EC 2.4.2.36 - NAD+—diphthamide ADP-ribosyltransferase

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IntEnz Enzyme Nomenclature
EC 2.4.2.36

Names

Accepted name:
NAD+—diphthamide ADP-ribosyltransferase
Other names:
ADP-ribosyltransferase
mono(ADPribosyl)transferase
mono(ADP-ribosyl)transferase
NAD—diphthamide ADP-ribosyltransferase
NAD+:peptide-diphthamide N-(ADP-D-ribosyl)transferase
Systematic name:
NAD+:diphthamide-[translation elongation factor 2] N-(ADP-D-ribosyl)transferase

Reaction

Comments:

Dihtheria toxin and some other bacterial toxins catalyse this reaction, which inactivates translation elongation factor 2 (EF2). The acceptor is diphthamide, a unique modification of a histidine residue in the elongation factor found in archaebacteria and all eukaryotes, but not in eubacteria. cf. EC 2.4.2.31 NAD(P)+—protein-arginine ADP-ribosyltransferase. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047286
CAS Registry Number: 52933-21-8
UniProtKB/Swiss-Prot:

References

  1. Lee, H. and Iglewski, W.J.
    Cellular ADP-ribosyltransferase with the same mechanism of action as diphtheria toxin and Pseudomonas toxin A.
    Proc. Natl. Acad. Sci. USA 81: 2703-2707 (1984). [PMID: 6326138]
  2. Ueda, K. and Hayaishi, O.
    ADP-ribosylation.
    Annu. Rev. Biochem. 54: 73-100 (1985). [PMID: 3927821]

[EC 2.4.2.36 created 1990, modified 2013]