Carboxypeptidase D
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.16 Serine-type carboxypeptidases > 3.4.16.6 carboxypeptidase D
Carboxypeptidase D is a serine carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate and sensitive to thiol-blocking reagents, in peptidase family S10 (carboxypeptidase C family); it preferentially releases a C-terminal arginine or lysine residue. By removing basic C-terminal residues it participates in secretory-pathway peptide processing. It appears in viruses and cellular organisms.
Carboxypeptidase D is a serine carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate and sensitive to thiol-blocking reagents, in peptidase family S10 (carboxypeptidase C family); it preferentially releases a C-terminal arginine or lysine residue. By removing basic C-terminal residues it participates in secretory-pathway peptide processing. It appears in viruses and cellular organisms.
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