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Literature summary for 3.4.17.2 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)

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
carboxypeptidase B
-
Sus scrofa

Temperature Optimum [°C]

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

pH Optimum

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

General Information

General Information Comment Organism
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