Information on EC 2.4.2.30 - NAD+ ADP-ribosyltransferase and Organism(s) Homo sapiens

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The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.2.30
-
RECOMMENDED NAME
GeneOntology No.
NAD+ ADP-ribosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
show the reaction diagram
the pART catalytic domain is found associated in Lego-like fashion with a variety of domains, including nucleic acid-binding, protein-protein interaction, and ubiquitylation domains; the pART catalytic domain is found associated in Lego-like fashion with a variety of domains, including nucleic acid-binding, protein-protein interaction, and ubiquitylation domains; the pART catalytic domain is found associated in Lego-like fashion with a variety of domains, including nucleic acid-binding, protein-protein interaction, and ubiquitylation domains; the pART catalytic domain is found associated in Lego-like fashion with a variety of domains, including nucleic acid-binding, protein-protein interaction, and ubiquitylation domains; the pART catalytic domain is found associated in Lego-like fashion with a variety of domains, including nucleic acid-binding, protein-protein interaction, and ubiquitylation domains; the pART catalytic domain is found associated in Lego-like fashion with a variety of domains, including nucleic acid-binding, protein-protein interaction, and ubiquitylation domains; the pART catalytic domain is found associated in Lego-like fashion with a variety of domains, including nucleic acid-binding, protein-protein interaction, and ubiquitylation domains; the pART catalytic domain is found associated in Lego-like fashion with a variety of domains, including nucleic acid-binding, protein-protein interaction, and ubiquitylation domains; the pART catalytic domain is found associated in Lego-like fashion with a variety of domains, including nucleic acid-binding, protein-protein interaction, and ubiquitylation domains
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
NAD metabolism
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-
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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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the enzyme inhibits the activation of NF-kappaB and downstream target genes in response to interleukin-1beta and tumour necrosis factor-alpha, dependent on catalytic activity and poly-ubiquitin binding
physiological function
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
show the reaction diagram
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
show the reaction diagram
NAD+ + (ADP-D-ribosyl)n-aryl hydrocarbon receptor
nicotinamide + (ADP-D-ribosyl)n+1-aryl hydrocarbon receptor + H+
show the reaction diagram
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-NEMO protein
nicotinamide + (ADP-D-ribosyl)n+1-NEMO protein + H+
show the reaction diagram
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the enzyme prevents poly-ubiquitination of NEMO protein
-
-
?
NAD+ + (ADP-D-ribosyl)n-peptide LL-37
nicotinamide + (ADP-D-ribosyl)n+1-peptide LL-37 + H+
show the reaction diagram
-
up to four of the five arginine residues present in peptide LL-37 can be ADP-ribosylated on the same peptide when incubated at a high NAD concentration
-
-
?
NAD+ + (ADP-D-ribosyl)n-serine/arginine-rich protein-specific kinase 2
nicotinamide + (ADP-D-ribosyl)n+1-serine/arginine-rich protein-specific kinase 2 + H+
show the reaction diagram
-
-
-
?
NAD+ + histone H1
nicotinamide + (ADP-D-ribosyl)-histone H1
show the reaction diagram
-
-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
show the reaction diagram
O95271, P09874, Q2NL67, Q460N5, Q8N5Y8, Q9NR21, Q9UGN5, Q9UKK3, Q9Y6F1
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
show the reaction diagram
NAD+ + (ADP-D-ribosyl)n-aryl hydrocarbon receptor
nicotinamide + (ADP-D-ribosyl)n+1-aryl hydrocarbon receptor + H+
show the reaction diagram
Q7Z3E1
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-NEMO protein
nicotinamide + (ADP-D-ribosyl)n+1-NEMO protein + H+
show the reaction diagram
-
the enzyme prevents poly-ubiquitination of NEMO protein
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
enhances activity
Mg2+
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enhances both the automodification and poly(ADP-ribosyl)ation of histone H1
Sr2+
-
enhances activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanamide
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(beta,beta-dimethylacryl)shikonin
64% inhibition at 0.01 mM; 64% inhibition at 0.01 mM
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-(pyridin-2-yl)ethyl]propanamide
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3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-phenylethyl]propanamide
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3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-(pyridin-2-yl)ethyl]propanamide
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3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylethyl]propanamide
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3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylpropyl]propanamide
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3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[1-(4-sulfamoylphenyl)ethyl]propanamide
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3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[1-(pyridin-2-yl)ethyl]propanamide
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3-aminobenzamide
3-aminobenzoic acid
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1 mM, 12% inhibition
bergapten
69% inhibition at 0.01 mM; 69% inhibition at 0.01 mM
Cu2+
-
-
deoxyshikonin
67% inhibition at 0.01 mM; 67% inhibition at 0.01 mM
DMSO
at 2% (v/v) DMSO isoform ARTD10 loses more than half of its activity; at 2% (v/v) DMSO isoform ARTD7 loses its activity completely
EB-47
i.e. 5'-deoxy-5'-[4-[2-[(2,3-dihydro-1-oxo-1H-isoindol-4-yl)amino]-2-oxoethyl]-1-piperazinyl]-5'-oxoadenosine dihydrochloride; i.e. 5'-deoxy-5'-[4-[2-[(2,3-dihydro-1-oxo-1H-isoindol-4-yl)amino]-2-oxoethyl]-1-piperazinyl]-5'-oxoadenosine dihydrochloride
embelin
57% inhibition at 0.01 mM; 57% inhibition at 0.01 mM
gambogic acid
75% inhibition at 0.01 mM; 75% inhibition at 0.01 mM
gossypol
75% inhibition at 0.01 mM; 75% inhibition at 0.01 mM
Hg2+
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-
