EC 2.4.2.31 - NAD+—protein-arginine ADP-ribosyltransferase
IntEnz Enzyme Nomenclature
EC 2.4.2.31
Names
NAD(P)+-arginine ADP-ribosyltransferase
mono(ADP-ribosyl)transferase
NAD+:L-arginine ADP-D-ribosyltransferase
NAD(P)+:L-arginine ADP-D-ribosyltransferase
NAD(P)+—arginine ADP-ribosyltransferase
mono-ADP-ribosyltransferase
ART
ART1
ART2
ART3
ART4
ART5
ART6
ART7
NAD(P)+—protein-arginine ADP-ribosyltransferase
NAD(P)+:protein-L-arginine ADP-D-ribosyltransferase
Reactions
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19149 [IUBMB]L-arginyl-[protein]GENERIC:10532Is ROOT: no
ROOT compound: GENERIC:9624Number of residues: 1NAD+Name origin: UniProt - CHECKED (C)Formula: C21H26N7O14P2
Charge: -1ChEBI compound status: CHECKED (C)=H+Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C)Nω-(ADP-D-ribosyl)-L-arginyl-[protein]GENERIC:15087Is ROOT: no
ROOT compound: GENERIC:9624Number of residues: 1 -
L-arginyl-[protein]GENERIC:10532Is ROOT: no
ROOT compound: GENERIC:9624Number of residues: 1NADP+Name origin: UniProt - CHECKED (C)Formula: C21H25N7O17P3
Charge: -3ChEBI compound status: CHECKED (C)=H+Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C)Nω-(2'-phospho-ADP-D-ribosyl)-L-arginyl-[protein]GENERIC:14033Is ROOT: no
ROOT compound: GENERIC:9624Number of residues: 1
Comments:
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 Nω-[(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 enzymatic activities. (cf. EC 2.4.2.36 NAD+—diphthamide ADP-ribosyltransferase).
Links to other databases
References
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Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes.J. Biol. Chem. 254 : 8891-8894 (1979). [PMID: 225315]
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Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes.J. Biol. Chem. 255 : 5838-5840 (1980). [PMID: 6247348]
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ADP-ribosylation.Annu. Rev. Biochem. 54 : 73-100 (1985). [PMID: 3927821]
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Functional aspects of protein mono-ADP-ribosylation.EMBO J. 22 : 1953-1958 (2003). [PMID: 12727863]
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ADP-ribosyltransferase-specific modification of human neutrophil peptide-1.J. Biol. Chem. 281 : 17054-17060 (2006). [PMID: 16627471]
[EC 2.4.2.31 created 1984, modified 1990, modified 2006]