Km[GTP] for Protein synthesis rate

Value 14 µM Range: ±2 µM
Organism Bacteria Escherichia coli
Reference Jewett MC, Miller ML, Chen Y, Swartz JR. Continued protein synthesis at low [ATP] and [GTP] enables cell adaptation during energy limitation.J Bacteriol. 2009 Feb191(3):1083-91PubMed ID19028899
Method To measure the dependence of the protein synthesis rate on [ATP] and [GTP], researchers used an in vitro cell-free system derived from E. coli extracts. Cell-free systems provide the opportunity to directly monitor, add, and remove components with much greater ease and accuracy than can be done with in vivo systems.
Comments Researchers used an integrated Escherichia coli cell-free platform that mimics the intracellular, energy-limited environment to show that protein synthesis rates are governed by simple Michaelis-Menten dependence on [ATP] and [GTP] (K(m)(ATP), 27 +/- 4 microM, BNID (104731) K(m)(GTP), 14 +/- 2 microM). Although the ATP concentration is probably the single most important parameter influencing the entire protein synthesis system, GTP is required for translation initiation, for elongation, and for termination.
Entered by Uri M
ID 104732