serine-type aminopeptidase activity

Definition

Target type: molecularfunction

Catalysis of the hydrolysis of a single N-terminal amino acid residue from 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). [https://www.ebi.ac.uk/merops/about/glossary.shtml#AMINOPEPTIDASE, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE]

Serine-type aminopeptidase activity refers to the enzymatic hydrolysis of peptide bonds at the N-terminus of a polypeptide chain. These enzymes specifically target the amino acid residue at the N-terminal end, cleaving the peptide bond between the first amino acid and the second. Serine-type aminopeptidases are characterized by the presence of a catalytic serine residue within their active site, which plays a crucial role in the hydrolysis reaction. The mechanism of action involves a nucleophilic attack by the activated hydroxyl group of the serine residue on the carbonyl carbon of the peptide bond. This attack leads to the formation of a covalent intermediate between the enzyme and the substrate. Subsequently, water molecules participate in the hydrolysis of the intermediate, releasing the N-terminal amino acid and regenerating the active enzyme. Serine-type aminopeptidases are involved in a wide range of biological processes, including protein processing, degradation, and signaling pathways. They play essential roles in the regulation of cellular function, development, and immune responses. Examples of serine-type aminopeptidases include aminopeptidase N, which is involved in the degradation of extracellular proteins, and dipeptidyl peptidase IV, which plays a role in glucose homeostasis.'
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Proteins (1)

Compounds (9)