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Lysozyme is a relatively small (129 AA) enzyme that catalyzes the hydrolysis of specific kinds of polysaccharides comprising the cell walls of bacteria.

In birds, lysozyme is an exceptionally abundant protein in fowl egg whites where it likely functions both as an antibiotic (see below) as well as a nutrient for early embryogenesis. In vertebrates, this "glycosidase" is found mainly in biological secretions (such as tears) where it probably serves as an anti-bacterial agent by digesting and weakening the rigid bacterial cell wall, thereby rendering the bacterial susceptible to osmotic lysis. The effect of lysozyme is similar to the effect of penicillin which also weakens the cell walls of bacteria only by irreversibly inhibiting a transpeptidase enzyme required for crosslinking peptidoglycan macromolecules formed in the biosynthesis of the cell wall. Under normal conditions, bacteria grow very rapidly in some cases doubling more than once in an hour. However, when cell wall crosslinking is disrupted, bacteria tend to lyse in hypotonic media as a result of the mechanical weakening of their cell walls [1]. This is a picture of is one of the key amino acid residue responsible for fluorescence property of HEWL.

References 1. http://mcdb-webarchive.mcdb.ucsb.edu/sears/biochemistry/tw-enz/lysozyme/HEWL/lysozyme-overview.htm ==

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of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

Function

Disease

Relevance

Structural highlights

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