Amino acid sequence and thermostability of xylanase A from Schizophyllum commune.
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.
Oku
T
T
Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ont.
Roy
C
C
Watson
D C
DC
Wakarchuk
W
W
Campbell
R
R
Yaguchi
M
M
Jurasek
L
L
Paice
M G
MG
D000595:Amino Acid Sequence; D005075:Biological Evolution; D004220:Disulfides / Q000737:chemistry; D043364:Endo-1,4-beta Xylanases; D004795:Enzyme Stability; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D012567:Schizophyllum / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid; D013696:Temperature
D004220:Disulfides; D006026:Glycoside Hydrolases; D043364:Endo-1,4-beta Xylanases