NAD(P)+-protein-arginine ADP-ribosyltransferase

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In enzymology, a NAD(P)+-protein-arginine ADP-ribosyltransferase (EC 2.4.2.31) is an enzyme that catalyzes the chemical reaction using nicotinamide adenine dinucleotide

NAD⁺ + protein L-arginine $\rightleftharpoons$ nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine NADP⁺ + protein L-arginine $\rightleftharpoons$ nicotinamide + Nomega-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine

as well as the corresponding reaction using nicotinamide adenine dinucleotide phosphate

NADP⁺ + protein L-arginine $\rightleftharpoons$ nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine NADP⁺ + protein L-arginine $\rightleftharpoons$ nicotinamide + Nomega-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine

Thus, the two substrates of this enzyme are NAD⁺ (or NADP⁺) and protein L-arginine, whereas its two products are nicotinamide and Nomega-(ADP-D-ribosyl)-protein-L-arginine (or Nomega-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine, respectively).

This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is NAD(P)+:protein-L-arginine ADP-D-ribosyltransferase. Other names in common use include ADP-ribosyltransferase, mono(ADP-ribosyl)transferase, NAD+:L-arginine ADP-D-ribosyltransferase, NAD(P)+-arginine ADP-ribosyltransferase, NAD(P)+-arginine ADP-ribosyltransferase, and NAD(P)+:L-arginine ADP-D-ribosyltransferase.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1GXY, 1GXZ, 1GY0, 1OG1, 1OG3, and 1OG4.

[edit] References

IUBMB entry for 2.4.2.31
BRENDA references for 2.4.2.31 (Recommended.)
PubMed references for 2.4.2.31
PubMed Central references for 2.4.2.31
Google Scholar references for 2.4.2.31
Moss J, Stanley SJ, Oppenheimer NJ (1979). "Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes". J. Biol. Chem. 254: 8891–4. PMID 225315.
Moss J, Stanley SJ, Watkins PA (1980). "Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes". J. Biol. Chem. 255: 5838–40. PMID 6247348.
Ueda K, Hayaishi O (1985). "ADP-ribosylation". Annu. Rev. Biochem. 54: 73–100. doi:10.1146/annurev.bi.54.070185.000445. PMID 3927821.