seriinkarboksüpeptidaases

Serine carboxypeptidases are a class of enzymes that catalyze the hydrolysis of the peptide bond at the carboxyl terminus of a peptide or protein. They belong to the serine hydrolase superfamily, characterized by a catalytic triad consisting of serine, aspartate, and histidine residues. This triad functions to activate the serine residue for nucleophilic attack on the peptide bond. Serine carboxypeptidases are found in a wide range of organisms, from bacteria and fungi to plants and animals, and play diverse biological roles.

In plants, serine carboxypeptidases are involved in various processes including seed germination, protein turnover, and defense against pathogens. For instance, they can be crucial for mobilizing stored proteins during germination to provide amino acids for seedling growth. Some plant serine carboxypeptidases have also been implicated in programmed cell death pathways. In animals, serine carboxypeptidases contribute to protein degradation and remodeling. They are known to be involved in the processing of prohormones and neuropeptides, as well as in the activation and inactivation of various signaling molecules.

The specific substrate preference and localization of serine carboxypeptidases vary depending on the particular enzyme. Some are soluble, while others are membrane-bound. Their activity can be regulated by endogenous inhibitors or by post-translational modifications. Research into serine carboxypeptidases continues to uncover their importance in maintaining cellular homeostasis and their involvement in various physiological and pathological conditions.