In enzymology, a NAD+-diphthamide ADP-ribosyltransferase (EC 2.4.2.36) is an enzyme that catalyzes the chemical reaction
NAD+ + peptide diphthamide ⇌ {\displaystyle \rightleftharpoons } nicotinamide + peptide N-(ADP-D-ribosyl)diphthamide Thus, the two substrates of this enzyme are NAD+ and peptide diphthamide, whereas its two products are nicotinamide and peptide N-(ADP-D-ribosyl)diphthamide. This enzyme belongs to the family of glycosyltransferases, to be specific, the pentosyltransferases. The systematic name of this enzyme class is NAD+:peptide-diphthamide N-(ADP-D-ribosyl)transferase. Other names in common use include ADP-ribosyltransferase, mono(ADPribosyl)transferase, and NAD-diphthamide ADP-ribosyltransferase.
Structural studies As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1S5B, PDB: 1S5C, PDB: 1S5D, PDB: 1S5E, PDB: 1S5F, PDB: 1SGK, PDB: 1TOX, PDB: 1XDT, PDB: 1XK9, PDB: 1ZM3, PDB: 1ZM4, PDB: 1ZM9, PDB: 2A5D, PDB: 2A5F, and PDB: 2A5G.
Clinical significance The extracellular ADP-ribosyl-transferase ART2 is expressed only on T cells. T cell activation of P2X7 receptors can activate the T cells or cause T cell differentiation, can affect T cell migration or (at high extracellular levels of NAD+) can induce cell death by ART2.
References
Lee H, Iglewski WJ (1984). "Cellular ADP-ribosyltransferase with the same mechanism of action as diphtheria toxin and Pseudomonas toxin A". Proc. Natl. Acad. Sci. U.S.A. 81 (9): 2703–7. Bibcode:1984PNAS...81.2703L. doi:10.1073/pnas.81.9.2703. PMC 345138. PMID 6326138. Ueda K, Hayaishi O (1985). "ADP-ribosylation". Annu. Rev. Biochem. 54 (1): 73–100. doi:10.1146/annurev.bi.54.070185.000445. PMID 3927821.
See also Diphtheria toxin Pseudomonas exotoxin ADP-ribosylation
