serine-type exopeptidase activity

Definition

Target type: molecularfunction

Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE, https://www.ebi.ac.uk/merops/about/glossary.shtml#EXOPEPTIDASE]

Serine-type exopeptidases are a class of enzymes that catalyze the hydrolysis of peptide bonds at the N-terminus of peptides or proteins. They are characterized by their active site, which contains a catalytic triad consisting of serine, histidine, and aspartate residues. This triad facilitates the removal of a single amino acid residue from the N-terminus of the peptide chain. The reaction mechanism involves the formation of a covalent intermediate between the serine residue and the carbonyl group of the peptide bond. This intermediate is then hydrolyzed, releasing the N-terminal amino acid and regenerating the enzyme. Serine-type exopeptidases are widely distributed in nature and are involved in a variety of cellular processes, including protein degradation, peptide processing, and signal transduction. They play important roles in regulating protein turnover, controlling cell growth and differentiation, and mediating immune responses. Examples of serine-type exopeptidases include aminopeptidases, carboxypeptidases, and dipeptidyl peptidases. They can exhibit different substrate specificities, depending on the residues surrounding the active site. For instance, some exopeptidases prefer to cleave peptides with specific amino acid residues at the N-terminus, while others are more promiscuous and can act on a broader range of substrates.'
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Proteins (2)

Compounds (21)