Metallocarboxypeptidase D
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.17 Metallocarboxypeptidases > 3.4.17.22 metallocarboxypeptidase D
Metallocarboxypeptidase D is a Co2+-activated zinc metallopeptidase in family M14, inhibited by [(2-guanidinoethyl)sulfanyl]butanedioate, a large 180-kDa molecule because of three copies of the metallopeptidase domain; the Drosophila silver gene product is similar, and it releases C-terminal Arg and Lys from polypeptides. By trimming basic C-terminal residues in the secretory pathway it processes peptide hormones. It appears in viruses and cellular organisms.
Metallocarboxypeptidase D is a Co2+-activated zinc metallopeptidase in family M14, inhibited by [(2-guanidinoethyl)sulfanyl]butanedioate, a large 180-kDa molecule because of three copies of the metallopeptidase domain; the Drosophila silver gene product is similar, and it releases C-terminal Arg and Lys from polypeptides. By trimming basic C-terminal residues in the secretory pathway it processes peptide hormones. It appears in viruses and cellular organisms.
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