Final answer:
Lysosomal enzymes have N-linked carbohydrate chains attached to asparagine residues within a specific motif, which are essential for protein stability and function within the acidic lysosomal environment.
Step-by-step explanation:
Lysosomal enzymes possess N-linked carbohydrate chains, which are involved in several cellular processes, including protein stability and cell signaling. These carbohydrate chains are attached enzymatically to the nitrogen atom of the asparagine (Asn) residue in the consensus sequence Asn-X-Ser/Thr, where X can be any amino acid except proline. The addition of these oligosaccharides begins in the rough endoplasmic reticulum and continues through the Golgi apparatus before the final glycoprotein is formed.
The glycosylation process not only increases the stability of the enzymes in plasma but also allows for proper functioning within the acidic environment of the lysosomes. Here, the enzymes are active and play a crucial role in the breakdown of macromolecules, degradation of intracellular and extracellular proteins, and the destruction of pathogens.