EC Number   |
Natural Substrates |
|---|
   2.4.2.36 | eEF2 + NAD+ |
i.e. eukaryotic elongation factor 2, contains a post-translationally modified histidine residue, known as diphthamide, which is the specific ADP-ribosylation target of Pseudomonas aeruginosa exotoxin A |
| 2.4.2.36 | more |
NAD+-dependent ADP-ribosyltransfer (ADPRT) including NAD+-glycohydrolysis (GH) activity, deadly virulent due to covalent modification and thus inactivation of proteins that are essential for the host |
| 2.4.2.36 | NAD+ + diphthamide-[Escherichia coli elongation factor Tu] |
- |
| 2.4.2.36 | NAD+ + diphthamide-[translation elongation factor 2] |
- |
| 2.4.2.36 | NAD+ + elongation factor 2 |
- |
| 2.4.2.36 | NAD+ + elongation factor 2 |
liver enzyme |
| 2.4.2.36 | NAD+ + elongation factor 2 |
NAD-glycohydrolase activity without acceptor substrate |
| 2.4.2.36 | NAD+ + elongation factor 2 |
i.e. elongation factor 2 of baby hamster kidney cells, forward ADP-ribosylation reaction is reversed by fragment A from Pseudomonas aeruginosa |
| 2.4.2.36 | NAD+ + essential ribosomal elongation factor 2 |
transfer of ADP-ribose moiety (oxocarbenium ion) of NAD+ onto N3 of diphthamide imidazole of essential ribosomal elongation factor 2 (eEF2) |
| 2.4.2.36 | NAD+ + G-protein |
NAD-dependent ADP-ribosylation of Arg201 of G-protein alpha-subunit, this locks the G-protein in its active state producing cAMP |
