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

NAD(P)+-protein-arginine ADP-ribosyltransferase
Identifiers
EC number	2.4.2.31
CAS number	Template:CAS
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 / EGO
Search PMC articles PubMed articles NCBI proteins

ART
File:PDB 1gy0 EBI.jpg 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
SCOP	1gy0
SUPERFAMILY	1gy0
Available protein structures: Pfam structures 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 $\rightleftharpoons$ 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, 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.

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.

Further reading

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