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ENZYME entry: EC 184.108.40.206
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|Elongation factor (EF).|
|Initiation factor (IF).|
|Peptide-release factor (RF).|
|Peptide-release or termination factor.|
|GTP + H(2)O <=> GDP + phosphate|
- 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 hydrolyzes it in prokaryotes.
- In eukaryotes, it is eIF-2 (150 kDa) that binds GTP.
- In the elongation phase, the GTP-hydrolyzing proteins are the EF-Tu
polypeptide of the prokaryotic transfer factor (43 kDa),
the eukaryotic elongation factor EF-1-alpha (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-1-alpha catalyze binding of aminoacyl-tRNA to the
ribosomal A-site, while EF-G and EF-2 catalyze 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.
- Formerly EC 220.127.116.11.
|PROSITE||PDOC00273 ; PDOC00905 ; PDOC00970|
|PRIAM enzyme-specific profiles||18.104.22.168|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.124|
|IUBMB Enzyme Nomenclature||126.96.36.199|
|MEDLINE||Find literature relating to 188.8.131.52|
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