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Literature summary extracted from

  • Bajaj, B.; Singh, S.; Khullar, M.; Singh, K.; Bhardwaj, S.
    Optimization of fibrinolytic protease production from Bacillus subtilis I-2 using agro-residues (2014), Braz. Arch. Biol. Technol., 57, 653-662.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.72 Aprotinin strong inhibition Bacillus subtilis
3.4.24.72 Ca2+ strong inhibition Bacillus subtilis
3.4.24.72 Co2+ strong inhibition Bacillus subtilis
3.4.24.72 Cu2+ strong inhibition Bacillus subtilis
3.4.24.72 EDTA strong inhibition Bacillus subtilis
3.4.24.72 EGTA strong inhibition Bacillus subtilis
3.4.24.72 Fe2+ slight inhibition Bacillus subtilis
3.4.24.72 Mg2+ strong inhibition Bacillus subtilis
3.4.24.72 Mn2+ strong inhibition Bacillus subtilis
3.4.24.72 Zn2+ strong inhibition Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.72 42000
-
 x * 42000, the enzyme exists in three isoforms of 42000, 48000 and 60000 Da, SDS-PAGE Bacillus subtilis
3.4.24.72 48000
-
 x * 48000, the enzyme exists in three isoforms of 42000, 48000 and 60000 Da, SDS-PAGE Bacillus subtilis
3.4.24.72 60000
-
 x * 60000, the enzyme exists in three isoforms of 42000, 48000 and 60000 Da, SDS-PAGE Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.72 fibrinogen + H2O Bacillus subtilis
-
 fibrin + ?
-
 ?
3.4.24.72 fibrinogen + H2O Bacillus subtilis I-2
-
 fibrin + ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.72 Bacillus subtilis
-
-
-
3.4.24.72 Bacillus subtilis I-2
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.72 ammonium sulfate precipitation and DEAE-Sephadex gel filtration Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.72 fibrinogen + H2O
-
 Bacillus subtilis fibrin + ?
-
 ?
3.4.24.72 fibrinogen + H2O
-
 Bacillus subtilis I-2 fibrin + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.72 ? x * 42000, the enzyme exists in three isoforms of 42000, 48000 and 60000 Da, SDS-PAGE Bacillus subtilis
3.4.24.72 ? x * 48000, the enzyme exists in three isoforms of 42000, 48000 and 60000 Da, SDS-PAGE Bacillus subtilis
3.4.24.72 ? x * 60000, the enzyme exists in three isoforms of 42000, 48000 and 60000 Da, SDS-PAGE Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
3.4.24.72 fibrinolytic protease
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.72 50
-
-
 Bacillus subtilis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.24.72 40 60 considerable activity is observed at 60°C (88.6%) and at 40°C (68.6%) Bacillus subtilis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.24.72 30 50 the enzyme is quite stable at 30-50°C for 60 min, but at 60°C and above activity decreases drastically Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.72 8
-
-
 Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.24.72 5 10 considerable activity is observed at pH 10.0 (84.4%). The enzyme exhibits poorer activity in the acidic pH 5.0-6.0 (53-64%) Bacillus subtilis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.4.24.72 7 10 after 60 min incubation the enzyme possesses remarkable stability at pH 7.0-10.0 (98.5-100%). In the acidic pH (5.0-6.0), the enzyme retains 77 and 85% activity, respectively Bacillus subtilis

Expression

EC Number Organism Comment Expression
3.4.24.72 Bacillus subtilis soybean meal supports maximum protease production, followed by malt extract, cotton cake, gelatin and beef extract up