Amino acid sequence and thermostability of xylanase A from Schizophyllum commune

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DOIResolve DOI: http://doi.org/10.1016/0014-5793(93)80698-T
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TypeArticle
Journal titleFEBS Letters
Volume334
Issue3
Pages296300; # of pages: 5
AbstractThe 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 involvement in catalysis. The disulfide bond in xylanase A is not conserved in this family. In spite of this, the B. subtilis xylanase was found to be more thermostable than xylanase A.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada; NRC Institute for Biological Sciences
Peer reviewedYes
NRC numberOKU1993
NPARC number9365313
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Record identifierfb3363e0-26bc-45d1-8731-2cc4a864e351
Record created2009-07-10
Record modified2016-05-09
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