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Literature summary extracted from

  • Turunen, O.; Vuorio, M.; Fenel, F.; Leisola, M.
    Engineering of multiple arginines into the Ser/Thr surface of Trichoderma reesei endo-1,4-beta-xylanase II increases the thermotolerance and shifts the pH optimum towards alkaline pH (2002), Protein Eng., 15, 141-145.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.8 expression of wild-type and mutant enzymes in Escherichia coli Trichoderma reesei

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.8 K58R site-directed mutagenesis, slight increase of thermostability at 55°C from half-life 5 min, wild-type, to 10-20 min, increased pH-stability compared to the wild-type enzyme Trichoderma reesei
3.2.1.8 K58R/A160R site-directed mutagenesis, no alteration of thermal or pH-stability Trichoderma reesei
3.2.1.8 K58R/A160R/N97R site-directed mutagenesis, no alteration of thermal or pH-stability Trichoderma reesei
3.2.1.8 K58R/A160R/N97R/N67R site-directed mutagenesis, no alteration of thermal or pH-stability Trichoderma reesei
3.2.1.8 K58R/A160R/N97R/N67R/T26R site-directed mutagenesis, no alteration of thermal or pH-stability Trichoderma reesei
3.2.1.8 K58R/A160R/N97R/N67R/T26R/A132R site-directed mutagenesis, no alteration of thermal or pH-stability Trichoderma reesei
3.2.1.8 additional information construction of several mutant with increased number of arginines on the protein surface showing unaltered thermal stability but narrowed pH optimum, mutation of arginines to Ser/Thr causes a pH profile shift Trichoderma reesei
3.2.1.8 S186R site-directed mutagenesis, reduced thermal stability at 50°C in absence of substrate compared to the wild-type enzyme Trichoderma reesei
3.2.1.8 S186R/N67R site-directed mutagenesis, reduced thermal stability at 50°C in absence of substrate compared to the wild-type enzyme Trichoderma reesei
3.2.1.8 S186R/N67R/T26R site-directed mutagenesis, reduced thermal stability at 50°C in absence of substrate, reduced stability at 60°C and unaltered at 65°C in presence of substrate, compared to the wild-type enzyme Trichoderma reesei
3.2.1.8 S186R/N67R/T26R/Q34R site-directed mutagenesis, highly reduced thermal stability at 50°C in absence of substrate, unaltered stability at 60°C and slightly increased at 65°C in presence of substrate, compared to the wild-type enzyme Trichoderma reesei
3.2.1.8 S186R/N67R/T26R/Q34R/N69R site-directed mutagenesis, reduced thermal stability at 50°C in absence of substrate, increased stability at 60°C and 65°C in presence of substrate, compared to the wild-type enzyme Trichoderma reesei
3.2.1.8 S186R/N67R/T26R/Q34R/S40R site-directed mutagenesis, highly reduced thermal stability at 50°C in absence of substrate, highly increased stability at 60°C and increased 65°C in presence of substrate, compared to the wild-type enzyme Trichoderma reesei

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.8 Trichoderma reesei P36218 xylanase II
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.8 xylan + H2O from birchwood Trichoderma reesei ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.8 endo-1,4-beta-xylanase II
-
 Trichoderma reesei
3.2.1.8 XYNII
-
 Trichoderma reesei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.8 50
-
 assay at Trichoderma reesei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.8 5
-
 assay at Trichoderma reesei

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.8 3 7.5
-
 Trichoderma reesei