Search results for EEF2

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Reaction (9 results from a total of 9)

Identifier: R-HSA-156930
Species: Homo sapiens
Compartment: cytosol
At the beginning of this reaction, 1 molecule of 'eEF2', and 1 molecule of 'GTP' are present. At the end of this reaction, 1 molecule of 'eEF2:GTP' is present.

This reaction takes place in the 'cytosol' (Guillot et al. 2013).
Identifier: R-HSA-8932243
Species: Homo sapiens
Compartment: cytosol
Protein-lysine N-methyltransferase EEF2KMT (EEF2KMT) catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on Lys-525.
Identifier: R-HSA-5367022
Species: Homo sapiens
Compartment: cytosol
By analogy to the activity of its experimentally characterized budding yeast homolog (Lin et al. 2014; Schaffrath et al. 2014), cytosolic DPH7 is inferred to catalyze the removal of a methyl group of Me-diphthine EEF2, yielding diphthine EEF2.
Identifier: R-HSA-5358484
Species: Homo sapiens
Compartment: cytosol
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).
Identifier: R-HSA-5358494
Species: Homo sapiens
Compartment: cytosol
The diphthamide biosynthesis protein 2 (DPH2) subunit of the cytosolic DPH1:DPH2:DPH3 complex catalyzes the transfer of a 3-amino-3-carboxypropyl group from S-adenosylmethionine (AdoMet) to residue 715 of nascent elongation factor 2 (EEF2), forming aminocarboxypropyl EEF2 and S-methylthioadenosine (MTAD). The association of DPH1, 2, and 3 to form a complex is inferred from studies of the homologous yeast proteins (Abdel-Fattah et al. 2013; Bar et al. 2008) and more limited studies of interactions among mouse and human ones (Liu et al. 2004). The identification of DPH2 as the catalytically active subunit of the DPH1:DPH2:DPH3 complex is inferred from the properties of the homologous Pyrococcus horikoshii protein (Zhang et al. 2010). DPH4 (DNAJC24) is needed for the reaction to occur but its exact role is unknown (Liu et al. 2004; Su et al. 2013). DPH3 is an electron donor for DPH1-DPH2 in the first step of diphthamide biosynthesis (Dong et al. 2014).
Identifier: R-HSA-5358475
Species: Homo sapiens
Compartment: cytosol
Cytosolic diphthamide biosynthesis protein 6 (DPH6) ligates an ammonium ion to diphthine-EEF2 to generate diphthamide-EEF2 in a reaction coupled to the hydrolysis of ATP to yield AMP and PPi (Su et al. 2012; Uthman et al. 2013; Wei et al. 2013).
Identifier: R-HSA-165758
Species: Homo sapiens
Compartment: cytosol
Phosphorylation of eEF2 kinase by S6K1-P results in decreased activity of this kinase. eEF2 kinase normally phosphorylates and deactivates eEF2, preventing its binding to the ribosome.
Identifier: R-HSA-5336421
Species: Homo sapiens
Compartment: cytosol
Target cell elongation factor 2 (EEF2) is ADP-ribosylated in a reaction catalyzed by cytosolic diphtheria toxin fragment A (DT A), inactivating it (Honjo et al. 1971; Van Ness et al. 1980a,b). The loss of EEF2 activity blocks target cell protein synthesis, and a small number of DT A molecules are capable of inactivating sufficient EEF2 to cause target cell death (Collier 1975).
Identifier: R-HSA-156915
Species: Homo sapiens
Compartment: cytosol
Following peptide bond formation, GTP-bound eEF2 catalyzes the translocation of the deacylated tRNA in the P-site and the peptidyl-tRNA in the A-site (the pre-translocation state) into the E- and P- sites (the post-translocation state), respectively. Thus, the mRNA advances by three bases to expose the next codon in the A-site. After translocation, GDP-bound eEF2 leaves the ribosome to allow another round of elongation. eEF2 is reactivated by the release of GDP and binds GTP for subsequent rounds.
This process is illustrated below with a peptidyl-tRNA with a growing peptide, a deacylated tRNA with an -OH and a ribosome with A,P and E sites to accommodate these three forms of tRNA is also shown.
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