| Value |
3.2
sec^-1
Range: ±0.48 sec^-1
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Zhang G, Fedyunin I, Miekley O, Valleriani A, Moura A, Ignatova Z. Global and local depletion of ternary complex limits translational elongation. Nucleic Acids Res. 2010 Aug38(14):4778-87. doi: 10.1093/nar/gkq196. p.4781 left column bottom paragraphPubMed ID20360046
|
| Primary Source |
Uter NT, Perona JJ. Long-range intramolecular signaling in a tRNA synthetase complex revealed by pre-steady-state kinetics. Proc Natl Acad Sci U S A. 2004 Oct 5 101(40):14396-401. Table - link PubMed ID15452355
|
| Method |
"A highly sensitive and generalizable assay for tRNA aminoacylation
was adapted for rigorous measurement of steady-state and
microscopic rate constants by E. coli GlnRS. The assay is based
on 32P-labeling at the 3'-internucleotide linkage of the tRNA
(ref 18 of primary source)." |
| Comments |
"Under
non-limiting Gln supply, the kinetic parameters of
the aaRS enzyme are kcat=3.20±0.48s^-1 and
Km=0.31±0.09µM (for tRNA) (primary source)" |
| Entered by |
Uri M |
| ID |
109637 |