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Literature summary extracted from

  • Simon, D.I.; Ezratty, A.M.; Loscalzo, J.
    The fibrin(ogen)olytic properties of cathepsin D (1994), Biochemistry, 33, 6555-6563.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.4.23.5 medicine the enzyme may have important implications in the pathophysiology and treatment of thrombotic disorders Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.23.5 0.0015
-
fibrinogen
-
Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.23.5 additional information Homo sapiens the enzyme may have important implications in the pathophysiology and treatment of thrombotic disorders ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.5 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.23.5 U-937 cell
-
Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.5 Fibrin + H2O
-
Homo sapiens ?
-
?
3.4.23.5 fibrinogen + H2O cleaves the alpha-chain, the beta-chain and the gamma-chain Homo sapiens low molecular weight fragments of fibrinogen
-
?
3.4.23.5 additional information the enzyme may have important implications in the pathophysiology and treatment of thrombotic disorders Homo sapiens ?
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.23.5 0.0014
-
fibrinogen
-
Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.23.5 3.5
-
fibrinogen Homo sapiens

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.23.5 3.5 5 pH 3.5: maximal activity, pH 5.0: about 50% of maximal activity, fibrinogen as substrate Homo sapiens