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Literature summary for 3.4.24.72 extracted from

  • Meshram, V.; Saxena, S.; Paul, K.; Gupta, M.; Kapoor, N.
    Production, purification and characterisation of a potential fibrinolytic protease from endophytic Xylaria curta by solid substrate fermentation (2017), Appl. Biochem. Biotechnol., 181, 1496-1512 .
    View publication on PubMed
Search for more literature for 3.4.24.72

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol about 65% residual activity at 2 mM Xylaria curta
Al3+ about 80% residual activity at 2 mM Xylaria curta
Co2+ about 80% residual activity at 2 mM Xylaria curta
Cu2+ about 55% residual activity at 2 mM Xylaria curta
EDTA complete inhibition at 2 mM Xylaria curta
EGTA complete inhibition at 2 mM Xylaria curta
Fe2+ complete inhibition at 2 mM Xylaria curta
K+ about 80% residual activity at 2 mM Xylaria curta
leupeptin about 75% residual activity at 2 mM Xylaria curta
Mg2+ about 75% residual activity at 2 mM Xylaria curta
Mn2+ about 70% residual activity at 2 mM Xylaria curta
Na+ about 85% residual activity at 2 mM Xylaria curta
phenylmethylsulfonyl fluoride about 70% residual activity at 2 mM Xylaria curta
tosyl-phenylalanine chloromethyl ketone about 80% residual activity at 2 mM Xylaria curta
Zn2+ complete inhibition at 2 mM Xylaria curta

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.3266
-
 azocasein at pH 7.8 and 37°C Xylaria curta

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ about 105% activity at 2 mM Xylaria curta

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
fibrinogen + H2O Xylaria curta the enzyme exhibits cleavage of Aalphaand Bbeta chains of fibrin(ogen) and has no effect on gamma chain fibrin + ?
-
 ?

Organism

Organism UniProt Comment Textmining
Xylaria curta
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation and Sephacryl S-300 gel filtration Xylaria curta

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 specific activity of 9.22 units/mg after 8.37fold purification. One unit is defined as the amount of the enzyme producing acid-soluble material from azocasein to cause an increase in absorbance of 0.001 at 660 nm per min Xylaria curta

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
azocasein + H2O
-
 Xylaria curta ?
-
 ?
bovine fibrinogen + H2O
-
 Xylaria curta fibrin + ?
-
 ?
fibrinogen + H2O the enzyme exhibits cleavage of Aalphaand Bbeta chains of fibrin(ogen) and has no effect on gamma chain Xylaria curta fibrin + ?
-
 ?
additional information the enzyme does not display any detectable hydrolysis of gamma chain of fibrin over a period of 180 min Xylaria curta ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 33000, SDS-PAGE Xylaria curta

Synonyms

Synonyms Comment Organism
fibrinolytic protease
-
 Xylaria curta

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
 Xylaria curta

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 55 about 75% activity 25°C, about 80% activity 30°C, 100% activity at 35°C, about 80% activity 40°C, about 60% activity 45°C, about 50% activity 50°C, about 45% activity 55°C. At 60°C, the activity of the enzyme is completely lost Xylaria curta

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 at 60°C, the activity of the enzyme is completely lost Xylaria curta

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Xylaria curta

pH Range

pH Minimum pH Maximum Comment Organism
5 9 more than 60% activity between pH 5.0 and 9.0, about 40% activity at pH 10.0, no activity at pH 4.0 Xylaria curta