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Amino acid sequence similarities between low molecular weight endo‐1,4‐β‐xylanases and family H cellulases revealed by clustering analysis
Author(s) -
Törrönen Anneli,
Kubicek Christian P.,
Henrissat Bernard
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80094-b
Subject(s) - cellulase , amino acid , biochemistry , amino acid residue , enzyme , peptide sequence , chemistry , structural similarity , sequence (biology) , similarity (geometry) , biology , gene , artificial intelligence , computer science , image (mathematics)
The amino acid sequences of seventeen family G xylanases and the two known family H cellulases have been compared by hydrophobic cluster analysis. A weak but significant similarity was demonstrated between these two families suggesting that these enzymes share the same molecular mechanism and catalytic residues and that they have related 3D folds. The major differences were found in the N‐terminal regions.