Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.6.5.3 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

Activating Compound Comment Organism Structure
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
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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Synonyms

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