EC Number   |
Natural Substrates |
|---|
  2.1.1.314 | 4 S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] |
- |
| 2.1.1.314 | 4 S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] |
the eukaryotic enzyme is part of the biosynthetic pathway of diphthamide. The modification is sufficient to create diphtheria toxin sensitivity |
| 2.1.1.314 | 4 S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] |
eukaryotic diphthine synthase, Dph5, is a promiscuous methyltransferase that catalyzes an extraordinary N,O-tetramethylation of 2-(3-carboxy-3-aminopropyl)-L-histidine to yield diphthine methyl ester. This compound is an intermediates in the biosynthesis of the post-translationally modified histidine residue diphthamide, a unique and essential residue part of the eukaryotic elongation factor 2 (eEF2) |
| 2.1.1.314 | 4 S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] |
in eukaryotes, the modification of an invariant histidine (His-699 in yeast) residue in translation elongation factor 2 (EF2) with diphthamide involves a conserved pathway encoded by the DPH1-DPH7 gene network. Diphthamide is the target for diphtheria toxin and related lethal ADP ribosylases, which collectively kill cells by inactivating the essential translocase function of EF2 during mRNA translation and protein biosynthesis |
| 2.1.1.314 | 4 S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] |
post-translational modification of eukaryotic elongation factor 2 (eEF2) |
| 2.1.1.314 | 4 S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] |
the enzyme is involved in the diphthamide modification pathway |
