Examination of the cleavage of the amide substrate shown by chymotrypsin with the use of stopped-flow kinetic methods reveals no burst. The reaction is monitored by noting the color produced by the release of the amino part of the substrate (highlighted in orange). Why is no burst observed with the amide substrate? H3C H₂C ZI 14 ZI The formation of the acyl-enzyme intermediate is slower than the hydrolysis of the acyl-enzyme intermediate. Chymotrypsin can cleave ester substrates, but it cannot cleave amide substrates. Acyl-enzyme intermediate hydrolysis occurs much more slowly than acyl-enzyme intermediate formation. The colored product remains attached to the enzyme after the acyl-enzyme intermediate is hydrolyzed. N

Examination of the cleavage of the amide substrate shown by chymotrypsin with the use of stopped-flow kinetic methods reveals no burst. The reaction is monitored by noting the color produced by the release of the amino part of the substrate (highlighted in orange). Why is no burst observed with the amide substrate? H3C H₂C ZI 14 ZI The formation of the acyl-enzyme intermediate is slower than the hydrolysis of the acyl-enzyme intermediate. Chymotrypsin can cleave ester substrates, but it cannot cleave amide substrates. Acyl-enzyme intermediate hydrolysis occurs much more slowly than acyl-enzyme intermediate formation. The colored product remains attached to the enzyme after the acyl-enzyme intermediate is hydrolyzed. N

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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