Lysozyme Structure
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Lysozyme Structure
This video describes the structure of the enzyme, lysozyme.
14.2K viewsMay 27, 2009
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SOLVED: Lysozyme is an enzyme that hydrolyzes linkages between subunits in certain bacterial peptidoglycans. The figure below depicts the chemical enzyme mechanism of lysozyme and the pH dependence of lysozyme function. Use this information to answer the two questions below:The linkage between subunits shown in the reaction above would best be described as: B-1-4 linkages between glucopyranose derivative components.b. The pKa of Glu35 and Asp52 are shifted from the standard values for these side
SOLVED: Lysozyme is an enzyme that hydrolyzes linkages between subunits in certain bacterial peptidoglycans. The figure below depicts the chemical enzyme mechanism of lysozyme and the pH dependence of lysozyme function. Use this information to answer the two questions below:The linkage between subunits shown in the reaction above would best be described as: B-1-4 linkages between glucopyranose derivative components.b. The pKa of Glu35 and Asp52 are shifted from the standard values for these side
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Lysozyme is an enzyme that cleaves bacterial cell walls. A sample of lysozyme extracted from chicken egg white has a molar mass of 13,930  g. A quantity of 0.100  g of this enzyme is dissolved in 150  g of water at 25^∘C. Calculate the vapor-pressure lowering, the depression in freezing point, the elevation in boiling point, and the osmotic pressure of this solution. (The vapor pressure of water at 25^∘C=23.76 mmHg.
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SOLVED: The enzymatic activity of lysozyme is optimal at pH 5.2 anddecreases above and below this pH value. Lysozyme containstwo amino acid residues in the active site essential for catalysis:Glu35 and Asp52. The pK valuefor the carboxyl side chains of these two residues are 5.9 and 4.5,respectively. What is the ionization state of each residue atthe pH optimum of lysozyme? How can the ionization states ofthese two amino acid residues explain the pH-activity profile oflysozyme?
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