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

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NAD(P)+-protein-arginine ADP-ribosyltransferase
Identifiers
EC number 2.4.2.31
CAS number 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 / EGO
ART
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

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.[1]

Structural studies[edit]

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[edit]

  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[edit]

  • 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. 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. 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