the crystal structures show attached N-glycans at two of the predicted N-glycosylation sites (Asn57 and Asn206) and also at Asn432 near the C terminus of the catalytic domain. O-glycosylation at Ser196 is indicated by electron density, on a loop where the glycan probably influences loop contacts across the active site and interactions with the cellulose surface
the crystal structures show attached N-glycans at two of the predicted N-glycosylation sites (Asn57 and Asn206) and also at Asn432 near the C terminus of the catalytic domain. O-glycosylation at Ser196 is indicated by electron density, on a loop where the glycan probably influences loop contacts across the active site and interactions with the cellulose surface
sequence shows four potential N-glycosylation sites at the catalytic module: Asn45, Asn194, Asn388, and Asn430. The N-linked glycans represent variable high-mannose oligosaccharides and the products of their sequential enzymatic trimming, according to the formula (Man)0-13(GlcNAc)2, or a single GlcNAc residue. Mutations in the glycosylation sites have no notable effect on pH-optimum of activity and enzyme thermostability but influence both the enzyme adsorption ability on Avicel and its activity against natural and synthetic substrates
in the case of Trichoderma reesei/Talatomyces emersonii chimeric cellobiohydrolase I containing the catalytic domain from Talaromyces emersonii and the linker and carbohydrate-binding module from Trichoderma reesei which is expressed from Yarrowia, the overall magnitude of glycosylation is similar or only slightly higher than that for native cellobiohydrolase I produced in Trichoderma reesei
there are four N-glycosylation sites at N270, N384, N45 and N64. N45 and N64 are N-glycosylated with high mannose type glycans. The catalytic domain of the enzyme is extensively O-glycosylated with hexoses and N-acetylhexosamines. There are several glycosylation sites (such as T383, S8, and S46) at the openings of the substrate-binding tunnel, and potentially involve in the binding of cellulose
there are four N-glycosylation sites at N270, N384, N45 and N64. N45 and N64 are N-glycosylated with high mannose type glycans. The catalytic domain of the enzyme is extensively O-glycosylated with hexoses and N-acetylhexosamines. There are several glycosylation sites (such as T383, S8, and S46) at the openings of the substrate-binding tunnel, and potentially involve in the binding of cellulose
there are four N-glycosylation sites at N270, N384, N45 and N64. N45 and N64 are N-glycosylated with high mannose type glycans. The catalytic domain of the enzyme is extensively O-glycosylated with hexoses and N-acetylhexosamines. There are several glycosylation sites (such as T383, S8, and S46) at the openings of the substrate-binding tunnel, and potentially involve in the binding of cellulose
the encoded preprotein consists of 535 amino acids, divided into a 17-residue signal peptide followed by a GH7 catalytic module of about 436 residues, a Ser/Thr-rich linker region of about 47 residues, and finally a C-terminal CBM1 of about 35 residues
the encoded preprotein consists of 535 amino acids, divided into a 17-residue signal peptide followed by a GH7 catalytic module of about 436 residues, a Ser/Thr-rich linker region of about 47 residues, and finally a C-terminal CBM1 of about 35 residues