825 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ - ? 398959 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ - ? 398959 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Saccharolobus solfataricus nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ - ? 398959 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Neisseria meningitidis nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ - ? 398959 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Paenibacillus larvae subsp. larvae nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ - ? 398959 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Staphylococcus aureus nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ - ? 398959 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Bacillus cereus nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ - ? 398959 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor 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 Saccharolobus solfataricus nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ - ? 398959 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA Streptomyces scabiei nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ - ? 398959 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Paenibacillus larvae subsp. larvae DSM 25719 nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ - ? 398959 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Saccharolobus solfataricus MT-4 / DSM 5833 nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ - ? 398959 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor 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 Saccharolobus solfataricus MT-4 / DSM 5833 nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ - ? 398959 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor - Pseudomonas aeruginosa PA103 nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ - ? 398959 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-acceptor the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA Streptomyces scabiei 87.22 nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ - ? 398959 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Aeromonas hydrophila nicotinamide + (ADP-D-ribosyl)n+1-actin - ? 423886 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-apolipoprotein - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-apolipoprotein - ? 380103 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-aryl hydrocarbon receptor - Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-aryl hydrocarbon receptor + H+ - ? 434696 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-beta-transducin repeat-containing protein - Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-beta-transducin repeat-containing protein + H+ - ? 457221 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-biotin - Bacillus cereus nicotinamide + (ADP-D-ribosyl)n+1-biotin + H+ - ? 435656 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-biotin - Bacillus cereus G9241 nicotinamide + (ADP-D-ribosyl)n+1-biotin + H+ - ? 435656 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-Crk-I - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-Crk-I - ? 380105 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-Crk-II - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-Crk-II - ? 380104 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-His6HRas the enzyme preferentially ADP-ribosylates membrane-associated His6HRas relative to its cytosolic His6HRasDELTACAAX with a C-terminal deletion Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-His6HRas - ? 380106 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-immunoglobulin A - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-immunoglobulin A - ? 380107 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-immunoglobulin G preferentially IgG3 Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-immunoglobulin G - ? 380108 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-NEMO protein the enzyme prevents poly-ubiquitination of NEMO protein Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-NEMO protein + H+ - ? 434697 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-p21ras - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-p21ras - ? 378711 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-p21ras ADP-ribosylation of p21ras does not alter interactions with guanidine nucleotides. Possible function of the enzyme in pathogenesis Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-p21ras - ? 378711 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-P2X7 ion channel - Mus musculus nicotinamide + (ADP-D-ribosyl)n+1-P2X7 ion channel + H+ - ? 434698 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-peptide LL-37 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 Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-peptide LL-37 + H+ - ? 435657 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-Rab2 - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-Rab2 - ? 380109 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-Rab3 - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-Rab3 - ? 