Chemistry
Chemistry
10th Edition
ISBN: 9781305957404
Author: Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher: Cengage Learning
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G.293.

 

Which of these amino acid side chains would be effective at carrying out covalent
catalysis in an enzyme-catalyzed reaction at pH 7.4? Assume that if more than 10%
of the side chain can act as a strong nucleophile, then there will be a sufficient
amount of nucleophile available for the enzyme to perform covalent catalysis.
Please select all possible answers.
Lysine side chain with pKa = 9.0, where the positively charged state is
destabilized by a nearby arginine side chain
Glutamate side chain with pKa = 6.5, where the negatively charged state is
destabilized due to the presence of a nearby Asp de chain
Histidine side chain with pKa = 5.5, where the positively charged state is
stabilized due to the presence of a nearby Asp side chain
Alanine side chain
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Transcribed Image Text:Which of these amino acid side chains would be effective at carrying out covalent catalysis in an enzyme-catalyzed reaction at pH 7.4? Assume that if more than 10% of the side chain can act as a strong nucleophile, then there will be a sufficient amount of nucleophile available for the enzyme to perform covalent catalysis. Please select all possible answers. Lysine side chain with pKa = 9.0, where the positively charged state is destabilized by a nearby arginine side chain Glutamate side chain with pKa = 6.5, where the negatively charged state is destabilized due to the presence of a nearby Asp de chain Histidine side chain with pKa = 5.5, where the positively charged state is stabilized due to the presence of a nearby Asp side chain Alanine side chain
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