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Literature summary for 3.2.1.8 extracted from

  • Michaux, C.; Pouyez, J.; Mayard, A.; Vandurm, P.; Housen, I.; Wouters, J.
    Structural insights into the acidophilic pH adaptation of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum (2010), Biochimie, 92, 1407-1415.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene xyl1, expression in Pichia pastoris Acidomyces acidophilus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant XYL1p, hanging drop vapour diffusion method, room temperature, 10 mg/ml protein, from 2 M ammonium sulfate, 100 mM CAPS, pH 10.5, and 200 mM lithium sulfate, X-ray diffraction structure determination and analysis at 1.9 A resolution, modeling Acidomyces acidophilus

Organism

Organism UniProt Comment Textmining
Acidomyces acidophilus Q6VAY1 gene XYL1
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Purification (Commentary)

Purification (Comment) Organism
recombinant XYL1p from Pichia astoris by anion exchange chromatography Acidomyces acidophilus

Subunits

Subunits Comment Organism
More homology modeling, enzyme XYL1p has the overall fold typical to family 11 xylanases, comparison of XYL1 structure with other homologous acidophilic, neutrophilic and alkalophilic xylanases, overview Acidomyces acidophilus

Synonyms

Synonyms Comment Organism
endo-1,4-beta-xylanase
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Acidomyces acidophilus
XYL1p
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Acidomyces acidophilus

General Information

General Information Comment Organism
additional information several sequence and structure modifications appears to be responsible for the acidophilic characteristic of XYL1p 1. The presence of an aspartic acid H bonded to the acid/base catalyst 2. the nature of specifically conserved residues in the active site 3. the negative potential at the surface 4. the decreased number of salt bridges and H bonds in comparison with highly alkaline enzymes Acidomyces acidophilus