Difference between revisions of "Part:BBa K4275006"

Revision as of 09:58, 12 October 2022

TrEGIII-t

T. reesei Endoglucanase III fused with type I dockerin can interact with type I cohesin and bind onto CipA scaffoldin of a cellulosome to achieve high-efficiency synergetic dehydrolysation of cellulose with exoglucanases and beta-glugosidases. EG randomly hydrolyzes internal amorphous regions of cellulose fibers, releasing oligosaccharides of various degrees of polymerization (DP) and consequently generating new chain ends, one reducing and one nonreducing.

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

Usage and Biology

TrEGIII from Glycoside hydrolases (GH)7 family cleave O-glycosidic bonds GH-catalyzed hydrolysis proceeds via a general acid mechanism involving a cyclic oxocarbenium-like transition state with protonation of the glycosidic oxygen. They utilise retaining mechanisms (carboxylate substitutes glycosidic bond, then neutralised by carboxylic acid, then water attacks the ester intermediate) and randomly cleave glycosidic linkages in disordered regions of cellulose as they have relatively open active site clefts.

Sequence and Features

References

1. Chang, Jui-Jen et al. "PGASO: A Synthetic Biology Tool For Engineering A Cellulolytic Yeast". Biotechnology For Biofuels, vol 5, no. 1, 2012. Springer Science And Business Media LLC, https://doi.org/10.1186/1754-6834-5-53.