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Literature summary for 3.4.17.1 extracted from

  • Reznik, S.E.; Fricker, L.D.
    Carboxypeptidases from A to Z: implications in embryonic development and Wnt binding (2001), Cell. Mol. Life Sci., 58, 1790-1804.
    View publication on PubMed
Search for more literature for 3.4.17.1

Metals/Ions

Metals/Ions Comment Organism Structure
additional information metallocarboxypeptidase Mammalia

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36000
-
 x * 36000 Mammalia

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mammalia the enzyme cleaves C-terminal hydrophobic aliphatic and aromatic residues from other peptides and proteins, not of food in contrast to pancreatic CPA1 and CPA2, for destruction, presumably following the action of chymase ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mammalia
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
mast cell
-
 Mammalia
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme cleaves C-terminal hydrophobic aliphatic and aromatic residues from other peptides and proteins, not of food in contrast to pancreatic CPA1 and CPA2, for destruction, presumably following the action of chymase Mammalia ?
-
 ?

Subunits

Subunits Comment Organism
? x * 36000 Mammalia

Synonyms

Synonyms Comment Organism
mast cell-CPA
-
 Mammalia
MC-CPA
-
 Mammalia
More the enzyme belongs to the metallocarboxypeptidase Mammalia

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 9
-
 Mammalia