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Information on EC 3.6.5.3 - protein-synthesizing GTPase

for references in articles please use BRENDA:EC3.6.5.3
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IUBMB 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-1alpha (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-1alpha 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.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
elongation factor, gtpase-activating protein, eif2alpha, elongation factor tu, eif2b, eef1a, ef-1alpha, eukaryotic initiation factor 2, elongation factor g, elongation factor 1 alpha, more
REACTION
REACTION DIAGRAM
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UNIPROT
LITERATURE
GTP + H2O = GDP + phosphate
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