Protein-synthesizing GTPase

Protein-synthesizing GTPase
EC number
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Protein-synthesizing GTPases (EC, elongation factor (EF), initiation factor (IF), peptide-release or termination factor) are enzymes involved in mRNA translation into protein by the ribosome, with systematic name GTP phosphohydrolase (mRNA-translation-assisting).[1][2][3][4][5] They usually include translation initiation factors such as IF-2 and translation elongation factors such as EF-Tu.


  1. Kurzchalia, T.V.; Bommer, U.A.; Babkina, G.T.; Karpova, G.G. (1984). "GTP interacts with the γ-subunit of eukaryotic initiation factor EIF-2". FEBS Lett. 175 (2): 313–316. doi:10.1016/0014-5793(84)80758-9. PMID 6566615.
  2. Kisselev, L.L.; Frolova, L.Yu. (1995). "Termination of translation in eukaryotes". Biochem. Cell Biol. 73 (11-12): 1079–1086. doi:10.1139/o95-116. PMID 8722024.
  3. Rodnina, M.V.; Savelsberg, A.; Katunin, V.I.; Wintermeyer, W. (1997). "Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome". Nature. 385 (6611): 37–41. doi:10.1038/385037a0. PMID 8985244.
  4. Freistroffer, D.V.; Pavlov, M.Y.; MacDougall, J.; Buckingham, R.H.; Ehrenberg, M. (1997). "Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner". EMBO J. 16: 4126–4133. doi:10.1093/emboj/16.13.4126. PMID 9233821.
  5. Krab, I.M.; Parmeggiani, A. (1998). "EF-Tu, a GTPase odyssey". Biochim. Biophys. Acta. 1443 (1-2): 1–22. doi:10.1016/s0167-4781(98)00169-9. PMID 9838020.
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