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Literature summary for 3.4.24.72 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
Search for more literature for 3.4.24.72

Inhibitors

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis I-2
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
fibrinolytic protease
-
 Bacillus subtilis

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
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

pH Stability pH Stability Maximum Comment Organism
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

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