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Literature summary for 3.2.1.8 extracted from

  • Turunen, O.; Etuaho, K.; Fenel, F.; Vehmaanpera, J.; Wu, X.; Rouvinen, J.; Leisola, M.
    A combination of weakly stabilizing mutations with a disulfide bridge in the alpha-helix region of Trichoderma reesei endo-1,4-beta-xylanase II increases the thermal stability through synergism (2001), J. Biotechnol., 88, 37-46.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli XL1-Blue Trichoderma reesei

Protein Variants

Protein Variants Comment Organism
additional information increase in thermal stability in the mutants leads to increased pH stability as well, but also to reduced activity at both acidic and alkaline pH levels Trichoderma reesei
N11D site-directed mutagenesis, increase of half-life to about 100 min at 65°C Trichoderma reesei
N38E site-directed mutagenesis, increase of half-life to about 100 min at 65°C Trichoderma reesei
Q162H site-directed mutagenesis, mutation at the C-terminus of the alpha-helix has a stabilizing effect at 55°C, not at 65°C Trichoderma reesei
Q162Y site-directed mutagenesis, mutation at the C-terminus of the alpha-helix has a stabilizing effect at 55°C, not at 65°C Trichoderma reesei
S110C/N154C site-directed mutagenesis, introduction of a disulfide bridge in the alpha-helix of the enzyme leads to increase of the half-life at 65°C from less than 1 min to 14 min Trichoderma reesei
S110C/N154C/Q162H site-directed mutagenesis, mutations lead to increased thermal and pH stability, overview Trichoderma reesei
S110C/N154C/Q162H/N11D site-directed mutagenesis, mutations lead to increased thermal and pH stability, overview Trichoderma reesei
S110C/N154C/Q162H/N11D/N38D site-directed mutagenesis, mutations lead to increased thermal and pH stability, overview Trichoderma reesei
S110C/N154C/Q162Y site-directed mutagenesis, mutations lead to increased thermal and pH stability, overview Trichoderma reesei
S110C/N154C/Q162Y/N11D site-directed mutagenesis, mutations lead to increased thermal and pH stability, overview Trichoderma reesei

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Trichoderma reesei

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25000
-
x * 21000-22000, native wild-type enzyme, SDS-PAGE, x * 25000, recombinant wild-type enzyme, SDS-PAGE Trichoderma reesei

Organism

Organism UniProt Comment Textmining
Trichoderma reesei
-
-
-

Subunits

Subunits Comment Organism
? x * 21000-22000, native wild-type enzyme, SDS-PAGE, x * 25000, recombinant wild-type enzyme, SDS-PAGE Trichoderma reesei

Synonyms

Synonyms Comment Organism
endo-1,4-beta-xylanase II
-
Trichoderma reesei
More enzyme belongs to family 11 Trichoderma reesei
XYNII
-
Trichoderma reesei

Temperature Optimum [°C]

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

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
-
temperature-dependence of activity of wild-type and mutant enzymes Trichoderma reesei

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
half-lives: wild-type enzyme below 1 min, S110C/N154C 14 min, S110C/N154C/Q162H and S110C/N154C/Q162Y 63 min, S110C/N154C/Q162H/N11D 107 min, S110C/N154C/Q162Y/N11D 97 min, S110C/N154C/Q162H/N11D/N38D 112 min Trichoderma reesei
70
-
10 min: inactivation of mutant S110C/N154C, 50-60% remaining activity of mutants S110C/N154C/Q162H/N11D, S110C/N154C/Q162Y/N11D, and S110C/N154C/Q162H/N11D/N38D Trichoderma reesei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 6
-
Trichoderma reesei

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
pH-dependence of activity of wild-type and mutant enzymes Trichoderma reesei