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Literature summary for 3.4.24.72 extracted from

  • Taneja, K.; Bajaj, B.; Kumar, S.; Dilbaghi, N.
    Production, purification and characterization of fibrinolytic enzyme from Serratia sp. KG-2-1 using optimized media (2017), 3 Biotech, 7, 184 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.72

Activating Compound

Activating Compound Comment Organism Structure
acetic acid about 200% activity at 2 mM Serratia sp. KG-2-1
acetone about 310% activity at 2 mM Serratia sp. KG-2-1
DMSO about 140% activity at 2 mM Serratia sp. KG-2-1
glycerol about 170% activity at 2 mM Serratia sp. KG-2-1
Isopropanol about 140% activity at 2 mM Serratia sp. KG-2-1
SDS about 250% activity at 2 mM Serratia sp. KG-2-1
Tween 20 about 240% activity at 2 mM Serratia sp. KG-2-1

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline 17.48% residual activity at 2 mM Serratia sp. KG-2-1
2-mercaptoethanol about 10% residual activity at 2 mM Serratia sp. KG-2-1
acetaldehyde about 3% activity at 2 mM Serratia sp. KG-2-1
Al3+ about 65% residual activity at 2 mM Serratia sp. KG-2-1
Ca2+ about 30% residual activity at 2 mM Serratia sp. KG-2-1
CTAB about 75% residual activity at 2 mM Serratia sp. KG-2-1
EDTA 16.51% residual activity at 2 mM Serratia sp. KG-2-1
ethanol about 90% residual activity at 2 mM Serratia sp. KG-2-1
Fe3+ about 40% residual activity at 2 mM Serratia sp. KG-2-1
Glutaraldehyde about 5% residual activity at 2 mM Serratia sp. KG-2-1
iodoacetate 17.08% residual activity at 2 mM Serratia sp. KG-2-1
methanol about 95% residual activity at 2 mM Serratia sp. KG-2-1
Mg2+ about 70% residual activity at 2 mM Serratia sp. KG-2-1
n-butanol about 75% residual activity at 2 mM Serratia sp. KG-2-1
phenylmethyl sulfonyl fluoride about 90% residual activity at 2 mM Serratia sp. KG-2-1
Zn2+ about 80% residual activity at 2 mM Serratia sp. KG-2-1

Metals/Ions

Metals/Ions Comment Organism Structure
Ba2+ about 170% activity at 2 mM Serratia sp. KG-2-1
Cu2+ about 110% activity at 2 mM Serratia sp. KG-2-1
Hg2+ about 150% activity at 2 mM Serratia sp. KG-2-1
K+ about 125% activity at 2 mM Serratia sp. KG-2-1
Mn2+ about 140% activity at 2 mM Serratia sp. KG-2-1
Na+ about 125% activity at 2 mM Serratia sp. KG-2-1

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
fibrinogen + H2O Serratia sp. KG-2-1
-
 fibrin + ?
-
 ?
low molecular weight kininogen + H2O Serratia sp. KG-2-1
-
 kallidin + ?
-
 ?

Organism

Organism UniProt Comment Textmining
Serratia sp. KG-2-1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation and DEAE-Sephadex gel filtration Serratia sp. KG-2-1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
fibrinogen + H2O
-
 Serratia sp. KG-2-1 fibrin + ?
-
 ?
low molecular weight kininogen + H2O
-
 Serratia sp. KG-2-1 kallidin + ?
-
 ?

Subunits

Subunits Comment Organism
? x * 52000, SDS-PAGE Serratia sp. KG-2-1

Synonyms

Synonyms Comment Organism
fibrinolytic protease
-
 Serratia sp. KG-2-1

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
 Serratia sp. KG-2-1

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
50 60 maximum enzyme activity at 40°C (100%) then decreases gradually with relative activity of 69.28 and 67.75% at 50 and 60°C, respectively Serratia sp. KG-2-1

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
10 30 the enzyme shows relatively high stability between 10-30°C retaining 94.87, 94.83 and 99.79% of activity at respective temperatures while at higher temperature activity decreases Serratia sp. KG-2-1

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Serratia sp. KG-2-1

pH Range

pH Minimum pH Maximum Comment Organism
7 10 highly active between pH 7.0 and 10.0 Serratia sp. KG-2-1

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 12 the purified enzyme shows higher stability between pH 6.0-8.0 retaining more than 90% of its activity while it retains 87.22 and 74.23% of its activity at pH 5.0 and 9.0, respectively. With further increase in pH 18% residual activity is observed at pH 12.0 Serratia sp. KG-2-1