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BRENDA support

Literature summary for 3.2.1.8 extracted from

  • Gruber, K.; Klintschar, G.; Hayn, M.; Schlacher, A.; Steiner, W.; Kratky, C.
    Thermophilic xylanase from Thermomyces lanuginosus high-resolution X-ray structure and modeling studies (1998), Biochemistry, 37, 13475-13485 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
to 1.55 A resolution. The central three sugar rings of the substrate are tightly bound, whereas the peripheral ones can assume different orientations and conformations. The thermostability is due to the presence of an extra disulfide bridge, as well as to an increase in the density of charged residues throughout the protein Thermomyces lanuginosus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
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Thermomyces lanuginosus
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Organism

Organism UniProt Comment Textmining
Thermomyces lanuginosus O43097
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