Difference between revisions of "Part:BBa K4275002"

Revision as of 12:21, 12 October 2022

NpaBGS-t

NpaBGS-t is fused with type I dokerin to enable the cellulase to interact with type I cohesin on Cipa2B9C scaffold and displayed on cellulosome complex. This type I dokerin-cohesin interaction is an extremely strong non-covalent interaction between molecules that stabilizes the structure of cellulosome. NpaBGS-t would act collectively with two other cellulases: an endoglucanase called TrEGIII-t and an exoglucanase called CBHII-t.

Beta-glucosidase is involved in the catalyzing the hydrolytic degradation of plant polysaccharide cellulose. In cellulose degradation, endoglucanase randomly cuts the beta-1,4-glycosidic bonds along cellulose chains, producing cellulose fragments of various length[1]. Exoglucanase then acts on either reducing or non-reducing ends of cellulose to free cellobiose molecules. Beta-glucosidase functions by converting cellobiose and oligosaccharides into glucose. As cellobiose is a strong allosteric inhibitor for the activity of both endo-beta-1,4-glucanase and cellodextrinase, beta-glucosidase plays an essential role in enhancing the efficiency of cellulose degradation[1].

Figure 1 The 3D structure of the protein predicted by Alphafold2.

Usage and Biology

NpaBGS is cDNA coding beta-glucosidase isolated from buffalo rumen fungus Neocallimastix patriciarum W5.

NpaBGS has 776 amino acid residues with a molecular mass of 85.1 kDa. Beta-glucosidase genes are commonly placed into glycosyl hydrolase families 1 and 3 (GH1 and GH3)[1]. NpaBGS is considered a beta-glucosidase of GH3 carrying two conserved putative domain - a GH3 N-terminal domain (Pfam00933) and a GH3 C-terminal domain (Pfam01915), located at residues 62 ~270 and 350 ~ 577 respectively. The aspartic acid residue Asp-251 in the conserved domain might be the active site of NpaBGS[1].

Sequence and Features

References

1.Chen, Hsin-Liang et al. "A Highly Efficient Β-Glucosidase From The Buffalo Rumen Fungus Neocallimastix Patriciarum W5". Biotechnology For Biofuels, vol 5, no. 1, 2012. Springer Science And Business Media LLC, https://doi.org/10.1186/1754-6834-5-24.