380110 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-rab4 - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-rab4 - ? 378712 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-rab4 ADP-ribosylation affects Rab4 function in membrane recycling Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-rab4 - ? 378712 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-Rab5 - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-Rab5 - ? 378713 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-Rab5 - ? 378713 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-Rab5 the enzyme ADP-ribosylates Rab5 at Gln79 Yersinia mollaretii nicotinamide + (ADP-D-ribosyl)n+1-Rab5 + H+ - ? 457224 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-RalA - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-RalA - ? 378714 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-RalA - ? 378714 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-Rap1A - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-Rap1A - ? 380111 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-Ras - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-Ras - ? 378715 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-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 Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-Ras - ? 378715 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-Ras protein - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-Ras protein - ? 380112 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-RhoA protein - Paenibacillus larvae subsp. larvae nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+ - ? 434699 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-RhoA protein - Paenibacillus larvae subsp. larvae BRL-230010 nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+ - ? 434699 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-serine/arginine-rich protein-specific kinase 2 - Homo sapiens nicotinamide + (ADP-D-ribosyl)n+1-serine/arginine-rich protein-specific kinase 2 + H+ - ? 435658 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-soybean trypsin inhibitor - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-soybean trypsin inhibitor - ? 380113 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-soybean-trypsin-inhibitor - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-soybean-trypsin-inhibitor - ? 380114 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Btk - Citrobacter rodentium nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Btk + H+ - ? 457225 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Csk - Citrobacter rodentium nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Csk + H+ - ? 457226 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Hck - Citrobacter rodentium nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Hck + H+ - ? 457227 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Lyn - Citrobacter rodentium nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Lyn + H+ - ? 457228 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Src - Citrobacter rodentium nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Src + H+ - ? 457229 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Syk - Citrobacter rodentium nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Syk + H+ - ? 457230 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Tec - Citrobacter rodentium nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Tec + H+ - ? 457231 2.4.2.30 NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Yes1 - Citrobacter rodentium nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Yes1 + H+ - ? 457232 2.4.2.30 NAD+ + 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 Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)-cyclophilin A - ? 386593 2.4.2.30 NAD+ + 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 Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)-cyclophilin A - ? 386593 2.4.2.30 NAD+ + 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 Pseudomonas aeruginosa 388 nicotinamide + (ADP-D-ribosyl)-cyclophilin A - ? 386593 2.4.2.30 NAD+ + 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 Pseudomonas aeruginosa 388 nicotinamide + (ADP-D-ribosyl)-cyclophilin A - ? 386593 2.4.2.30 NAD+ + Galphai - Bordetella pertussis nicotinamide + (ADP-D-ribosyl)-Galphai + H+ - ? 457222 2.4.2.30 NAD+ + Galphai - Bordetella pertussis Tohama I nicotinamide + (ADP-D-ribosyl)-Galphai + H+ - ? 457222 2.4.2.30 NAD+ + Galphai3C20 - Bordetella pertussis nicotinamide + N-(ADP-D-ribosyl)-Galphai3C20 - ? 458165 2.4.2.30 NAD+ + GTPase RhoA the exoenzyme modifies the low-molecular-mass GTPases RhoA, B, and C specifically at Asn41 Hathewaya limosa nicotinamide + (ADP-D-ribosyl)-GTPase RhoA - ? 389323 2.4.2.30 NAD+ + GTPase RhoB the exoenzyme modifies the low-molecular-mass GTPases RhoA, B, and C specifically at Asn41 Hathewaya limosa nicotinamide + (ADP-D-ribosyl)-GTPase RhoB - ? 389324 2.4.2.30 NAD+ + GTPase RhoC the exoenzyme modifies the low-molecular-mass GTPases RhoA, B, and C specifically at Asn41 Hathewaya limosa nicotinamide + (ADP-D-ribosyl)-GTPase RhoC - ? 