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Literature summary extracted from

  • Joo, J.C.; Pohkrel, S.; Pack, S.P.; Yoo, Y.J.
    Thermostabilization of Bacillus circulans xylanase via computational design of a flexible surface cavity (2010), J. Biotechnol., 146, 31-39.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.8 D101N site-directed mutagenesis, deleterious mutation Niallia circulans
3.2.1.8 D101N/G103F/R132A/R136A site-directed mutagenesis, the mutant is expressed in inclusion bodies Niallia circulans
3.2.1.8 F48Y site-directed mutagenesis, the mutant shows increased thermostability and activity compared to the wild-type enzyme Niallia circulans
3.2.1.8 F48Y/R49A/T50V/T147L site-directed mutagenesis, the half-life of the mutant is 4fold increased compared to the wild-type enzyme Niallia circulans
3.2.1.8 F48Y/T147L site-directed mutagenesis, the half-life of the mutant is 7.5fold increased compared to the wild-type enzyme Niallia circulans
3.2.1.8 F48Y/T50V site-directed mutagenesis, the half-life of the mutant is increased compared to the wild-type enzyme Niallia circulans
3.2.1.8 F48Y/T50V/T147L site-directed mutagenesis, the half-life of the mutant is 15fold increased compared to the wild-type enzyme Niallia circulans
3.2.1.8 G103F site-directed mutagenesis, the mutation introduced a bulky hydrophobic residue causing a clash with the neighbouring residues that results in destabilization Niallia circulans
3.2.1.8 R132A site-directed mutagenesis, deleterious mutation Niallia circulans
3.2.1.8 R136A site-directed mutagenesis, deleterious mutation Niallia circulans
3.2.1.8 R49A site-directed mutagenesis, deleterious mutation Niallia circulans
3.2.1.8 T147L site-directed mutagenesis, the mutant shows increased thermostability and activity compared to the wild-type enzyme Niallia circulans
3.2.1.8 T50V site-directed mutagenesis, the mutant shows increased thermostability and activity compared to the wild-type enzyme Niallia circulans
3.2.1.8 T50V/T147L site-directed mutagenesis, the half-life of the mutant is increased compared to the wild-type enzyme Niallia circulans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.8 additional information
-
 additional information kinetics of wild-type and mutant enzymes Niallia circulans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.8 beta-1,4-xylan + H2O Niallia circulans
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.8 Niallia circulans P09850
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.8 beta-1,4-xylan + H2O
-
 Niallia circulans ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.8 Bcx
-
 Niallia circulans
3.2.1.8 xylanase
-
 Niallia circulans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.8 40
-
 assay at Niallia circulans

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.8 additional information
-
 Tm of wild-type and mutant enzymes Niallia circulans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.8 5.5
-
 assay at Niallia circulans