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In site-directed mutagenesis experiments of an enzyme, scientists altered an aspartate residue to glutamate, lysine, phenylalanine, or valine. Which Glutamate Lysine Phenylalanine Valine

In site-directed mutagenesis experiments of an enzyme, scientists altered an aspartate residue to glutamate, lysine, phenylalanine, or valine. Which Glutamate Lysine Phenylalanine Valine

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Which substitution is expected to have the least effect on enzymatic activity?
### Question on Site-Directed Mutagenesis **Description:** In site-directed mutagenesis experiments of an enzyme, scientists altered an aspartate residue to glutamate, lysine, phenylalanine, or valine. Which substitution would most likely disrupt the function of the enzyme? **Options:** - ☐ Glutamate - ☐ Lysine - ☐ Phenylalanine - ☐ Valine **Explanation:** Site-directed mutagenesis is a molecular biology method that is used to make specific and intentional changes to the DNA sequence of a gene and its protein product. In the context of this question, scientists altered a specific amino acid residue, aspartate, to see which changes would most likely disrupt the enzyme's function. **Amino Acid Substitutions:** - **Glutamate**: Similar to aspartate, both are negatively charged at physiological pH. - **Lysine**: Positively charged at physiological pH, significantly different in charge from aspartate. - **Phenylalanine**: Nonpolar and neutral, structurally different as well. - **Valine**: Nonpolar and neutral, smaller side chain compared to aspartate. By understanding the properties of each amino acid, one can predict which substitutions might disrupt enzyme function due to changes in charge, size, or hydrophobicity. ### Educational Focus: This question is aimed at teaching students about the impact of amino acid substitutions on protein function, specifically emphasizing the importance of properties such as charge, size, and polarity in maintaining enzyme functionality.
Transcribed Image Text:### Question on Site-Directed Mutagenesis **Description:** In site-directed mutagenesis experiments of an enzyme, scientists altered an aspartate residue to glutamate, lysine, phenylalanine, or valine. Which substitution would most likely disrupt the function of the enzyme? **Options:** - ☐ Glutamate - ☐ Lysine - ☐ Phenylalanine - ☐ Valine **Explanation:** Site-directed mutagenesis is a molecular biology method that is used to make specific and intentional changes to the DNA sequence of a gene and its protein product. In the context of this question, scientists altered a specific amino acid residue, aspartate, to see which changes would most likely disrupt the enzyme's function. **Amino Acid Substitutions:** - **Glutamate**: Similar to aspartate, both are negatively charged at physiological pH. - **Lysine**: Positively charged at physiological pH, significantly different in charge from aspartate. - **Phenylalanine**: Nonpolar and neutral, structurally different as well. - **Valine**: Nonpolar and neutral, smaller side chain compared to aspartate. By understanding the properties of each amino acid, one can predict which substitutions might disrupt enzyme function due to changes in charge, size, or hydrophobicity. ### Educational Focus: This question is aimed at teaching students about the impact of amino acid substitutions on protein function, specifically emphasizing the importance of properties such as charge, size, and polarity in maintaining enzyme functionality.
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