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Literature summary for 3.6.5.3 extracted from

  • Nagano, T.; Yutthanasirikul, R.; Hihara, Y.; Hisabori, T.; Kanamori, T.; Takeuchi, N.; Ueda, T.; Nishiyama, Y.
    Oxidation of translation factor EF-G transiently retards the translational elongation cycle in Escherichia coli (2015), J. Biochem., 158, 165-172 .
    View publication on PubMed
Search for more literature for 3.6.5.3

Cloned(Commentary)

Cloned (Comment) Organism
in vitro translation of the enzyme using the PURE reconstituted translation system derived from Escherichia coli Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Fusidic acid a specific inhibitor of the GTPase activity of EF-G, almost complete inhibition Escherichia coli
H2O2 oxidation of EF-G inhibits the function of EF-G on the ribosome. With hydrogen peroxide, neither the insertion of EF-G into the ribosome nor single-cycle translocation activity in vitro is affected, while the GTPase activity and the dissociation of EF-G from the ribosome are suppressed when EF-G is oxidized. The synthesis of longer peptides is suppressed to a greater extent than that of a shorter peptide when EF-G is oxidized Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Escherichia coli
-
 GDP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6M8
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
 Escherichia coli GDP + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
EF-G
-
 Escherichia coli
elongation factor G
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli

General Information

General Information Comment Organism
malfunction EF-G is inactivated upon formation of an intramolecular disulfide bond by Cys114 and Cys266. The enzyme is reactivated by thioredoxin, and replacement of Cys114 by serine allows H2O2-treated EF-G to support translation at the same rate as DTT-treated EF-G. Oxidation of EF-G inhibits the function of EF-G on the ribosome. The GTPase activity and the dissociation of EF-G from the ribosome are suppressed when EF-G is oxidized. With hydrogen peroxide, neither the insertion of EF-G into the ribosome nor single-cycle translocation activity in vitro is affected, while the GTPase activity and the dissociation of EF-G from the ribosome are suppressed when EF-G is oxidized. The synthesis of longer peptides is suppressed to a greater extent than that of a shorter peptide when EF-G is oxidized. The formation of the disulphide bond in EF-G might interfere with the hydrolysis of GTP that is coupled with dissociation of EF-G from the ribosome and might thereby retard the turnover of EF-G within the translational machinery Escherichia coli
physiological function elongation factor G (EF-G) is a key protein in translational elongation. It interacts with 70S ribosomes Escherichia coli