Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Chen, Y.; Shiota, M.; Ohuchi, M.; Towatari, T.; Tashiro, J.; Murakami, M.; Yano, M.; Yang, B.; Kido, H.
    Mast cell tryptase from pig lungs triggers infection by pneumotropic Sendai and influenza A viruses. Purification and characterization (2000), Eur. J. Biochem., 267, 3189-3197.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.4.21.59 medicine viruses utilizes the enzyme to trigger their infectivity and multiplication in lungs, an inhibitor may regulate the enzyme activity and viral infections in vivo Sus scrofa

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.21.59
-
Sus scrofa

General Stability

EC Number General Stability Organism
3.4.21.59 heparin stabilizes the enzyme, retains about 50% activity in a low-salt solution after 2 h incubation at 25°C Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.59 antipain
-
Sus scrofa
3.4.21.59 Aprotinin
-
Sus scrofa
3.4.21.59 benzamidine
-
Sus scrofa
3.4.21.59 diisopropylfluorophosphate
-
Sus scrofa
3.4.21.59 leupeptin
-
Sus scrofa
3.4.21.59 additional information chymostatin, E64 and pestatin have no effect Sus scrofa
3.4.21.59 mucus protease inhibitor
-
Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.59 mast cell
-
Sus scrofa
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.59 32000
-
4 * 32000, SDS-PAGE Sus scrofa
3.4.21.59 120000
-
gel filtration Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.59 additional information Sus scrofa post-translational proteolytic cleavage of the precursors of the fusion glycoproteins of enveloped RNA viruses is indispensable for their fusion activity and infectivity, enzyme triggers infection by pneumotropic Sendai and influenza A viruses by processing ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.59 Sus scrofa
-
pig
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.21.59 3930
-
-
Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.59 Ac-Ser-Ile-Gln-Ser-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 51.2% Sus scrofa ?
-
?
3.4.21.59 human influenza virus HA + H2O
-
Sus scrofa HA1 + HA2
-
?
3.4.21.59 additional information activity only toward substrates with Arg at the P1 position, only 0.3% and 0.1% activity with t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarin 7-amide and Arg-4-methylcoumarin 7-amide, Suc-Ala-Pro-Ala-4-methylcoumarin 7-amide and Suc-Leu-Leu-Val-Leu-4-methylcoumarin 7-amide are no substrates Sus scrofa ?
-
?
3.4.21.59 additional information post-translational proteolytic cleavage of the precursors of the fusion glycoproteins of enveloped RNA viruses is indispensable for their fusion activity and infectivity, enzyme triggers infection by pneumotropic Sendai and influenza A viruses by processing Sus scrofa ?
-
?
3.4.21.59 Pro-Phe-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 3.9% Sus scrofa ?
-
?
3.4.21.59 t-butyloxycarbonyl-Gln-Ala-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 100% Sus scrofa ?
-
?
3.4.21.59 t-butyloxycarbonyl-Gln-Arg-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 26.0% Sus scrofa ?
-
?
3.4.21.59 t-butyloxycarbonyl-Gln-Gly-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 63.3% Sus scrofa ?
-
?
3.4.21.59 t-butyloxycarbonyl-Glu(OBzl)-Ala-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 67.3% Sus scrofa ?
-
?
3.4.21.59 t-butyloxycarbonyl-Glu(OBzl)-Gly-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 26.3% Sus scrofa ?
-
?
3.4.21.59 t-butyloxycarbonyl-Glu-Lys-Lys-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 1.6% Sus scrofa ?
-
?
3.4.21.59 t-butyloxycarbonyl-Gly-Lys-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 10.9% Sus scrofa ?
-
?
3.4.21.59 t-butyloxycarbonyl-Ile-Glu-Gly-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 3.5% Sus scrofa ?
-
?
3.4.21.59 t-butyloxycarbonyl-Leu-Arg-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 5.9% Sus scrofa ?
-
?
3.4.21.59 t-butyloxycarbonyl-Leu-Gly-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 30.0% Sus scrofa ?
-
?
3.4.21.59 t-butyloxycarbonyl-Leu-Lys-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 14.4% Sus scrofa ?
-
?
3.4.21.59 t-butyloxycarbonyl-Phe-Ser-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 36.3% Sus scrofa ?
-
?
3.4.21.59 t-butyloxycarbonyl-Val-Pro-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 6.1% Sus scrofa ?
-
?

Subunits

EC Number Subunits Comment Organism
3.4.21.59 tetramer 4 * 32000, SDS-PAGE Sus scrofa

Synonyms

EC Number Synonyms Comment Organism
3.4.21.59 Mast cell tryptase
-
Sus scrofa
3.4.21.59 tryptase
-
Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.59 7.5 8
-
Sus scrofa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.21.59 6
-
no activity below Sus scrofa