| EC |
2.4.2.36 |
| Accepted name: |
NAD+—diphthamide ADP-ribosyltransferase |
| Reaction: |
NAD+ + diphthamide-[translation elongation factor 2] = nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2] |
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For diagram of diphthamide biosynthesis, click here |
| Glossary: |
diphthamide = 2-[4-amino-4-oxo-3-(trimethylammonio)butyl]-L-histidine |
| Other name(s): |
ADP-ribosyltransferase; mono(ADPribosyl)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 |
| Comments: |
Diphtheria 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: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 52933-21-8 |
| 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 (1984) 2703–2707. [DOI] [PMID: 6326138] |
| 2. |
Ueda, K. and Hayaishi, O. ADP-ribosylation. Annu. Rev. Biochem. 54 (1985) 73–100. [DOI] [PMID: 3927821] |
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| [EC 2.4.2.36 created 1990, modified 2013] |
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