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EC Tree
IUBMB Comments The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20--30 units.
The taxonomic range for the selected organisms is: Saccharolobus solfataricus The enzyme appears in selected viruses and cellular organisms
Synonyms
parp, pertussis toxin, parp-1, poly(adp-ribose) polymerase, parp1, poly (adp-ribose) polymerase, poly(adp-ribose) polymerase-1, c3 exoenzyme, adprt, exoenzyme s,
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(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-protein
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193-kDa vault protein
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adenosine diphosphate ribosyltransferase
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ADP-ribosylating thermozyme
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ADP-ribosyltransferase
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ADP-ribosyltransferase (polymerizing)
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NAD(+) ADP-ribosyltransferase
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NAD+:ADP-ribosyltransferase (polymerizing)
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NAD-protein ADP-ribosyltransferase
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PARP-related/IalphaI-related H5/proline-rich
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poly(ADP-ribose) polymerase
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poly(ADP-ribose) polymerase-like enzyme
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poly(ADP-ribose) synthase
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poly(ADP-ribose) transferase
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poly(ADP-ribosyl)transferase
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poly[ADP-ribose] synthetase
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Tankyrase-like protein
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Tankyrase-related protein
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TRF1-interacting ankyrin-related ADP-ribose polymerase
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pentosyl group transfer
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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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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
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
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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
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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
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Mg2+
0.1 mM, 4.1fold activation
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3-aminobenzamide
10 mM, 47% inhibition
nicotinamide
10 mM, 14% inhibition
Zn2+
0.5 mM, 50% inhibition
3-aminobenzamide
10 mM, 47% inhibition
nicotinamide
10 mM, 14% inhibition
Zn2+
0.5 mM, 47% inhibition
additional information
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phenanthroline has no or a slightly activating effect
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additional information
phenanthroline has no or a slightly activating effect
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DNA
slightly increases activity
oligodeoxyribonucleotides
slightly enhance enzyme activity with the maximal increase of 50% as compared to the control
Mg2+
5 mM, 6.3fold activation
Phenanthroline
0.1 mM, 1.1fold activation
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7 - 9.5
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pH 7.0: about 75% of maximal activity, pH 9.5: about 70% of maximal activity
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80
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7 - 7.2
isoelectric focusing
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SwissProt
brenda
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PARP_SACSO
231
0
24334
Swiss-Prot
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50000
1 * 50000, SDS-PAGE
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monomer
1 * 50000, SDS-PAGE
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x * 54000-55000, SDS-PAGE
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Faraone-Mennella, M.R.; Gambacorta, A.; Nicolaus, B.; Farina, B.
Purification and biochemical characterization of a poly(ADP-ribose) polymerase-like enzyme from the thermophilic archaeon Sulfolobus solfataricus.
Biochem. J.
335
441-447
1998
Saccharolobus solfataricus
brenda
Faraone Mennella, M.R.; Castellano, S.; De Luca, P.; Discenza, A.; Gambacorta, A.; Nicolaus, B.; Farina, B.
Comparison of the ADP-ribosylating thermozyme from Sulfolobus solfataricus and the mesophilic poly(ADP-ribose) polymerases
FEMS Microbiol. Lett.
192
9-14
2000
Saccharolobus solfataricus, Saccharolobus solfataricus (B3EWG9), Saccharolobus solfataricus MT-4 / DSM 5833
brenda
Faraone-Mennella, M.R.; Piccialli, G.; De Luca, P.; Castellano, S.; Giordano, A.; Rigano, D.; De Napoli, L.; Farina, B.
Interaction of the ADP-ribosylating enzyme from the hyperthermophilic archaeon Sulfolobus solfataricus with DNA and ss-oligo deoxy ribonucleotides
J. Cell. Biochem.
85
146-157
2002
Saccharolobus solfataricus (B3EWG9), Saccharolobus solfataricus MT-4 / DSM 5833 (B3EWG9)
brenda
Transporter Classification Database (TCDB):
1.I.1.1.3