Difference between revisions of "Part:BBa K4275006"
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<partinfo>BBa_K4275006 short</partinfo>
 
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<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.
  
 
[[File:GreatBay SCIE--3D TrEGIII-t.png|950px]]
 
[[File:GreatBay SCIE--3D TrEGIII-t.png|950px]]
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<p align="center"><b>Figure 1</b> The 3D structure of the protein predicted by Alphafold2. </p>
  
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===Usage and Biology===
 
===Usage and Biology===
  
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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.
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<span class='h3bb'>Sequence and Features</span>
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===Sequence and Features===
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<partinfo>BBa_K4275006 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K4275006 SequenceAndFeatures</partinfo>
  

Revision as of 23:05, 11 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.

GreatBay SCIE--3D TrEGIII-t.png

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


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 322
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal SapI site found at 194