Karboksüpeptidaase

Karboksüpeptidaase is a type of enzyme that catalyzes the hydrolysis of peptide bonds. Specifically, it cleaves amino acids from the carboxyl-terminus of a peptide chain. This process is essential in various biological functions, including protein degradation and the processing of precursor proteins into their active forms.

These enzymes are broadly classified into two main groups: exopeptidases, which cleave amino acids from the ends of peptide chains, and endopeptidases, which cleave peptide bonds within the chain. Karboksüpeptidaases fall under the exopeptidase category, acting exclusively on the C-terminal end.

The activity of karboksüpeptidaases can be regulated by various factors, including pH, temperature, and the presence of specific activators or inhibitors. They play crucial roles in cellular homeostasis by removing unwanted or damaged proteins. In some cases, they are involved in the activation of peptide hormones or neurotransmitters by processing larger precursor molecules.

Research into karboksüpeptidaases is ongoing, with a focus on their specific mechanisms of action, their roles in health and disease, and their potential as therapeutic targets. Understanding these enzymes contributes to a deeper comprehension of protein metabolism and its implications for various physiological processes.