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- W2282289538 abstract "We have measured, by permeable membrane/mass spectrometry, the /sup 16/O//sup 18/O, /sup 12/C//sup 13/C, and solvent H/sup 2/O/D/sup 2/O kinetic isotope effects (kie) associated with acyl-alpha-chymotrypsin hydrolysis and transesterification. The hydrolysis of alpha-chymotrypsinyl 2-furoate has a /sup 12/C//sup 13/C kie of approximately 1.06. Transesterification of the same acyl enzyme shows /sup 16/O//sup 18/O, /sup 12/C//sup 13/C, and solvent H/sup 2/O/D/sup 2/O kinetic isotope effects of 1.015 (0.003), 1.01-1.02, and 2.226 (0.007), respectively. From the temperature independence of the /sup 16/O//sup 18/O transesterification kinetic isotope effect and kinetic data reported elsewhere, we conclude that there are two active forms of acylchymotrypsin. We also propose that formation of the tetrahedral intermediate is the rate-limiting step in both hydrolysis and transesterification and that the position of the transition state in the transesterification is closer to the starting enzyme ester while that for the hydrolytic reaction is closer to the tetrahedral intermediate. These results are discussed in terms of reaction mechanism plasticity." @default.
- W2282289538 created "2016-06-24" @default.
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- W2282289538 date "1986-11-18" @default.
- W2282289538 modified "2023-09-22" @default.
- W2282289538 title "Permeable membrane/mass spectrometric measurement of solvent /sup 1/H//sup 2/H, /sup 12/C//sup 13/C, and /sup 16/O//sup 18/O kinetic isotope effects associated with alpha-chymotrypsin deacylation: evidence for reaction mechanism plasticity" @default.
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