Cellulase families revealed by hydrophobic cluster analysi

doi:10.1016/0378-1119(89)90339-9

Gene

Volume 81, Issue 1, 1 September 1989, Pages 83-95

https://doi.org/10.1016/0378-1119(89)90339-9 Get rights and content

Abstract

The amino acid sequences of 21 β-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 cellobiohydrolase of Ce. fimi. For each family, conserved potentially catalytic residues 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.

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Cellulase families revealed by hydrophobic cluster analysi

Abstract

FEBS Lett.

Gene

Trends Biotechnol.

FEBS Lett.

J. Mol. Biol.

FEMS Microbiol. Lett.

J. Biotechnol.

Gene

Gene

Gene

Gene

Gene

Gene

FEBS Lett.

FEBS Lett.

Structural and functional domains of cellobiohydrolase I from Trichoderma reesei. A small angle X-ray scattering study of the intact enzyme and its core

Eur. Biophys. J.

Sequence of a cellulase gene of the thermophilic bacterium Clostridium thermocellum

J. Bacteriol.

Primary structure homologies between two zinc metallopeptidases, the neutral endopeptidase 24.11 (‘enkephalinase’) and thermolysin, through clustering analysis

Biochemistry

The disulphide bridges in a cellobiohydrolase and an endoglucanase from Trichoderma reesei

Biochem. J.

Resolution of glycanases of Trichoderma reesei with respect to cellulose and xylan degradation

Biotechnol. Appl. Biochem.

Nucleotide sequence and deduced primary structure of cellobiohydrolase II from Trichoderma reesei

Bio/Technology

The relation between the divergence of sequence and the structure in proteins

EMBO J.