Biology:Protein-synthesizing GTPase
From HandWiki
Short description: Class of enzymes
| 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
- ↑ "GTP interacts with the gamma-subunit of eukaryotic initiation factor eIF-2". FEBS Letters 175 (2): 313–6. October 1984. doi:10.1016/0014-5793(84)80758-9. PMID 6566615.
- ↑ "Termination of translation in eukaryotes". Biochemistry and Cell Biology 73 (11–12): 1079–86. 1995. doi:10.1139/o95-116. PMID 8722024.
- ↑ "Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome". Nature 385 (6611): 37–41. January 1997. doi:10.1038/385037a0. PMID 8985244.
- ↑ "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. July 1997. doi:10.1093/emboj/16.13.4126. PMID 9233821.
- ↑ "EF-Tu, a GTPase odyssey". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1443 (1–2): 1–22. November 1998. doi:10.1016/s0167-4781(98)00169-9. PMID 9838020.
External links
- Protein-synthesizing+GTPase at the US National Library of Medicine Medical Subject Headings (MeSH)
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