A kinetic analysis of the interaction of elongation factor Tu with guanosine nucleotides and elongation factor Ts.
作者： J F Eccleston
DOI: 10.1016/S0021-9258(18)90646-0
关键词:
摘要: The interaction of elongation factor Tu (EF-Tu) and Ts (EF-Ts) from Escherichia coli has been investigated by kinetic methods. It was found that EF-Ts purified on an EF-Tu affinity column contained a transphosphorylase activity which could transfer the gamma-phosphate GTP to [3H]GDP. However, this showed different sensitivities heat N-ethylmaleimide compared activity. Using chromophoric GDP analogue, 2-amino-6-mercaptopurine riboside 5'-diphosphate (thioGDP), spectrophotometric titrations stopped-flow experiments enabled X thioGDP with be investigated. results were analyzed according scheme Chau et al. (Chau, V., Romero, G., Biltonen, R.L. (1981) J. Biol. Chem. 256, 5591-5596). (Formula: see text) Values for rate constants obtained k1 greater than or equal 2 10(8) M-1 s-1, k-1 2600 k2 = 500 k-2 4 10(5) s-1. most notable feature these is binds at approaching expected diffusion-controlled reaction whereas several orders magnitude more slowly this. relevance interactions involving discussed.
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