AMINO-ACID-SEQUENCE AND THERMOSTABILITY OF XYLANASE-A FROM SCHIZOPHYLLUM-COMMUNE

被引:31
作者
OKU, T
ROY, C
WATSON, DC
WAKARCHUK, W
CAMPBELL, R
YAGUCHI, M
JURASEK, L
PAICE, MG
机构
[1] NATL RES COUNCIL CANADA, INST BIOL SCI, 100 SUSSEX DR, OTTAWA K1A 0R6, ONTARIO, CANADA
[2] PULP & PAPER RES INST CANADA, POINTE CLAIRE H9R 3J9, QUEBEC, CANADA
关键词
XYLANASE; BASIDIOMYCETE; HOMOLOGY; BACILLUS;
D O I
10.1016/0014-5793(93)80698-T
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 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.
引用
收藏
页码:296 / 300
页数:5
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