Lysozyme: Difference between revisions
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File:Lysozymecrystals1.png|Lysozyme crystals | |||
File:Mecanism_of_action_for_Lysozyme.svg|Mechanism of action for Lysozyme | |||
File:Lysozyme_glycosyl_covalent_intermediate.gif|Lysozyme glycosyl covalent intermediate | |||
File:LysozymeIntermediates_copy.png|Lysozyme intermediates | |||
File:JBSlysozymemechanism_copy2.jpg|Lysozyme mechanism | |||
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Latest revision as of 04:44, 18 February 2025
Lysozyme is an enzyme that is capable of breaking down the cell walls of certain bacteria, making it an important part of the immune system. It was discovered in 1922 by Alexander Fleming, who also discovered penicillin.
Structure[edit]
Lysozyme is a small protein of 129 amino acids and has a molecular weight of approximately 14.3 kDa. It has a compact, globular structure, and is stabilized by four disulfide bridges.
Function[edit]
Lysozyme functions by hydrolyzing the 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan, which is the major component of gram-positive bacterial cell wall. This hydrolysis leads to the rupture of the bacterial cell wall and subsequent cell death.
Clinical significance[edit]
Lysozyme has been used in the food industry as a preservative and in medicine as an antibiotic. It is also being studied for its potential use in treating HIV and cancer.


