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Information on EC 2.4.2.31 - NAD+-protein-arginine ADP-ribosyltransferase

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.31 NAD+-protein-arginine ADP-ribosyltransferase
IUBMB Comments
Protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in the regulation of cellular activities . Arginine residues in proteins act as acceptors. Free arginine, agmatine [(4-aminobutyl)guanidine], arginine methyl ester and guanidine can also do so. The enzyme from some, but not all, species can also use NADP+ as acceptor (giving rise to Nomega-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine as the product), but more slowly [1,5]. The enzyme catalyses the NAD+-dependent activation of EC 4.6.1.1, adenylate cyclase. Some bacterial enterotoxins possess similar enzymic activities. (cf. EC 2.4.2.36 NAD+---diphthamide ADP-ribosyltransferase).
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UNIPROT: Q844J9
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
at1, at2, iota toxin, rt6.1, rt6.2, mono(adp-ribosyl)transferase, arginine-specific adp-ribosyltransferase, nad:arginine adp-ribosyltransferase, arginine-specific mono-adp-ribosyltransferase, xopai, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
VIP2
the A component of the binary toxin
(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-arginine
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ADP-ribosyltransferase
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ADPRT
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alloantigen Rt6.1
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alloantigen Rt6.2
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arginine specific ADP-ribosyltransferase
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arginine specific mono-ADP-ribosyltransferase
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arginine-specific mono-ADP-ribosyltransferase
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ART
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AT1
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AT2
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Dombrock blood group carrier molecule
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mono(ADP-ribosyl)transferase
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NAD(P)+-arginine ADP-ribosyltransferase
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NAD+:arginine ADP-ribosyltransferase
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NAD+:arginine ecto-mono(ADP-ribosyl)transferase
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NAD+:L-arginine ADP-D-ribosyltransferase
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NAD-arginine ADP-ribosyltransferase
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NAD-arginine mono-ADP-ribosyltransferase B
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NAD-dependent ADPribosyltransferase
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NAD:arginine ADP-ribosyltransferase B
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RT6
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RT6.1
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RT6.2
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T-cell surface protein Rt6.1
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T-cell surface protein Rt6.2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
NAD+:protein-L-arginine ADP-D-ribosyltransferase
Protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in the regulation of cellular activities [4]. Arginine residues in proteins act as acceptors. Free arginine, agmatine [(4-aminobutyl)guanidine], arginine methyl ester and guanidine can also do so. The enzyme from some, but not all, species can also use NADP+ as acceptor (giving rise to Nomega-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine as the product), but more slowly [1,5]. The enzyme catalyses the NAD+-dependent activation of EC 4.6.1.1, adenylate cyclase. Some bacterial enterotoxins possess similar enzymic activities. (cf. EC 2.4.2.36 NAD+---diphthamide ADP-ribosyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
81457-93-4
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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+ + [actin]-L-arginine177
nicotinamide + [actin]-N-(ADP-D-ribosyl)-L-arginine177 + 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+ + [actin]-L-arginine177
nicotinamide + [actin]-N-(ADP-D-ribosyl)-L-arginine177 + H+
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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?
Q844J9_BACTU
462
0
52374
TrEMBL
other Location (Reliability: 2)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
the enzyme is used as insectizide
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chakroun, M.; Banyuls, N.; Bel, Y.; Escriche, B.; Ferre, J.
Bacterial vegetative insecticidal proteins (Vip) from entomopathogenic bacteria
Microbiol. Mol. Biol. Rev.
80
329-350
2016
Bacillus thuringiensis (Q844J9)
Manually annotated by BRENDA team