cysteine-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 mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#AMINOPEPTIDASE, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE]

Cysteine-type aminopeptidase activity refers to the enzymatic hydrolysis of peptide bonds at the N-terminus of a polypeptide chain, specifically involving a cysteine residue in the active site. This activity is crucial for a wide range of biological processes, including protein degradation, neuropeptide processing, hormone maturation, and immune response. The catalytic mechanism typically involves the formation of a covalent intermediate between the cysteine residue and the peptide substrate. This intermediate is then hydrolyzed, releasing the N-terminal amino acid and regenerating the active enzyme. Cysteine-type aminopeptidases are highly specific for their substrates and are often regulated by factors such as pH, metal ions, and inhibitors. They play important roles in various cellular compartments, including the cytosol, lysosomes, and the extracellular space.'
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Proteins (1)

Compounds (1)