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Literature summary for 3.4.21.37 extracted from

  • Collins, J.; Szardenings, M.; Maywald, F.; Bl๖cker, H.; Frank, R.; Hecht, H.J.; Vasel, B.; Schomburg, D.; Fink, E.; Fritz, H.
    Human leukocyte elastase inhibitors: designed variants of human pancreatic secretory trypsin inhibitor (hPSTI) (1990), Biol. Chem. Hoppe-Seyler, 371, 29-36.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
pancreatic secretory trypsin inhibitor variants of human secretory trypsin inhibitor are constructed with the aim of producing inhibitors specific for human leukocyte elastase. Models of the human pancreatic secretory trypsin inhibitor/human leukocytic elastase and human pancreatic secretory trypsin inhibitor/chymotrypsin complexes are generated by computer aided protein design and used to plan better human leukocyte elastase inhibitors. The native human pancreatic secretory trypsin inhibitor with Lys in position P1 (amino acid 18) is a highly potent inhibitor for trypsin and completely inactive towards chymotrypsin and elastase like proteinases. Replacing the Lys in P1 by Leu (pancreatic secretory trypsin inhibitor 7) causes a drastic change of the specificity : this variant no longer inhibits trypsin-like enzymes but is an excellent inhibitor of chymotrypsin and human leukocytic elastase Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Source Tissue

Source Tissue Comment Organism Textmining

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information variants of human secretory trypsin inhibitor are constructed with the aim of producing inhibitors specific for human leukocyte elastase. Models of the human pancreatic secretory trypsin inhibitor/human leukocytic elastase and human pancreatic secretory trypsin inhibitor/chymotrypsin complexes are generated by computer aided protein design and used to plan better human leukocyte elastase inhibitors Homo sapiens