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Information on EC 2.4.2.30 - NAD+ ADP-ribosyltransferase and Organism(s) Saccharolobus solfataricus and UniProt Accession B3EWG9

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.30 NAD+ ADP-ribosyltransferase
IUBMB Comments
The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20--30 units.
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This record set is specific for:
Saccharolobus solfataricus
UNIPROT: B3EWG9
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Word Map
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(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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ADPRT
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C3 exoenzyme
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exoenzyme C3
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exoenzyme S
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msPARP
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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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pADPRT
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PARP
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PARP-related/IalphaI-related H5/proline-rich
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PH5P
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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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TANK1
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TANK2
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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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VPARP
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
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-
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PATHWAY SOURCE
PATHWAYS
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.
CAS REGISTRY NUMBER
COMMENTARY hide
58319-92-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
show the reaction diagram
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
show the reaction diagram
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
show the reaction diagram
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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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
0.1 mM, 4.1fold activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.5
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pH 7.0: about 75% of maximal activity, pH 9.5: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.2
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PARP_SACSO
231
0
24334
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
1 * 50000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 50000, SDS-PAGE
?
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x * 54000-55000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
-
half-life: 204 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team