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Literature summary extracted from

  • Wang, J.; Chao, J.; Chao, L.
    Purification and characterization of recombinant tissue kallikrein from Escherichia coli and yeast (1991), Biochem. J., 276, 63-71.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.35 expression in Escherichia coli and in yeast Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.35 antipain wild-type and recombinant enzyme Rattus norvegicus
3.4.21.35 Aprotinin wild-type and recombinant enzyme Rattus norvegicus
3.4.21.35 leupeptin wild-type and recombinant enzyme Rattus norvegicus

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 Rattus norvegicus
-
 peptides
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.35 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.35 recombinant enzyme Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.35 kininogen + H2O wild-type and recombinant enzyme Rattus norvegicus kinin + ?
-
 ?
3.4.21.35 low-molecular-weight kininogen + H2O
-
 Rattus norvegicus kallidin + kinin
-
 ?
3.4.21.35 polypeptide + H2O
-
 Rattus norvegicus peptides
-
 ?
3.4.21.35 Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
-
 Rattus norvegicus Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
 ?
3.4.21.35 Tosyl-Arg methyl ester + H2O
-
 Rattus norvegicus Tosyl-Arg + methanol
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.35 9
-
 tosyl-Arg methyl ester hydrolase activity and kininogenase activity of wild-type and recombinant enzyme Rattus norvegicus