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Literature summary for 3.4.21.59 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

Application Comment Organism
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)

Crystallization (Comment) Organism
-
Sus scrofa

General Stability

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

Inhibitors

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

Localization

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Sus scrofa
-
pig
-

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ac-Ser-Ile-Gln-Ser-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 51.2% Sus scrofa ?
-
?
human influenza virus HA + H2O
-
Sus scrofa HA1 + HA2
-
?
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 ?
-
?
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 ?
-
?
Pro-Phe-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 3.9% Sus scrofa ?
-
?
t-butyloxycarbonyl-Gln-Ala-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 100% Sus scrofa ?
-
?
t-butyloxycarbonyl-Gln-Arg-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 26.0% Sus scrofa ?
-
?
t-butyloxycarbonyl-Gln-Gly-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 63.3% Sus scrofa ?
-
?
t-butyloxycarbonyl-Glu(OBzl)-Ala-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 67.3% Sus scrofa ?
-
?
t-butyloxycarbonyl-Glu(OBzl)-Gly-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 26.3% Sus scrofa ?
-
?
t-butyloxycarbonyl-Glu-Lys-Lys-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 1.6% Sus scrofa ?
-
?
t-butyloxycarbonyl-Gly-Lys-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 10.9% Sus scrofa ?
-
?
t-butyloxycarbonyl-Ile-Glu-Gly-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 3.5% Sus scrofa ?
-
?
t-butyloxycarbonyl-Leu-Arg-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 5.9% Sus scrofa ?
-
?
t-butyloxycarbonyl-Leu-Gly-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 30.0% Sus scrofa ?
-
?
t-butyloxycarbonyl-Leu-Lys-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 14.4% Sus scrofa ?
-
?
t-butyloxycarbonyl-Phe-Ser-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 36.3% Sus scrofa ?
-
?
t-butyloxycarbonyl-Val-Pro-Arg-4-methyl-coumarin 7-amide + H2O synthetic substrate, relative activity 6.1% Sus scrofa ?
-
?

Subunits

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

Synonyms

Synonyms Comment Organism
Mast cell tryptase
-
Sus scrofa
tryptase
-
Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8
-
Sus scrofa

pH Range

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