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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


Many of the cell鈥檚 hydrolytic enzymes are located in the lysosome, where the pH is 鈭�5. What would you expect to be the optimum pH for these enzymes, and why would this protect the rest of the cell from the destructive power of these enzymes upon the accidental rupture of a lysosome?

What roles do proximity and orientation play in enzymatic catalysis?

Lysozyme residues Asp 101 and Arg 114 are required for efficient catalysis, although they are located some distance from the active sites Glu 35 and Asp 52. Substituting Ala for either Asp 101 or Arg 114 does not significantly alter the enzyme鈥檚 tertiary structure, but it significantly reduces its catalytic activity. Explain.

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 螖G鈥� for each case. Why is tight binding of S not advantageous?

What role do low-barrier hydrogen bonds play in serine protease catalysis?
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