exopeptidázokkal

Exopeptidases are a group of enzymes that catalyze the hydrolysis of peptide bonds at the terminal ends of proteins and peptides. Unlike endopeptidases, which cleave peptide bonds within a polypeptide chain, exopeptidases act on the free amino or carboxyl termini. This action results in the stepwise removal of single amino acids from the peptide chain.

There are two main classes of exopeptidases: aminopeptidases and carboxypeptidases. Aminopeptidases cleave peptide bonds adjacent to the free amino terminus of a polypeptide, releasing amino acids one by one from the N-terminus. Carboxypeptidases, conversely, cleave peptide bonds adjacent to the free carboxyl terminus, removing amino acids from the C-terminus. Both classes play crucial roles in protein metabolism, digestion, and cellular regulation.

In the digestive system, exopeptidases, along with endopeptidases, are essential for breaking down dietary proteins into absorbable amino acids and small peptides. In cells, they are involved in protein turnover, the degradation of damaged or misfolded proteins, and the generation of signaling peptides. The specific activity and substrate specificity of different exopeptidases vary, allowing for precise control over protein breakdown and amino acid availability. Their activity is often tightly regulated to prevent uncontrolled protein degradation.