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Literature summary extracted from

  • Hansson, S.; Singh, R.; Gudkov, A.T.; Liljas, A.; Logan, D.T.
    Crystal structure of a mutant elongation factor G trapped with a GTP analogue (2005), FEBS Lett., 579, 4492-4497.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.5.3 structure of the mutant enzyme T84A in complex with the non-hydrolysable GTP analogue GDPNP Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.5.3 GTP + H2O Thermus thermophilus elongation factor G catalyzes the translocation step in protein synthesis on the ribosome GDP + phosphate
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Organism

EC Number Organism UniProt Comment Textmining
3.6.5.3 Thermus thermophilus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.5.3 GTP + H2O elongation factor G catalyzes the translocation step in protein synthesis on the ribosome Thermus thermophilus GDP + phosphate
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3.6.5.3 GTP + H2O enzyme-GTP and enzyme-GDP conformations in solution are very similar. The major contribution to the active GTPase conformation, which is quite different, therefore comes from its interaction with the ribosome Thermus thermophilus GDP + phosphate
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Synonyms

EC Number Synonyms Comment Organism
3.6.5.3 EF-G
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Thermus thermophilus
3.6.5.3 elongation factor G
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Thermus thermophilus