Lysozyme is an enzyme that defends your body against bacterial invaders in fluids like tears, mucus, breast milk, and saliva. Lysozyme cleaves the peptidoglycan component of the bacterial cell wall, resulting in the death of the bacterium. Peptidoglycan is made of long polysaccharide chains linked to each other by peptides. The active site of lysozyme binds to six sugar residues, labeled A through F, and breaks the β1-4 glycosidic bond between the D and E rings.
Please use picture to draw and show arrows and info on correct structure
The lysozyme peptidoglycan hydrolysis reaction proceeds in two steps. In the first step, the peptidoglycan molecule becomes the catalytic residues of the enzyme are restored. Depicted below are two snapshots of the peptidogÅycan hydrolysis reaction. The drawings show the D ring (left) and E ring (right) sugars bound in the active site of lýsozyme along with the carboxylic acid groups of two catalytically important amino acids. Aspartate (Asp52, indicated by Ri) is positioned below the sugars and glutamic acid (Gu35, indicated by R2) is above. For simplicity, only one pair of electrons is shown on the carboxylate ions. covalently bound to the enzyme. In the second step, a water molecule is consumed and Add 3 curved arrows to show the electron flow in the first step of the reaction, leading to formation of the structures shown to the right (not including H20). Hint: Begin with the nucleophilic attack of Add 3 curved arrows to show the electron flow in the second step of the reaction, which results in the final products and the restoration of the original charge states of the carboxyl groups. Note: The E ring sugar be part of this reaction step. Asp52 on the anomeric carbon atom of the D ring. on the right will not Glu35 R2 Glu35 R2 CH2 OH CH2 OH HO E ring Asp52 Asp52 #Try Againse)Next Exitr O Previous ⧠Give Up & View Solution Explanation
