Cellulase families revealed by hydrophobic cluster analysis

• Published in: Gene Vol. 81; no. 1; p. 83
• Main Authors: Henrissat, B, Claeyssens, M, Tomme, P, Lemesle, L, Mornon, J P
• Format: Journal Article
• Language: English
• Published: Netherlands 01-09-1989
• Subjects: Amino Acid Sequence; Bacteria - enzymology; Bacteria - genetics; Binding Sites; Cellulase - classification; Cellulase - genetics; Cluster Analysis; Molecular Sequence Data; Protein Conformation; Sequence Homology, Nucleic Acid; Solubility
• ISSN: 0378-1119
• DOI: 10.1016/0378-1119(89)90339-9

The amino acid sequences of 21 beta-glycanases have been compared by hydrophobic cluster analysis. Six families of cellulases have been identified on the basis of primary structure homology: (A) endoglucanases B, C and E of Clostridium thermocellum; endoglucanases of Erwinia chrysanthemi and Bacillus sp.; endoglucanase III of Trichoderma reesei; endoglucanase I of Schizophyllum commune; (B) cellobiohydrolase II of T. reesei; endoglucanases of Cellulomonas fimi and Streptomyces sp; (C) cellobiohydrolases I of T. reesei and of Phanerochaete chrysosporium; endoglucanase I of T. reesei; (D) endoglucanase A of C. thermocellum and an endoglucanase from Ce. uda; (E) endoglucanase D of C. thermocellum and an endoglucanase from Pseudomonas fluorescens; (F) xylanases of C. thermocellum and of Cryptococcus albidus and the cellobio-hydrolase of Ce. fimi. For each family, conserved potentially catalytic residues have have been listed and previous allocations of the active-site residues are evaluated in the light of the alignment of the amino acid sequences. A strong homology is also reported for the putative cellulose-binding domains of cellulases of Ce. fimi and of P. fluorescens.