Abstract
Acetylcholinesterase (AChE) catalyzes the hydrolysis of its physiological substrate acetylcholine as well as of a number of other acetic acid esters. A key feature of AChE is its speed in cleaving substrates (Rosenberry, 1975a). The second order rate constant for acetylcholine hydrolysis (kcat/Kapp = 2 × 108 M-1s-1) approaches the value expected for a diffusion-controlled reaction. The turnover rate for acetylcholine (kcat = 2 x 104 s-1) is at the upper limit of reactions catalyzed by general acid-base catalysis. Quinn (1987) has noted that an enzyme with such a high catalytic efficiency is likely to have evolved to a point where the free energies of successive transition states are nearly matched and comparable to the diffusional barrier for substrate binding.
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© 1992 Springer Science+Business Media New York
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Haas, R., Adams, E.W., Rosenberry, M.A., Rosenberry, T.L. (1992). Substrate-Selective Inhibition and Peripheral Site Labeling of Acetylcholinesterase by Platinum(Terpyridine)Chloride. In: Shafferman, A., Velan, B. (eds) Multidisciplinary Approaches to Cholinesterase Functions. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3046-6_18
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DOI: https://doi.org/10.1007/978-1-4615-3046-6_18
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