Difference between revisions of "Part:BBa K4275002"
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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. | 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. 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. | + | 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]. |
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NpaBGS is cDNA coding beta-glucosidase isolated from buffalo rumen fungus <i>Neocallimastix patriciarum</i> W5. | NpaBGS is cDNA coding beta-glucosidase isolated from buffalo rumen fungus <i>Neocallimastix patriciarum</i> 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). 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. | + | 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]. |
Revision as of 10:36, 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
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 502
- 21INCOMPATIBLE WITH RFC[21]Illegal XhoI site found at 1577
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 1074
Illegal AgeI site found at 88
Illegal AgeI site found at 106 - 1000COMPATIBLE WITH RFC[1000]
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.