DPH5 transfers four methyl groups from AdoMet to aminocarboxypropyl EEF2

Stable Identifier
R-HSA-5358484
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
1508200 DPH5, a methyltransferase gene required for diphthamide biosynthesis in Saccharomyces cerevisiae

Mattheakis, LC, Shen, WH, Collier, RJ

Mol. Cell. Biol. 1992
3346227 The post-translational trimethylation of diphthamide studied in vitro

Moehring, JM, Moehring, TJ

J. Biol. Chem. 1988
15485916 Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2

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

Mol. Cell. Biol. 2004
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
diphthine synthase activity of DPH5 [cytosol]
Physical Entity
Activity
Orthologous Events
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Created