Abstract
The stopped‐flow and temperature‐jump techniques are applied to the study of the relaxations of an allosteric protein, the aspartokinase I‐homoserine dehydrogenase I of E. coli K 12. A concerted conformation change is known to occur in this protein under the influence of aspartate, of the K+ ions and of threonine, all of which are effectors of the catalytic activities. The kinetics of the conformation change can be followed by making use of effects on the ultraviolet absorption and on the fluorescence of the protein itself. Stopped‐flow experiments demonstrate that the relaxation observed after addition of any of the three effectors described is an exponential process, which appears to correspond to the slower of two temperature relaxations. In the absence of added ligands, the rates of these relaxations are approximately 1000 sec–1 and 14 sec–1 at 28°. The effects of the ligands on the processes observed in the stopped‐flow and in the temperature‐jump experiments are interpreted and the mechanism of the conformation change is shown to include at least two isomerization steps.
References
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Dates
Type | When |
---|---|
Created | 20 years, 6 months ago (March 3, 2005, 11:47 a.m.) |
Deposited | 1 year, 11 months ago (Oct. 1, 2023, 2 p.m.) |
Indexed | 1 year, 7 months ago (Jan. 26, 2024, 6:01 p.m.) |
Issued | 55 years, 9 months ago (Dec. 1, 1969) |
Published | 55 years, 9 months ago (Dec. 1, 1969) |
Published Online | 20 years, 6 months ago (March 3, 2005) |
Published Print | 55 years, 9 months ago (Dec. 1, 1969) |
@article{Janin_1969, title={The Threonine‐Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K 12: Relaxations of the Allosteric Equilibrium}, volume={11}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1969.tb00805.x}, DOI={10.1111/j.1432-1033.1969.tb00805.x}, number={3}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={Janin, Joël and Iwatsubo, M.}, year={1969}, month=dec, pages={530–540} }