ExplorEnz: EC 2.4.2.31

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2.4.2.31

Accepted name:

NAD⁺—protein-arginine ADP-ribosyltransferase

Reaction:

NAD⁺ + protein L-arginine = nicotinamide + N^ω-(ADP-D-ribosyl)-protein-L-arginine

Other name(s):

ADP-ribosyltransferase; mono(ADP-ribosyl)transferase; NAD⁺:L-arginine ADP-D-ribosyltransferase; NAD(P)⁺-arginine ADP-ribosyltransferase; NAD(P)⁺:L-arginine ADP-D-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

Systematic name:

NAD⁺:protein-L-arginine ADP-D-ribosyltransferase

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 N^ω-[(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).

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 81457-93-4

References:

1.	Moss, J., Stanley, S.J. and Oppenheimer, N.J. Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes. J. Biol. Chem. 254 (1979) 8891–8894. [PMID: 225315]
2.	Moss, J., Stanley, S.J. and Watkins, P.A. Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes. J. Biol. Chem. 255 (1980) 5838–5840. [PMID: 6247348]
3.	Ueda, K. and Hayaishi, O. ADP-ribosylation. Annu. Rev. Biochem. 54 (1985) 73–100. [DOI] [PMID: 3927821]
4.	Corda, D. and Di Girolamo, M. Functional aspects of protein mono-ADP-ribosylation. EMBO J. 22 (2003) 1953–1958. [DOI] [PMID: 12727863]
5.	Paone, G., Stevens, L.A., Levine, R.L., Bourgeois, C., Steagall, W.K., Gochuico, B.R. and Moss, J. ADP-ribosyltransferase-specific modification of human neutrophil peptide-1. J. Biol. Chem. 281 (2006) 17054–17060. [DOI] [PMID: 16627471]

[EC 2.4.2.31 created 1984, modified 1990, modified 2006]