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Literature summary extracted from

  • Mohr, D.; Wintermeyer, W.; Rodnina, M.V.
    GTPase activation of elongation factors Tu and G on the ribosome (2002), Biochemistry, 41, 12520-12528.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.6.5.3 ribosome stimulates GTPase activity of elongation factor Tu. The factor binding site is loacetd on the 50S ribosomal subunit and comprises proteins L7/12, L10, L11, the l11-binding region of 23 rRNA, and the sarcin-ricin loop of 23S rRNA. L7/12 stimulates the GTPase activity of elongation factor Tu by inducing the catalytically active conformation of the G domain Escherichia coli
3.6.5.3 ribosome stimulates GTPase activity of elongation factor Tu. The factor binding site is loacetd on the 50S ribosomal subunit and comprises proteins L7/12, L10, L11, the l11-binding region of 23 rRNA, and the sarcin-ricin loop of 23S rRNA. L7/12 stimulates the GTPase activity of elongation factor G by inducing the catalytically active conformation of the G domain Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.6.5.3 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.5.3 GTP + H2O elongation factor Tu Escherichia coli GDP + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.6.5.3 elongation factor G
-
 Escherichia coli
3.6.5.3 elongation factor Tu
-
 Escherichia coli