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Literature summary extracted from

  • Fenel, F.; Zitting, A.; Kantelinen, A.
    Increased alkali stability in Trichoderma reesei endo-1,4-beta-xylanase II by site directed mutagenesis (2006), J. Biotechnol., 121, 102-107.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.8 F180Q/H144C/N92C increased resistance towards thermal inactivation at alkaline pH Trichoderma reesei
3.2.1.8 H144C/N92C increased resistance towards thermal inactivation at alkaline pH Trichoderma reesei
3.2.1.8 H22K/F180Q/H144C/N92C increased resistance towards thermal inactivation at alkaline pH Trichoderma reesei
3.2.1.8 N97R/F93W/H144K increased resistance towards thermal inactivation at alkaline pH Trichoderma reesei

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.8 Trichoderma reesei P36217
-
-

Substrates and Products (Substrate)

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

Synonyms

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.8 5 5.5
-
Trichoderma reesei

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.8 Trichoderma reesei isoelectric focusing
-
9