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Literature summary for 3.2.1.8 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

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Niallia circulans P09850
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
Bcx
-
Niallia circulans
xylanase
-
Niallia circulans

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

pH Optimum

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