menadione
55% inhibition at 0.01 mM; 55% inhibition at 0.01 mM
methyl (2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanoate
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myricetin
78% inhibition at 0.01 mM; 78% inhibition at 0.01 mM
N-[(1R)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
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N-[(1S)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
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N-[(2S)-1-hydroxy-3-phenylpropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
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N-[(2S)-1-hydroxybutan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
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N-[(2S)-1-hydroxypropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
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N-[1-[4-(1H-imidazol-1-yl)phenyl]ethyl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
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nicotinamide
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1 mM, 93% inhibition
olaparib
i.e. 4-[(3-[(4-cyclopropylcarbonyl)piperazin-4-yl]carbonyl)-4-fluorophenyl]methyl(2H)phthalazin-1-one; i.e. 4-[(3-[(4-cyclopropylcarbonyl)piperazin-4-yl]carbonyl)-4-fluorophenyl]methyl(2H)phthalazin-1-one
PCMB
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complete
phenantridinone
i.e. 6(5H)-phenantridinone; i.e. 6(5H)-phenantridinone
Plumbagin
67% inhibition at 0.01 mM; 67% inhibition at 0.01 mM
TIQ-A
i.e. 4H-thieno[2,3-c]isoquinolin-5-one; i.e. 4H-thieno[2,3-c]isoquinolin-5-one
trimethylpsoralen
61% inhibition at 0.01 mM; 61% inhibition at 0.01 mM
Zn2+
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0038
(2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanamide
Homo sapiens;
Q9Y6F1
pH and temperature not specified in the publication
0.1
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-(pyridin-2-yl)ethyl]propanamide
Homo sapiens;
Q9Y6F1
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.0152
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-phenylethyl]propanamide
Homo sapiens;
Q9Y6F1
pH and temperature not specified in the publication
0.0013
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-(pyridin-2-yl)ethyl]propanamide
Homo sapiens;
Q9Y6F1
pH and temperature not specified in the publication
0.0009
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylethyl]propanamide
Homo sapiens;
Q9Y6F1
pH and temperature not specified in the publication
0.0022
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylpropyl]propanamide
Homo sapiens;
Q9Y6F1
pH and temperature not specified in the publication
0.0144
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[1-(4-sulfamoylphenyl)ethyl]propanamide
Homo sapiens;
Q9Y6F1
pH and temperature not specified in the publication
0.00118
EB-47
Homo sapiens;
Q460N3
isoform ARDT10, pH and temperature not specified in the publication
0.0022
methyl (2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanoate
Homo sapiens;
Q9Y6F1
pH and temperature not specified in the publication
0.1
N-[(1R)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens;
Q9Y6F1
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.1
N-[(1S)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens;
Q9Y6F1
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.001
N-[(2S)-1-hydroxy-3-phenylpropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens;
Q9Y6F1
pH and temperature not specified in the publication
0.0096
N-[(2S)-1-hydroxybutan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens;
Q9Y6F1
pH and temperature not specified in the publication
0.0111
N-[(2S)-1-hydroxypropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens;
Q9Y6F1
pH and temperature not specified in the publication
0.0132
N-[1-[4-(1H-imidazol-1-yl)phenyl]ethyl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens;
Q9Y6F1
pH and temperature not specified in the publication
0.000925 - 0.00204
olaparib
0.000745 - 0.00114
phenantridinone
0.000232
TIQ-A
Homo sapiens;
Q460N3
isoform ARDT7, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.325
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-
1.02
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
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reaction with histone in presence of DNA, 0.1 M glycine-NaOH buffer
8.7
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reaction with histone in presence of DNA, 0.1 M Tris-HCl buffer
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
x * 25000, SDS-PAGE; x * 25000, SDS-PAGE
116000
-
1 * 116000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 25000, SDS-PAGE; x * 25000, SDS-PAGE
monomer
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1 * 116000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitors, sitting drop vapor diffusion method
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography; HisTrap column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta2 (DE3) cells; expressed in Escherichia coli Rosetta2 (DE3) cells
expressed in Mus musculus
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expression of the enzyme in HEK-293 cells using a luciferase reporter vector, PARP-1 expression analysis, overview
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gene PARP11, chromosomal location 12p13.3, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview; gene PARP14, chromosomal location 3q21.1, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview; gene PARP16, chromosomal location 15q22.2, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview; gene PARP1, chromosomal location 1q41-q42, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview; gene PARP2, chromosomal location 14q11.2-q12, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview; gene PARP3, chromosomal location 3p21.1-22.2, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview; gene PARP4, chromosomal location 13q11, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview; gene PARP6, chromosomal location 15q22.23, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview; gene TNKS1, chromosomal location 8p23.1, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
PARP-1, DNA and amino acid sequence determination and analysis of wild-type and mutant genes
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G888W
inactive; inactive
H532A
inactive
I163A
the enzyme shows wild type activity
Y564A
inactive
additional information