Protein-synthesizing GTPase
EC no.
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB 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 TV, Bommer UA, Babkina GT, Karpova GG (October 1984). "GTP interacts with the gamma-subunit of eukaryotic initiation factor eIF-2". FEBS Letters. 175 (2): 313–6. doi:10.1016/0014-5793(84)80758-9. PMID 6566615.
  2. ^ Kisselev LL (1995). "Termination of translation in eukaryotes". Biochemistry and Cell Biology. 73 (11–12): 1079–86. doi:10.1139/o95-116. PMID 8722024.
  3. ^ Rodnina MV, Savelsbergh A, Katunin VI, Wintermeyer W (January 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 DV, Pavlov MY, MacDougall J, Buckingham RH, Ehrenberg M (July 1997). "Release factor RF3 in E.coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner". The EMBO Journal. 16 (13): 4126–33. doi:10.1093/emboj/16.13.4126. PMC 1170035. PMID 9233821.
  5. ^ Krab IM, Parmeggiani A (November 1998). "EF-Tu, a GTPase odyssey". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1443 (1–2): 1–22. doi:10.1016/s0167-4781(98)00169-9. PMID 9838020.