| Value |
85
sec^-1
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Hani S. Zaher and Rachel Green, Fidelity at the Molecular Level: Lessons from Protein Synthesis. Cell Volume 136, Issue 4, 20 February 2009, Pages 746-762PubMed ID19239893
|
| Primary Source |
T. Pape, W. Wintermeyer and M.V. Rodnina, Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E-coli ribosome, EMBO J. 17 (1998), pp. 7490–7497.PubMed ID9857203
|
| Method |
pre-steady-state kinetic experiments. Rate constants monitored by fluorescence changes in a proflavin-labeled tRNAPhe derivative. |
| Comments |
Constant is for unbinding of (EF-Tu+ GTP+ aa-tRNA) ternary complex and A site of ribosome |
| Entered by |
Uri M |
| ID |
103471 |