Amino acid sequence and thermostability of xylanase A from Schizophyllum commune.

@article{Oku1993AminoAS,
  title={Amino acid sequence and thermostability of xylanase A from Schizophyllum commune.},
  author={Tadatake Oku and Christian Roy and David C. Watson and Warren W. Wakarchuk and Robert Campbell and Makoto Yaguchi and Lubo Jurasek and Michael G. Paice},
  journal={FEBS letters},
  year={1993},
  volume={334 3},
  pages={296-300}
}
The amino acid sequence (197 residues) of xylanase A from the fungus, Schizophyllum commune, was determined by automated analysis of peptides from proteolytic and acid cleavage. The sequence is similar to two Trichoderma xylanases (approximately 56% identical amino acids), but also shows at least 40% identities with xylanases from Bacillus subtilis, B. pumilus and B. circulans. The conserved regions of the enzyme contain only two glutamic acid residues which implicates their possible… CONTINUE READING