Sandbox Reserved 1730
From Proteopedia
| This Sandbox is Reserved from August 30, 2022 through May 31, 2023 for use in the course Biochemistry I taught by Kimberly Lane at the Radford University, Radford, VA, USA. This reservation includes Sandbox Reserved 1730 through Sandbox Reserved 1749. |
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Function
Lysozyme binds to the membrane of bacterial cells and catalyzes the breakdown of those membranes killing the cell. The carbohydrates forming the membranes of the bacteria cells are what keep the cell together and functioning. When lysozyme binds to these membranes it catalyzes the reaction between the membrane and water, breaking the bonds between the carbohydrates and causing the membrane to fall apart. The positive charge of lysozyme is what draws it to the negative charge of the bacterial membrane.
Relevance
Lysozyme (muramidase) is an enzyme that can be found in many biological settings. The enzyme is located in saliva, tears, mucous, and human milk. Lysozyme is also found in large concentrations in egg whites from hens. Lysozyme is stable in typical conditions, thus there is a lot of research and information behind the function and structure of the enzyme.
Lysozyme serves a crucial role in our immune system due to its anti-bacterial properties. The enzyme breaks down the cell membranes of bacterial cells. Lysozyme in a single chain alkaline protein with 129 amino acid residues and four disulfide bonds. It catalyzes the breakdown of β-1,4-glycosidic bonds in the cell membrane of bacterial cells. Lysozyme is also known to have antiviral, antitumor, and anti-inflammatory properties.
Lysozyme is also vital in the understanding of the roles of proteins in diseases and how an organism fends off those diseases. It has been used as a model to understand how enzymes catalyze reactions in the body[1]
