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Information on EC 2.4.2.30 - NAD+ ADP-ribosyltransferase and Organism(s) Bos taurus
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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
- agonist
- bcl-2
- camp
- cyclase
- g-proteins
-
adp-ribosylation
- phospholipase
- ovarian
- necrosis
- endothelial
-
toxin-sensitive
- leukemia
- adenylate
- cholera
- cyclin
-
gtp-binding
- inositol
- bordetella
- guanine
-
annexin
- gtp
- erk
-
pro-apoptotic
-
anti-apoptotic
- mapks
- chromatin
-
apoptosis-inducing
- phosphoinositide
-
muscarinic
-
tunel
-
phorbol
-
adenylyl
- forskolin
-
receptor-mediated
-
protein-coupled
- pkc
-
heterotrimeric
-
caspase-dependent
-
acellular
-
forskolin-stimulated
- survivin
- aif
-
sub-g1
- xiap
- rad51
- carbachol
-
brca1/2
- molecular biology
- drug development
- pharmacology
- toxoid
- analysis
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-protein
-
-
-
-
193-kDa vault protein
-
-
-
-
adenosine diphosphate ribosyltransferase
-
-
-
-
ADP-ribosyltransferase
-
-
-
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ADP-ribosyltransferase (polymerizing)
-
-
-
-
ADPRT
-
-
-
-
C3 exoenzyme
-
-
-
-
exoenzyme C3
-
-
-
-
exoenzyme S
-
-
-
-
msPARP
-
-
-
-
NAD(+) ADP-ribosyltransferase
-
-
-
-
NAD+:ADP-ribosyltransferase (polymerizing)
-
-
-
-
NAD-protein ADP-ribosyltransferase
-
-
-
-
pADPRT
-
-
-
-
PARP
-
-
-
-
PARP-related/IalphaI-related H5/proline-rich
-
-
-
-
PH5P
-
-
-
-
poly(ADP-ribose) polymerase
-
-
-
-
poly(ADP-ribose) synthase
-
-
-
-
poly(ADP-ribose) transferase
-
-
-
-
poly(ADP-ribosyl)transferase
-
-
-
-
poly[ADP-ribose] synthetase
-
-
-
-
TANK1
-
-
-
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TANK2
-
-
-
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Tankyrase-like protein
-
-
-
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Tankyrase-related protein
-
-
-
-
TRF1-interacting ankyrin-related ADP-ribose polymerase
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-
-
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VPARP
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
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
58319-92-9
-
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
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
-
-
?
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
-
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
-
-
?
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
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
the enzyme is a DNA repair enzyme
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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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+
carsalam
-
5 mM, 88% inhibition in presence of Mg2+, 68% inhibition in absence of Mg2+
Isoquinoline
-
5 mM, 47% inhibition in presence of Mg2+, 34% inhibition in absence of Mg2+
novobiocin
-
IC50: 2.2 mM, 5 mM, 90% inhibition in presence of Mg2+, 59% inhibition in absence of Mg2+
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+
xanthurenic acid
-
5 mM, 88% inhibition in presence of Mg2+, 65% inhibition in absence of Mg2+
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
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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+
DNA
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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
harmaline hydrochloride
-
activates more strongly in absence of Mg2+ than in presence of Mg2+
Phthalic acid
-
activates more strongly in absence of Mg2+ than in presence of Mg2+
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
2.2
novobiocin
Bos taurus
-
IC50: 2.2 mM, 5 mM, 90% inhibition in presence of Mg2+, 59% inhibition in absence of Mg2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PARP1_BOVIN
1016
0
113486
Swiss-Prot
other Location (Reliability: 2)
F1MU08_BOVIN
1016
0
113368
TrEMBL
other Location (Reliability: 1)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Banasik, M.; Komura, H.; Shimoyama, M.; Ueda, K.
Specific inhibitors of poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferase
J. Biol. Chem.
267
1569-1575
1992
Bos taurus
De Murcia, G.; Huletsky, A.; Poirier, G.G.
Modulation of chromatin structure by poly(ADP-ribosyl)ation
Biochem. Cell Biol.
66
626-635
1988
Bos taurus
Rankin, P.W.; Jacobson, E.L.; benjamin, R.C.; Moss, J.; Jacobson, M.K.
Quantitative studies of inhibitors of ADP-ribosylation in vitro and in vivo
J. Biol. Chem.
264
4312-4317
1989
Bos taurus
EXTERNAL LINKS (specific for EC-Number 2.4.2.30)
Transporter Classification Database (TCDB): 1.I.1.1.3
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