NAD(+)—diphthamide ADP-ribosyltransferase
In enzymology, a NAD+-diphthamide ADP-ribosyltransferase (EC 2.4.2.36) is an enzyme that catalyzes the chemical reaction
| NAD+-diphthamide ADP-ribosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.2.36 | ||||||||
| CAS no. | 52933-21-8 | ||||||||
| 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 | ||||||||
| |||||||||
- NAD+ + peptide diphthamide 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
editAs of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes 1S5B, 1S5C, 1S5D, 1S5E, 1S5F, 1SGK, 1TOX, 1XDT, 1XK9, 1ZM3, 1ZM4, 1ZM9, 2A5D, 2A5F, and 2A5G.
Clinical significance
editThe extracellular ADP-ribosyl-transferase ART2 is expressed only on T cells.[1] 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.[1]
References
edit- ^ a b Rivas-Yáñez E, Barrera-Avalos C, Bono R, Sauma D (2020). "P2X7 Receptor at the Crossroads of T Cell Fate". International Journal of Molecular Sciences. 21 (14): 4937. doi:10.3390/ijms21144937. PMC 7404255. PMID 32668623.
- 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
edit