389325 2.4.2.30 NAD+ + H2O - Rattus norvegicus nicotinamide + ADP-ribose - ? 377283 2.4.2.30 NAD+ + histone H1 - Homo sapiens nicotinamide + (ADP-D-ribosyl)-histone H1 - ? 377284 2.4.2.30 NAD+ + 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 Trypanosoma brucei nicotinamide + (ADP-D-ribosyl)-histone H2A - ? 375191 2.4.2.30 NAD+ + histone H2A the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B Trypanosoma brucei nicotinamide + (ADP-D-ribosyl)-histone H2A - ? 375191 2.4.2.30 NAD+ + histone H2B - Bos taurus nicotinamide + (ADP-D-ribosyl)-histone H2B - ? 375192 2.4.2.30 NAD+ + 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 Trypanosoma brucei nicotinamide + (ADP-D-ribosyl)-histone H2B - ? 375192 2.4.2.30 NAD+ + histone H2B the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B Trypanosoma brucei nicotinamide + (ADP-D-ribosyl)-histone H2B - ? 375192 2.4.2.30 NAD+ + lymphocyte function-associated antigen LFA-1 - Mus musculus nicotinamide + ? - ? 377285 2.4.2.30 NAD+ + 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 Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)-moesin - ? 386594 2.4.2.30 NAD+ + moesin modification of Arg553, Arg560 and Arg563, activity with wild-type and mutant moesins, overview Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)-moesin - ? 386594 2.4.2.30 NAD+ + p53 - Mus musculus nicotinamide + (ADP-D-ribosyl)-p53 - ? 386595 2.4.2.30 NAD+ + p53 PARP-1 interacts with and poly(ADP-ribosyl)ates p53, which participates in DNA recombination Mus musculus nicotinamide + (ADP-D-ribosyl)-p53 - ? 386595 2.4.2.30 NAD+ + 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 Gallus gallus nicotinamide + (ADP-ribosyl)-poly(ADP-ribose) polymerase-1 - ? 377287 2.4.2.30 NAD+ + Rab31 the enzyme ADP-ribosylates Rab31 at Gln64 Yersinia mollaretii nicotinamide + (ADP-D-ribosyl)-Rab31 + H+ - ? 457223 2.4.2.30 NAD+ + Rab5 protein Rab5 mediates entry of the EGFR into early endosomes Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+ - ? 398962 2.4.2.30 NAD+ + Rab5 protein Rab5 mediates entry of the EGFR into early endosomes Pseudomonas aeruginosa PA103 nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+ - ? 398962 2.4.2.30 NAD+ + Rab9 protein - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+ - ? 398963 2.4.2.30 NAD+ + Rab9 protein - Pseudomonas aeruginosa PA103 nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+ - ? 398963 2.4.2.30 NAD+ + Ras interaction requires residue Leu428 Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)-Ras - ? 386597 2.4.2.30 NAD+ + Ras GTPase - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)-Ras GTPase - ? 386596 2.4.2.30 NAD+ + Ras2p Ras2p is a yeast protein, activity absolutely requires the yeast protein Bmh1p Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)-Ras2p + H+ - ? 401512 2.4.2.30 NAD+ + RhoA - Bacillus cereus nicotinamide (ADP-D-ribosyl)-RhoA - ? 377289 2.4.2.30 NAD+ + RhoA - Bacillus cereus 2339 nicotinamide (ADP-D-ribosyl)-RhoA - ? 377289 2.4.2.30 NAD+ + RhoB - Bacillus cereus nicotinamide (ADP-D-ribosyl)-RhoB - ? 377290 2.4.2.30 NAD+ + RhoB - Bacillus cereus 2339 nicotinamide (ADP-D-ribosyl)-RhoB - ? 377290 2.4.2.30 NAD+ + RhoC weak activity Bacillus cereus nicotinamide (ADP-D-ribosyl)-RhoC - ? 377291 2.4.2.30 NAD+ + RhoC weak activity Bacillus cereus 2339 nicotinamide (ADP-D-ribosyl)-RhoC - ? 377291 2.4.2.30 NAD+ + RNA polymerase - Tequatrovirus T4 nicotinamide + (ADP-D-ribosyl)-RNA polymerase - ? 375193 2.4.2.30 NAD+ + 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 Tequatrovirus T4 nicotinamide + (ADP-D-ribosyl)-RNA polymerase - ? 375193 2.4.2.30 NAD+ + RNA polymerase - Tequatrovirus T4 ModA nicotinamide + (ADP-D-ribosyl)-RNA polymerase - ? 375193 2.4.2.30 NAD+ + 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 Tequatrovirus T4 ModA nicotinamide + (ADP-D-ribosyl)-RNA polymerase - ? 375193 2.4.2.30 NAD+ + RNA polymerase - Tequatrovirus T4 ModB nicotinamide + (ADP-D-ribosyl)-RNA polymerase - ? 375193 2.4.2.30 NAD+ + 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 Tequatrovirus T4 ModB nicotinamide + (ADP-D-ribosyl)-RNA polymerase - ? 375193 2.4.2.30 NAD+ + soybean trypsin inhibitor the exoenzyme modifies the substrate at an arginine residue Hathewaya limosa nicotinamide + (ADP-D-ribosyl)-soybean trypsin inhibitor - ? 389326 2.4.2.30 NAD+ + topoisomerase I - Mus musculus nicotinamide + (ADP-D-ribosyl)-topoisomerase I - ? 386598 2.4.2.30 NAD+ + 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 Mus musculus nicotinamide + (ADP-D-ribosyl)-topoisomerase I - ? 386598 2.4.2.30 NAD+ + vimentin - Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)-vimentin - ? 386599 2.4.2.30 NAD+ + wild-type exoenzyme C3 activity of the recombinant mutant Q217E exoenzyme C3, modification at Arg86 Hathewaya limosa nicotinamide + (ADP-D-ribosyl)-wild-type exoenzyme C3 - ? 389327 2.4.2.30 nicotinamide 1,N6-ethenoadenine dinucleotide + (ADP-D-ribosyl)n-vH-Ras protein - Pseudomonas aeruginosa nicotinamide + ? - ? 435655 2.4.2.30 nicotinamide 1,N6-ethenoadenine dinucleotide + (ADP-D-ribosyl)n-vH-Ras protein - Pseudomonas aeruginosa PAK nicotinamide + ? - ? 435655