Organic Chemistry
Organic Chemistry
12th Edition
ISBN: 9781118875766
Author: T. W. Graham Solomons, Craig B. Fryhle, Scott A. Snyder
Publisher: WILEY
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Chapter 24, Problem 2LGP
Interpretation Introduction

Interpretation:

Notes for a class presentation on the mechanism of chymotrypsin are to be prepared by considering the role of catalytic triad with regard to acid–base catalysis and the relative propensity of various groups.

Concept introduction:

Pancreatic enzymes involved in the hydrolysis of peptide bonds are generally calledserine proteases because their enzymatic activity involve a serine residue. Chymotrypsin is a pancreatic enzyme that is involved in the hydrolysis of peptide bonds.

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Amylase’ is an enzyme in our saliva that digests the ‘amylose’ protein in mouth. How could you justify the mechanism of enzymatic action using enzyme-catalyzed reaction models?
An enzyme catalyzes the hydrolysis of an ester with a certain activity, but this activity is lost in a 3 M urea solution. What is the most likely explanation for the loss of activity? (A) Urea binds to the active site of the enzyme competitively with the substrate. (B) Urea causes the cleavage of the peptide bonds in the enzyme. (C) Urea causes the enzyme to denature and lose its specific three-dimensional shape. (D) Urea reacts with disulfide bonds in the enzyme.
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