“NAD(P)(+)—protein-arginine ADP-ribosyltransferase”的意思、由来-开放百科全书

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

释义

Structural studies
References
Further reading

{{enzyme
| Name = NAD(P)+-protein-arginine ADP-ribosyltransferase
| EC_number = 2.4.2.31
| CAS_number = 81457-93-4
| IUBMB_EC_number = 2/4/2/31
| GO_code = 0003956
| image =
| width =
| caption =
}}{{Infobox protein family
| Symbol = ART
| Name = ART
| image = PDB 1gy0 EBI.jpg
| width =
| caption = crystal structure of the eucaryotic mono-adp-ribosyltransferase art2.2; crystal form c (p3121)
| Pfam = PF01129
| Pfam_clan = CL0084
| InterPro = IPR000768
| SMART = START
| PROSITE = PDOC00993
| MEROPS =
| SCOP = 1gy0
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}

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

NAD⁺ + protein L-arginine nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine NADP⁺ + protein L-arginine 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 nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine NADP⁺ + protein L-arginine 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 {{PDB link|1GXY}}, {{PDB link|1GXZ}}, {{PDB link|1GY0}}, {{PDB link|1OG1}}, {{PDB link|1OG3}}, and {{PDB link|1OG4}}.

References

1. ^{{cite journal | vauthors = Okazaki IJ, Zolkiewska A, Nightingale MS, Moss J | title = Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferases | journal = Biochemistry | volume = 33 | issue = 43 | pages = 12828–36 |date=November 1994 | pmid = 7947688 | doi = 10.1021/bi00209a014| url = }}

Structural studies

References

Further reading