Reaction: NAD+ + protein L-arginine = nicotinamide + Nω-(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
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 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: BRENDA, EXPASY, 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. [PMID: 3927821]
4. Corda, D. and Di Girolamo, M. Functional aspects of protein mono-ADP-ribosylation. EMBO J. 22 (2003) 1953-1958. [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) 17054Ð17060. [PMID: 16627471]