Member database | SUPERFAMILY |
SUPERFAMILY type | homologous superfamily |
Description Imported from IPR035971
The microbial degradation of cellulose and xylans requires several types of enzymes such as endoglucanases (
3.2.1.4), cellobiohydrolases (
3.2.1.91) (exoglucanases), or xylanases (
3.2.1.8)
[1]. Structurally, cellulases and xylanases generally consist of a catalytic domain joined to a cellulose-binding domain (CBD) by a short linker sequence rich in proline and/or hydroxy-amino acids. The CBD of a number of fungal cellulases has been shown to consist of 36 amino acid residues, and it is found either at the N-terminal or at the C-terminal extremity of the enzymes. As it is shown in the following schematic representation, there are four conserved cysteines in this type of CBD domain, all involved in disulphide bonds.
+----------------+ | +-----|---------+ | | | | xxxxxxxCxxxxxxxxxxCxxxxxCxxxxxxxxxCx
References Imported from IPR035971
1.Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families. Gilkes NR, Henrissat B, Kilburn DG, Miller RC Jr, Warren RA. Microbiol. Rev. 55, 303-15, (1991). View articlePMID: 1886523