Protein-synthesizing GTPase

Protein-synthesizing GTPase
Identifiers
EC number 3.6.5.3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Protein-synthesizing GTPases (EC 3.6.5.3, 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.

References

  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.
This article is issued from Wikipedia - version of the 8/10/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.