| Value |
190
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 labeled tRNAs |
| Comments |
The initial selection of tRNA is comprised of initial binding step, which is independent of the codon/anti codon interaction, Coding recognition step, in which codon/anticodon recognition occurs and a GTPase activation step. Constant is for coding recognition of (EF-Tu+ GTP+ aa-tRNA) ternary complex and A site of ribosome. This value is similar both for cognate (correct) codons and near cognate (that differ by one nucleotide) codons |
| Entered by |
Uri M |
| ID |
103472 |