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Literature summary for 3.4.21.7 extracted from

  • Dahiya, M.; Singh, S.; Rajamohan, G.; Sethi, D.; Ashish, D.; Dikshit, K.L.
    Intermolecular interactions in staphylokinase-plasmin(ogen) bimolecular complex: function of His43 and Tyr44 (2011), FEBS Lett., 585, 1814-1820.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
additional information staphylokinase, SAK, forms a 1:1 stoichiometric complex with human plasmin and switches its substrate specificity to generate a plasminogen activator complex with a crucial requirement of a positively charged and an aromatic residue, respectively, at positions 43 and 44, i.e. SAKHis43 and SAKTyr44, for optimal functioning of SAK-Pm activator complex. Role of these residues in making cation-pi and pi-pi interactions with Trp215 of plasmin and thus establishing the crucial intermolecular contacts within the active site cleft of the activator complex for the cofactor activity of staphylokinase. Molecular modeling and structure analysis, overview Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information staphylokinase forms a 1:1 stoichiometric complex with human plasmin and switches its substrate specificity to generate a plasminogen activator complex Homo sapiens ?
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