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Chapter 11: Q26 P (page 359)

Predict the effect on lysozyme鈥檚 activity of mutating Glu 35 to Asp and Asp 52 to Glu.

Short Answer

Expert verified

The catalytic activity of lysozyme would be lost.

Step by step solution

01

Lysozyme

Animals generate the antimicrobial enzyme lysozyme, also known as muramidase or N-acetylmuramideglycanhydrolase, which is a component of the innate immune system.

02

Explanation of the effect on lysozyme activity

If Glu and Asp were to switch places, lysozyme's catalytic activity would decrease. The pKa of the relevant residues determines the catalysis process, with Glu being protonated and Asp 52 being deprotonated. Due to its slightly higher pKa than aspartic acid, glutamic acid would be protonated in position 52 , preventing it from forming a covalent connection with the oxonium ion during catalysis.

Hence, lysozyme would lose catalytic activity.

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Most popular questions from this chapter

The covalent catalytic mechanism of an enzyme depends on a single active site Cys whose pK is 8. A mutation in a nearby residue alters the microenvironment so that this pK increases to 10. Would the mutation cause the reaction rate to increase or decrease? Explain.

Wolfenden has stated that it is meaningless to distinguish between the 鈥渂inding sites鈥� and the 鈥渃atalytic sites鈥� of enzymes. Explain.

Describe how different enzymes are classified and named?

What are some ways that active site residues can be identified?

What factors influence an enzyme鈥檚 substrate specificity?
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