IntEnz

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

IntEnz Enzyme Nomenclature
EC 2.4.2.31

Names

Reactions

• 19149 [IUBMB]
  L-arginyl-[protein]

  L-arginyl-[protein]

  GENERIC:10532

  Is ROOT: no
  ROOT compound: GENERIC:9624

  Number of residues: 1

  L-arginine residue L-arginine residue Name origin: UniProt - CHECKED (C) CHEBI:29965 Formula: C6H13N4O Charge: 1 Position: undefined ChEBI compound status: CHECKED (C)

  +

  NAD⁺

  NAD(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:57540

  Formula: C21H26N7O14P2
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  =

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  N^ω-(ADP-D-ribosyl)-L-arginyl-[protein]

  N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein]

  GENERIC:11346

  Is ROOT: no
  ROOT compound: GENERIC:9624

  Number of residues: 1

  Nω-(ADP-D-ribosyl)-L-arginine residue N(omega)-(ADP-D-ribosyl)-L-arginine residue Name origin: UniProt - CHECKED (C) CHEBI:83960 Formula: C21H32N9O14P2 Charge: -1 Position: undefined ChEBI compound status: CHECKED (C)

  +

  nicotinamide

  nicotinamide

  Name origin: UniProt - CHECKED (C)

  CHEBI:17154

  Formula: C6H6N2O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  
• 54884
  L-arginyl-[protein]

  L-arginyl-[protein]

  GENERIC:10532

  Is ROOT: no
  ROOT compound: GENERIC:9624

  Number of residues: 1

  L-arginine residue L-arginine residue Name origin: UniProt - CHECKED (C) CHEBI:29965 Formula: C6H13N4O Charge: 1 Position: undefined ChEBI compound status: CHECKED (C)

  +

  NADP⁺

  NADP(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:58349

  Formula: C21H25N7O17P3
  Charge: -3

  ChEBI compound status: CHECKED (C)

  

  =

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  N^ω-(2'-phospho-ADP-D-ribosyl)-L-arginyl-[protein]

  N(omega)-(2'-phospho-ADP-D-ribosyl)-L-arginyl-[protein]

  GENERIC:14033

  Is ROOT: no
  ROOT compound: GENERIC:9624

  Number of residues: 1

  Nω-(2'-phospho-ADP-D-ribosyl)-L-arginine residue N(omega)-(2'-phospho-ADP-D-ribosyl)-L-arginine residue Name origin: UniProt - CHECKED (C) CHEBI:138385 Formula: C21H31N9O17P3 Charge: -3 Position: undefined ChEBI compound status: CHECKED (C)

  +

  nicotinamide

  nicotinamide

  Name origin: UniProt - CHECKED (C)

  CHEBI:17154

  Formula: C6H6N2O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

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 enzymatic activities. (cf. EC 2.4.2.36 NAD⁺—diphthamide ADP-ribosyltransferase).

Links to other databases

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]