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Literature summary extracted from

  • Chen, V.C.; Chao, L.; Chao, J.
    A positively charged loop on the surface of kallistatin functions to enhance tissue kallikrein inhibition by acting as a secondary binding site for kallikrein (2000), J. Biol. Chem., 275, 40371-40377.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.35 kallistatin complex formation, highly specific; inhibitor protein mutants with amino acid substitutions of basic residues at a heparin binding site, which is essential for inhibition of kallikrein; positively charged loop on the surface of kallistatin enhances inhibition of tissue kallikrein by acting as a secondary binding site for kallikrein, model, chimeric mutants; serine protease inhibitor, i.e. serpin, with unique P1 Phe Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.35 polypeptide + H2O Homo sapiens
-
peptides
-
?

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.35 D-Val-Leu-Arg-p-nitroanilide + H2O
-
Homo sapiens D-Val-Leu-Arg + p-nitroaniline
-
?
3.4.21.35 polypeptide + H2O
-
Homo sapiens peptides
-
?