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Literature summary for 3.2.1.8 extracted from

  • Kvesitadze, E.; Lomitashvili, T.; Khutsishvili, M.; Lamed, R.; Bayer, E.
    Isolation and properties of a thermostable endoglucanase from a thermophilic mutant strain of Thielavia terrestris (1995), Appl. Biochem. Biotechnol., 50, 137-143 .
No PubMed abstract available
Search for more literature for 3.2.1.8

Organism

Organism UniProt Comment Textmining
Thermothielavioides terrestris
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2500
-
 pH not specified in the publication, temperature not specified in the publication Thermothielavioides terrestris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
larch xylan + H2O
-
 Thermothielavioides terrestris ?
-
 ?
additional information enzyme exhibits both endoglucanase and xylanase activites, reactions of EC 3.2.1.4 and 3.2.1.8, respectively Thermothielavioides terrestris ?
-
 ?

Subunits

Subunits Comment Organism
? x * 69000, SDS-PAGE Thermothielavioides terrestris

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
 6 h, 80% residual activity Thermothielavioides terrestris

pI Value

Organism Comment pI Value Maximum pI Value
Thermothielavioides terrestris isoelectric focusing
-
 6.4