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Fig. 2 | Biotechnology for Biofuels and Bioproducts

Fig. 2

From: Characterization of a novel thermophilic metagenomic GH5 endoglucanase heterologously expressed in Escherichia coli and Saccharomyces cerevisiae

Fig. 2

Alignment of Cel776 with GH5 family proteins of known structure. Alignment of Cel776 to sequences in the CAZy database annotated as GH5 with known structure. Green triangles indicate conserved residues of GH5 that have been linked to the catalytic activity of the enzyme. The orange triangle highlights the conserved catalytic residue that act as nucleophile. The blue triangle indicates the conserved catalytic residue that acts as proton donor (mutated in two of the proteins that are rendered inactive). The blue box indicates a predicted N-glycosylation site in the Cel776 sequence. 4u5i.1.A: sequence of inactive mutant CtCel5E (E314A) bifunctional cellulase/xylanase from Clostridium thermocellum. 3azr.1.A: sequence of inactive mutant TmCel5A (E253A) multifunctional endoglucanase from Thermotoga maritima. 3rjy.1.A: sequence of FnCel5A endoglucanase from Fervidobacterium nodosum Rt17-B1

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