Amino acid sequence similarities between low molecular weight endo-1,4-beta-xylanases and family H cellulases revealed by clustering analysis.
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.
Törrönen
A
A
Institut für Biochemische Technologie und Mikrobiologie, Technische Universität Wien, Austria.
Kubicek
C P
CP
Henrissat
B
B
D000595:Amino Acid Sequence; D001419:Bacteria / Q000201:enzymology / Q000235:genetics; D002480:Cellulase / Q000737:chemistry* / Q000235:genetics; D016000:Cluster Analysis; D043364:Endo-1,4-beta Xylanases; D005658:Fungi / Q000201:enzymology / Q000235:genetics; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000235:genetics; D007527:Isoenzymes / Q000737:chemistry* / Q000235:genetics; D008838:Microcomputers; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid; D012984:Software
D007527:Isoenzymes; D006026:Glycoside Hydrolases; D002480:Cellulase; D043364:Endo-1,4-beta Xylanases