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Information on EC 2.4.2.30 - NAD+ ADP-ribosyltransferase

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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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UNIPROT: W2E3J5
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Word Map
The enzyme appears in 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
mono-ADP-ribosyl transferase C3
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(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-protein
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-
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193-kDa vault protein
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adenosine diphosphate ribosyltransferase
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-
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ADP-ribosyltransferase
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ADP-ribosyltransferase (polymerizing)
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-
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ADPRT
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C3 exoenzyme
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-
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exoenzyme C3
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-
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exoenzyme S
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-
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msPARP
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NAD(+) ADP-ribosyltransferase
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-
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NAD+:ADP-ribosyltransferase (polymerizing)
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NAD-protein ADP-ribosyltransferase
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-
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pADPRT
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-
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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) 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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-
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Tankyrase-related protein
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-
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TRF1-interacting ankyrin-related ADP-ribose polymerase
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-
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VPARP
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-
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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-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
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
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-[[1-(1H-pyrazolo[3,4-d]pyrimidin-4-yl)piperidin-3-yl]methyl]methanesulfonamide
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
(ADP-D-ribosyl)n-RhoA protein
at pH 7.4 and 37°C
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0.034
NAD+
at pH 7.4 and 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011
N-[[1-(1H-pyrazolo[3,4-d]pyrimidin-4-yl)piperidin-3-yl]methyl]methanesulfonamide
at pH 7.4 and 37°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.6
calculated from amino acid sequence
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?
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
x * 22000, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 22000, calculated from amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 28% (w/v) PEG 4000, 200 mM sodium acetate, and 100 mM Tris, pH 8.5
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap chelating Sepharose column chromatography, and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Krska, D.; Ravulapalli, R.; Fieldhouse, R.J.; Lugo, M.R.; Merrill, A.R.
C3larvin toxin, an ADP-ribosyltransferase from Paenibacillus larvae
J. Biol. Chem.
290
1639-1653
2015
Paenibacillus larvae subsp. larvae (W2E3J5), Paenibacillus larvae subsp. larvae BRL-230010 (W2E3J5)
Manually annotated by BRENDA team
Lugo, M.R.; Merrill, A.R.
An in-silico sequence-structure-function analysis of the N-terminal lobe in CT group bacterial ADP-ribosyltransferase toxins
Toxins
11
365
2019
Bacillus cereus (Q8KNY0), Staphylococcus aureus (Q9ADS9), Paenibacillus larvae subsp. larvae (W2E3J5), Paenibacillus larvae subsp. larvae DSM 25719 (W2E3J5)
Manually annotated by BRENDA team