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Literature summary for 3.4.21.73 extracted from

  • Hoyer-Hansen, G.; Ronne, E.; Solberg, H.; Behrendt, N.; Ploug, M.; Lund, L.R.; Ellis, V.; Dano, K.
    Urokinase plasminogen activator cleaves its cell surface receptor releasing the ligand-binding domain (1992), J. Biol. Chem., 267, 18224-18229.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
uPA from Serono and low-molecular weight uPa from Le Petit
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Mammalia
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uPA from Serono and low-molecular weight uPa from Le Petit
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Cellular receptor of urokinase-type plasminogen activator + H2O cleavage between domains 1 and 2 generating a cell-associated variant of the receptor of urokinase-type plasminogen activator without ligand-binding properties, uPA catalyzed cleavage does not require binding of the protease to the receptor through its epidermal growth factor-like receptor-binding domain, low-molecular weight uPA lacking this domain also cleaves the substrate Homo sapiens ?
-
?
plasminogen + H2O
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Homo sapiens plasmin + ?
-
?