Difference between revisions of "Part:BBa K4275006"
(→Sequence and Features) |
|||
| Line 3: | Line 3: | ||
<partinfo>BBa_K4275006 short</partinfo> | <partinfo>BBa_K4275006 short</partinfo> | ||
| − | <i>T. reesei</i> 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. | + | <i>T. reesei</i> 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[1]. |
[[File:GreatBay SCIE--3D TrEGIII-t.png|950px]] | [[File:GreatBay SCIE--3D TrEGIII-t.png|950px]] | ||
| Line 10: | Line 10: | ||
===Usage and Biology=== | ===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. | + | 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[1]. 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[1]. |
Revision as of 10:46, 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[1].
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[1]. 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[1].
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 322
- 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI site found at 194
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.