EC 2.4.2.31 - NAD+—protein-arginine ADP-ribosyltransferase

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IntEnz Enzyme Nomenclature
EC 2.4.2.31

Names

Accepted name:
NAD+—protein-arginine ADP-ribosyltransferase
Other names:
ADP-ribosyltransferase
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
Systematic name:
NAD+:protein-L-arginine ADP-D-ribosyltransferase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00993
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003956
CAS Registry Number: 81457-93-4
UniProtKB/Swiss-Prot: (29) [show] [UniProt]

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: 8891-8894 (1979). [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: 5838-5840 (1980). [PMID: 6247348]
  3. Ueda, K. and Hayaishi, O.
    ADP-ribosylation.
    Annu. Rev. Biochem. 54: 73-100 (1985). [PMID: 3927821]
  4. Corda, D. and Di Girolamo, M.
    Functional aspects of protein mono-ADP-ribosylation.
    EMBO J. 22: 1953-1958 (2003). [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: 17054-17060 (2006). [PMID: 16627471]

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