Trichoderma reesei cellobiohydrolase Cel6A (formerly CBHII) has a tunnel shaped active site with four internal subsites for the glucose units. We have predicted an additional ring stacking interaction for a sixth glucose moiety with a tryptophan residue (W272) found on the domain surface. Mutagenesis of this residue selectively impairs the enzyme function on crystalline cellulose but not on soluble or amorphous substrates. Our data shows that W272 forms an additional subsite at the entrance of the active site tunnel and suggests it has a specialised role in crystalline cellulose degradation, possibly in guiding a glucan chain into the tunnel. (C) 1998 Federation of European Biochemical Societies.
|Number of pages||6|
|Publication status||Published - 16 Jun 1998|
|MoE publication type||A1 Journal article-refereed|
- crystalline cellulose
- sugar binding site
- LIMITED PROTEOLYSIS
- GLYCOSYL HYDROLASES