EC 3 - Hydrolases
EC 3.6 - Acting on acid anhydrides
EC 3.6.5 - Acting on GTP; involved in cellular and subcellular movement
EC 3.6.5.3 - Protein-synthesizing GTPase
IntEnz Enzyme Nomenclature
EC 3.6.5.3
Names
initiation factor (IF)
peptide-release or termination factor
Reaction
- GTP + H2O = GDP + phosphate
Comments:
This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis. In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyses it in prokaryotes. In eukaryotes, it is eIF-2 (150 kDa) that binds GTP. In the elongation phase, the GTP-hydrolysing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1α (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa). EF-Tu and EF-1α catalyse binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyse the translocation of peptidyl-tRNA from the A-site to the P-site. GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs.
Links to other databases
References
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GTP interacts with the γ-subunit of eukaryotic initiation factor EIF-2.FEBS Lett. 175 : 313-316 (1984). [PMID: 6566615]
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Termination of translation in eukaryotes.Biochem. Cell Biol. 73 : 1079-1086 (1995). [PMID: 8722024]
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Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome.Nature 385 : 37-41 (1997). [PMID: 8985244]
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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 (1997). [PMID: 9233821]
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EF-Tu, a GTPase odyssey.Biochim. Biophys. Acta 1443 : 1-22 (1998). [PMID: 9838020]
[EC 3.6.5.3 created 2000 as EC 3.6.1.48, transferred 2003 to EC 3.6.5.3]