DPH5 transfers four methyl groups from AdoMet to aminocarboxypropyl EEF2

Stable Identifier
Reaction [transition]
Homo sapiens
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Cytosolic diphthamide biosynthesis protein 5 (DPH5) transfers four methyl groups from S-adenosylmethionine (AdoMet) to elongation factor 2 (EEF2) whose histidine residue at position 715 has been conjugated with a 3-amino 3-carboxypropyl group, forming methylated diphthine EEF2 and S-adenosylhomocysteine (AdoHcy). DPH5 activity has been identified in cells of diverse eukaryotic species including humans and has been characterized in detail in budding yeast (Liu et al. 2004; Matteakis et al. 1992; Moehring & Moehring 1988).

Literature References
PubMed ID Title Journal Year
3346227 The post-translational trimethylation of diphthamide studied in vitro

Moehring, TJ, Moehring, JM

J. Biol. Chem. 1988
1508200 DPH5, a methyltransferase gene required for diphthamide biosynthesis in Saccharomyces cerevisiae

Mattheakis, LC, Collier, RJ, Shen, WH

Mol. Cell. Biol. 1992
15485916 Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2

Leppla, SH, Liu, S, Kuremsky, JG, Fink, GR, Milne, GT

Mol. Cell. Biol. 2004
Catalyst Activity

diphthine synthase activity of DPH5 [cytosol]

Orthologous Events
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