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Literature summary for 3.4.21.73 extracted from

  • Jendroszek, A.; Madsen, J.; Chana-Munoz, A.; Dupont, D.; Christensen, A.; Panitz, F.; Fuechtbauer, E.; Lovell, S.; Jensen, J.
    Biochemical and structural analyses suggest that plasminogen activators coevolved with their cognate protein substrates and inhibitors (2019), J. Biol. Chem., 294, 3794-3805 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.73

Protein Variants

Protein Variants Comment Organism
L97bG/H99Y/S195A/R217E site-directed mutagenesis, the mutant shows altered interaction with human plasminogen activator inhibitor-1 compare to wild-type Homo sapiens
L97bG/S195A site-directed mutagenesis, the mutant shows altered interaction with human plasminogen activator inhibitor-1 compare to wild-type Homo sapiens
L97bG/S195A/R217E site-directed mutagenesis, the mutant shows altered interaction with human plasminogen activator inhibitor-1 compare to wild-type Homo sapiens
additional information analysis of interaction kinetics of the wild-type and mutant human enzymes with human and zebrafish plasminogen activator inhibitor-1 and of the zebrafish wild-type and mutant enzyme with both inhibitors, overview Homo sapiens
S195A site-directed mutagenesis, the mutant shows altered interaction with human plasminogen activator inhibitor-1 compare to wild-type Homo sapiens
S195A/R217E site-directed mutagenesis, the mutant shows altered interaction with human plasminogen activator inhibitor-1 compare to wild-type Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
human PAI-1 human plasminogen activator inhibitor-1, complex structure of uPA:PAI-1 Michaelis complex, interaction analysis, the S3-pocket-lining residues of uPA and the P3 residue of both PAI-1 and plasminogen form numerous polar interactions in the human uPA:PAI-1 Michaelis complex, overview Homo sapiens
additional information although the interaction areas between protease-substrate and protease-inhibitor are shared, the two interactions are mechanistically different. Species specificity of the reaction of PAI-1 and uPA. Analysis of interaction kinetics of the wild-type and mutant human enzymes with human and zebrafish plasminogen activator inhibitor-1 and of the zebrafish wild-type and mutant enzyme with both inhibitors, overview Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P00749
-
-

Synonyms

Synonyms Comment Organism
uPA
-
 Homo sapiens

General Information

General Information Comment Organism
evolution biochemical and structural analyses suggest that plasminogen activators coevolved with their cognate protein substrates and inhibitors. The binding interfaces of uPA:plasminogen and uPA:PAI-1 may have coevolved to maintain tight interactions Homo sapiens
additional information although the interaction areas between protease-substrate and protease-inhibitor are shared, the two interactions are mechanistically different Homo sapiens