Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.17.1 additional information metallocarboxypeptidase Mammalia

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.17.1 36000
-
 x * 36000 Mammalia

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.17.1 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

EC Number Organism UniProt Comment Textmining
3.4.17.1 Mammalia
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.17.1 mast cell
-
 Mammalia
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.17.1 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

EC Number Subunits Comment Organism
3.4.17.1 ? x * 36000 Mammalia

Synonyms

EC Number Synonyms Comment Organism
3.4.17.1 mast cell-CPA
-
 Mammalia
3.4.17.1 MC-CPA
-
 Mammalia
3.4.17.1 additional information the enzyme belongs to the metallocarboxypeptidase Mammalia

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.17.1 7 9
-
 Mammalia