2.4.2.30: NAD+ ADP-ribosyltransferase This is an abbreviated version! For detailed information about NAD+ ADP-ribosyltransferase, go to the full flat file .
Reaction
NAD+ +
(ADP-D-ribosyl)n-acceptor =
nicotinamide +
(ADP-D-ribosyl)n+1-acceptor +
H+
Synonyms (adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-protein, 193-kDa vault protein , 2,3,7,8-tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase, adenosine diphosphate ribosyltransferase, ADP-ribosylating thermozyme, ADP-ribosyltransferase, ADP-ribosyltransferase (polymerizing), ADP-ribosyltransferase 3, ADP-ribosyltransferase C3cer, ADP-ribosyltransferase-1, ADPr, ADPRT, ADPRT , ART, ART1, ARTC2.2, ARTD10, ARTD10/PARP10, ARTD11, ARTD14, ARTD3, ARTD7/PARP15, ARTD8, asparagine-specific ADP-ribosyltransferase, B aggressive lymphoma protein 2, C3 exoenzyme, C3-like toxin, C3larvin toxin, C3lim, CRM66, diphtheria toxin-like ADP-ribosyltranferase, ecto-ADP-ribosyltransferase, ecto-ADP-ribosyltransferase 2.2, ecto-ADP-ribosyltransferase ART2.2, EspJ, Exo53, exoenzyme C3, exoenzyme S, exoenzyme T, ExoS, ExoT, exotoxin-S, mART, ModA, ModB, mono ADP-ribosyltransferase, mono(ADP-ribosyl) transferase, mono-ADP-ribosyl transferase C3, mono-ADP-ribosyltransferase, More, msPARP , NAD(+) ADP-ribosyltransferase , NAD+:ADP-ribosyltransferase (polymerizing), NAD-dependent ADP-ribosyltransferase, NAD-protein ADP-ribosyltransferase, NarE, pADPRT, PAR polymerase, PARP, PARP , PARP-1, PARP-7, PARP-related/IalphaI-related H5/proline-rich , PARP1, PARP10, PARP11, PARP14, PARP3, PARPss, pertussis toxin, PH5P , poly (ADP-ribose) polymerase, poly (ADP-ribose) polymerase-1, poly(ADP-ribose) polymerase, poly(ADP-ribose) polymerase family member 11, poly(ADP-ribose) polymerase-1, poly(ADP-ribose) polymerase-11, poly(ADP-ribose) polymerase-like enzyme, poly(ADP-ribose) synthase, poly(ADP-ribose) transferase, poly(ADP-ribosyl)transferase, poly[ADP-ribose] synthetase , PTx, PtxS1, scabin, TANK1, TANK1 , TANK2 , tankyrase I, Tankyrase-like protein , Tankyrase-related protein , TbSIR2RP1, TiPARP, TNKS-1, TRF1-interacting ankyrin-related ADP-ribose polymerase, TRF1-interacting ankyrin-related ADP-ribose polymerase , TTS-ExoS, type III-secreted toxin, VahC, VPARP , vsdc, YART
ECTree
Activating Compound
Activating Compound on EC 2.4.2.30 - NAD+ ADP-ribosyltransferase
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3-amino-1-methyl-5H-pyrido[4,3-b]indole
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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
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activates in presence of Mg2+, inhibits in absence of Mg2+
ATP
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5-10 mM, 20-30% stimulation
Bmh1p
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a yeast homologue of the human FAS, acts as an activating ExoS cofactor, overview
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FAS
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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
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GDP
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increases activity in absence of Mg2+
GTP
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increases activity in absence of Mg2+
GTP(gammaS)
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increases activity in absence of Mg2+
harmaline hydrochloride
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activates more strongly in absence of Mg2+ than in presence of Mg2+
Mg2+
5 mM, 6.3fold activation
oligodeoxyribonucleotides
slightly enhance enzyme activity with the maximal increase of 50% as compared to the control
Phenanthroline
0.1 mM, 1.1fold activation
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
DNA
Cryptothecodinium cohnii
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required
DNA
-
absolute requirement
DNA
-
absolute requirement
DNA
-
enzyme has an N-terminal binding domain
DNA
slightly increases activity
protein 14-3-3
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dependent on
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protein 14-3-3
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required, interaction analysis, interaction equires residues L426, D427, and L428, overview, binding study of mutant enzymes, overview
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additional information
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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
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additional information
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DNA binding by PARP-1 triggers its activity and it adds poly(ADP-ribose) polymers to itself and to surrounding histones, overview
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additional information
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PARP-1 is activated in response to DNA damage and participates in DNA repair, genomic integrity and cell death
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additional information
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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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