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  • Title: Kinetic parameters governing the formation of eIF-2.methionyl-tRNAi complexes in protein synthesis.
    Author: Manchester KL, Stasikowski P.
    Journal: Biochem Int; 1990; 20(2):257-65. PubMed ID: 2317212.
    Abstract:
    Published data have been analysed to determine the rate constants governing the exchange of GDP in the complex of the eukaryotic protein synthesis initiation factor eIF-2 with GDP, catalysed by eIF-2B. The interaction of eIF-2B with eIF-2.GDP appears to include a very high 'on' rate constant of up to 4 x 10(8) M-1 sec-1 - a value very similar to that found by others for the interaction of the bacterial elongation factors Tu and Ts. Assuming a substituted enzyme mechanism that leads to displacement of GDP and ultimately to formation of a quaternary complex eIF-2B.eIF-2.GTP.methionyl-tRNA, minimum rate constants have been estimated for the additional reactions assuming in vivo rates of protein synthesis. Rate constants for the other reactions are unexceptional.
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