Literature summary for 3.4.21.35 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.

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Inhibitors

Inhibitors	Comment	Organism	Structure
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)

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)