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

NAD(P)+-protein-arginine ADP-ribosyltransferase
Identifiers
EC no.	2.4.2.31
CAS no.	81457-93-4
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

ART
crystal structure of the eucaryotic mono-adp-ribosyltransferase art2.2; crystal form c (p3121)
Identifiers
Symbol	ART
Pfam	PF01129
Pfam clan	CL0084
InterPro	IPR000768
SMART	START
PROSITE	PDOC00993
SCOP2	1gy0 / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

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 ${\displaystyle \rightleftharpoons }$ nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine NADP^+ + protein L-arginine ${\displaystyle \rightleftharpoons }$ 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 ${\displaystyle \rightleftharpoons }$ nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine NADP^+ + protein L-arginine ${\displaystyle \rightleftharpoons }$ 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, and NAD(P)+:L-arginine ADP-D-ribosyltransferase.

At least five forms of the enzyme have been characterised to date, some of which are attached to the membrane via glycosylphosphatidylinositol (GPI) anchors, while others appear to be secreted. The enzymes contain ~250-300 residues, which encode putative signal sequences and carbohydrate attachment sites. In addition, the N- and C-termini are predominantly hydrophobic, a characteristic of GPI-anchored proteins.[1]

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.

References

1. Okazaki IJ, Zolkiewska A, Nightingale MS, Moss J (November 1994). "Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferases". Biochemistry. 33 (43): 12828–36. doi:10.1021/bi00209a014. PMID 7947688.

Further reading

• 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 (18): 8891–4. doi:10.1016/S0021-9258(19)86783-2. 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 (12): 5838–40. doi:10.1016/S0021-9258(19)70705-4. PMID 6247348.
• Ueda K, Hayaishi O (1985). "ADP-ribosylation". Annu. Rev. Biochem. 54 (1): 73–100. doi:10.1146/annurev.bi.54.070185.000445. PMID 3927821.

This article incorporates text from the public domain Pfam and InterPro: IPR000768