Final answer:
The key residues in the active site of lysozyme are glutamic acid and histidine, making option D the correct answer. These amino acids are particularly well-suited for enzyme catalysis due to their functional properties in the active site of lysozyme.
Step-by-step explanation:
The active site of lysozyme has two key residues that are critical for its enzymatic activity. The correct answer is D. Glutamic acid and histidine. These two amino acids are involved in the catalytic mechanism of lysozyme. The enzymatic activity of lysozyme, like that of other enzymes, depends on its active site, which is a specifically shaped region where substrates bind and reactions take place. Lysozyme's ability to catalyze the hydrolysis of glycosidic bonds in bacterial cell walls is due to the specific interaction of its active site amino acids with its substrate. It should be noted that certain amino acids, including histidine, cysteine, aspartic acid, arginine, and glutamic acid, are frequently found within the active sites of enzymes due to their ability to participate in acid-base and nucleophilic catalysis.