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Literature summary extracted from

  • Kovacs, A.; Szabo, L.; Longstaff, C.; Tenekedjiev, K.; Machovich, R.; Kolev, K.
    Ambivalent roles of carboxypeptidase B in the lytic susceptibility of fibrin (2014), Thromb. Res., 133, 80-87.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.17.2 Fibrin + H2O Sus scrofa CPB activity generates fine-mesh fibrin which is more difficult to lyse by tPA ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.17.2 Sus scrofa
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.17.2 Fibrin + H2O CPB activity generates fine-mesh fibrin which is more difficult to lyse by tPA Sus scrofa ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.17.2 carboxypeptidase B
-
 Sus scrofa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.17.2 37
-
 assay at Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.17.2 7.4
-
 assay at Sus scrofa

General Information

EC Number General Information Comment Organism
3.4.17.2 metabolism CPB activity generates fine-mesh fibrin which is more difficult to lyse by tPA but conversely, CPB and plasmin together can stimulate fibrinolysis Sus scrofa