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Literature summary extracted from

  • Kido, H.; Fukusen, N.; Katunuma, N.
    Chymotrypsin- and trypsin-type serine proteases in rat mast cells: properties and functions (1985), Arch. Biochem. Biophys., 239, 436-443.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.39 alpha1-Aantichymotrypsin
-
 Rattus norvegicus
3.4.21.39 alpha1-antitrypsin
-
 Rattus norvegicus
3.4.21.39 antipain
-
 Rattus norvegicus
3.4.21.39 Aprotinin
-
 Rattus norvegicus
3.4.21.39 bestatin
-
 Rattus norvegicus
3.4.21.39 decanoyl lysophosphatidic acid
-
 Rattus norvegicus
3.4.21.39 diisopropyl fluorophosphate
-
 Rattus norvegicus
3.4.21.39 dilauroyl phosphatidic acid
-
 Rattus norvegicus
3.4.21.39 dioleoyl phosphatidic acid
-
 Rattus norvegicus
3.4.21.39 dipalmitoyl phosphatidic acid
-
 Rattus norvegicus
3.4.21.39 distearoyl phosphatidic acid
-
 Rattus norvegicus
3.4.21.39 elaidic acid
-
 Rattus norvegicus
3.4.21.39 linoleic acid
-
 Rattus norvegicus
3.4.21.39 linolenic acid
-
 Rattus norvegicus
3.4.21.39 oleamide
-
 Rattus norvegicus
3.4.21.39 oleic acid
-
 Rattus norvegicus
3.4.21.39 oleoyl lysophosphatidic acid
-
 Rattus norvegicus
3.4.21.39 palmitoyl lysophosphatidic acid
-
 Rattus norvegicus
3.4.21.39 phosphatidic acid from bovine brain Rattus norvegicus
3.4.21.39 phosphatidylethanolamine
-
 Rattus norvegicus
3.4.21.39 phosphatidylinositol
-
 Rattus norvegicus
3.4.21.39 phosphatidylserine
-
 Rattus norvegicus
3.4.21.39 Soybean trypsin inhibitor
-
 Rattus norvegicus
3.4.21.39 stearic acid
-
 Rattus norvegicus
3.4.21.59 alpha1-antitrypsin
-
 Rattus norvegicus
3.4.21.59 antipain
-
 Rattus norvegicus
3.4.21.59 Aprotinin
-
 Rattus norvegicus
3.4.21.59 diisopropyl fluorophosphate
-
 Rattus norvegicus
3.4.21.59 leupeptin
-
 Rattus norvegicus
3.4.21.59 Soybean trypsin inhibitor
-
 Rattus norvegicus
3.4.21.59 Trypstatin inhibition above pH 7.5 Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.59 mast cell granule
-
 Rattus norvegicus 42629
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.59 CaCl2 tryptase free from trypstatin is activated by 10 mM CaCl2, but tryptase associated with trypstatin is not Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.59 additional information
-
 MW of the complex of tryptase and trypstatin: 144000, rat, gel filtration, MW of trypstatin is 7600 on gel filtration Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.39 additional information Rattus norvegicus the enzyme plays a crucial or significant role in the process of degranulation ?
-
 ?
3.4.21.59 additional information Rattus norvegicus enzyme plays a crucial role in the process of degranulation ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.39 Rattus norvegicus
-
-
-
3.4.21.59 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.39
-
 Rattus norvegicus
3.4.21.59 with an associated protein (trypstatin) that inhibits the protease activity above pH 7.5 (enzyme from peritoneal mast cells) Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.39 mast cell
-
 Rattus norvegicus
-
3.4.21.39 peritoneum
-
 Rattus norvegicus
-
3.4.21.59 mast cell peritoneal Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.39 benzoyl-Arg-4-methylcoumarin 7-amide + H2O 1.2% of the activity with succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin 7-amide Rattus norvegicus benzoyl-Arg + 4-methylcoumarin 7-amide
-
 ?
3.4.21.39 additional information the enzyme plays a crucial or significant role in the process of degranulation Rattus norvegicus ?
-
 ?
3.4.21.39 Pro-Phe-Arg-4-methylcoumarin 7-amide + H2O 4.6% of the activity with succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin 7-amide Rattus norvegicus ?
-
 ?
3.4.21.39 Succinyl-Ala-Ala-Pro-Phe-4-methylcoumarin 7-amide + H2O 26.6% of the activity with succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin 7-amide Rattus norvegicus ?
-
 ?
3.4.21.39 succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin 7-amide + H2O
-
 Rattus norvegicus ?
-
 ?
3.4.21.39 t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarin 7-amide + H2O 2.6% of the activity with succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin 7-amide Rattus norvegicus ?
-
 ?
3.4.21.59 additional information enzyme plays a crucial role in the process of degranulation Rattus norvegicus ?
-
 ?
3.4.21.59 N-tert-Butyloxycarbonyl-Ile-Glu-Gly-Arg 4-methylcoumarin 7-amide + H2O rapid hydrolysis by free enzyme, scarcely hydrolyzed by the enzyme associated with trypstatin Rattus norvegicus N-tert-Butyloxycarbonyl-Ile-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
 ?
3.4.21.59 N-tert-Butyloxycarbonyl-Phe-Ser-Arg 4-methylcoumarin 7-amide + H2O
-
 Rattus norvegicus N-tert-Butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
 ?
3.4.21.59 N-tert-Butyloxycarbonyl-Val-Pro-Arg 4-methylcoumarin 7-amide + H2O
-
 Rattus norvegicus N-tert-Butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.59 7.5
-
 tryptase associated with trypstatin Rattus norvegicus
3.4.21.59 8.5
-
 tryptase free of trypstatin Rattus norvegicus