Lysozyme

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Last updated 6:30 PM on 5/8/26
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12 Terms

1
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How is lysozyme example of divergent evolution?

similar to mammalian lactalbumin but lysozyme doesn't have calcium binding site

2
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What does lysozyme do?

destroy bacterial cell walls, hydrolyses beta (1,4) glycosidic linkages of N-acetylmuramic acid-N-acetylglucosamine linkages

3
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What is peptidoglycan structure

6 nag-nam units

4
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When are D-amino acids used in conjunction with L-amino acids?

Pentapeptide attached to NAM in NAM-NAG unit in neisseria meningitis

5
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How does peptidoglycan gram positive and gram-negative structure differ?

gram positive has large peptidoglycan, gram negative has outer membrane therefore an extra periplasmic space and small peptidoglycan

6
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How are Nag-Nam units cleaved?

hydrolysis

7
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What type of mechanism does lysozyme use?

retaining

8
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What is near the active site in lysozyme?

aromatic amino acid

9
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What conformation change is needed for active site?

chair to half-chair to reduce steric clash and make it more likely to cleave

10
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Where is the steric clash in lysozyme?

Between 4th residue C6 and O6

11
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How was mechanism recently discovered for lysozyme?

through fluoride incubation and mutation of Glu to gln

12
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Is there a catalytic intermediate in the cleavage?

yes