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Chapter 11: Q26 P (page 359)

Predict the effect on lysozyme’s 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

Explain why lysozyme cleaves the artificial substrate NAG4~4000fourtimes more slowly than it cleavesNAG6 .

Draw a transition state diagram of (a) a non-enzymatic reaction and the corresponding enzyme-catalysed reaction in which (b) S binds loosely to the enzyme and (c) S binds very tightly to the enzyme. Compare ΔG‡ for each case. Why is tight binding of S not advantageous?

Using the reaction shown in Box 11-1 (the attack of an amine on thecarbonyl group of a ketone) as a starting point, draw curved arrows torepresent the acid-catalyzed reaction (when the group —A—H is present).

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

What are the advantages of synthesizing proteases as zymogens?
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