Carboxypeptidase C
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.16 Serine-type carboxypeptidases > 3.4.16.5 carboxypeptidase C
Carboxypeptidase C is a lysosomal/plant serine carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate and sensitive to thiol-blocking reagents, widely distributed in eukaryotes and the type example of peptidase family S10; it releases a C-terminal amino acid with broad specificity. By trimming C-terminal residues it participates in plant vacuolar and mammalian lysosomal protein turnover. It appears in viruses and cellular organisms.
Carboxypeptidase C is a lysosomal/plant serine carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate and sensitive to thiol-blocking reagents, widely distributed in eukaryotes and the type example of peptidase family S10; it releases a C-terminal amino acid with broad specificity. By trimming C-terminal residues it participates in plant vacuolar and mammalian lysosomal protein turnover. It appears in viruses and cellular organisms.
References:
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