Difference between revisions of "Part:BBa K4275005"

 
Line 3: Line 3:
 
<partinfo>BBa_K4275005 short</partinfo>
 
<partinfo>BBa_K4275005 short</partinfo>
  
−
1
+
MtCDH-t, fused with a dockerin, is a cellobiose dehydrogenase, one of the five cellulose-related enzymes fixed on type I cohesion, and thus on the scaffold composed of CipA2B9C and OlpB. Its reductive nature enables it to act as an electron donor to the “cellulase booster”, TaLPMO-t, another cellulose-related enzyme on the scaffold which boosts the efficiency of crystalline cellulose degradation. By fusing a type 1 dockerin through a CBM and a 36-bp glycine-rich linker at the C terminal of MtCDH, the free fungal reductase is converted into the cellulosomal mode. Synergizing with the other four cellulose-related enzymes and cellulose binding modules, MtCDH-t is an important contributor to the enhanced efficiency of cellulose degradation. This is a part in a part collection where we enable efficient degradation of cellulose in textile waste.
 +
 
  
−
<!-- Add more about the biology of this part here
 
 
===Usage and Biology===
 
===Usage and Biology===
 +
MtCDH-t, fused with a dockerin, is a cellobiose dehydrogenase that enhances cellulose degradation by coupling the oxidation of cellobiose to the reductive activation of polysaccharide monooxygenases (PMO) that catalyze the insertion of oxygen into C−H bonds adjacent to the glycosidic linkage. MtCDH has a heme domain at the N-terminal and a flavin domain at the C-terminal. The flavin domain is the site of oxidation of cellobiose, and subsequently, electrons are transferred to the heme domain. The reduced heme domain reduced the PMOs. MtCDH-t is fused with a type 1 dockerin through a CBM and a 36-bp glycine-rich linker, thus can bind to type 1 cohesin of the scaffold, immobilizing the enzyme.
  
 
<!-- -->
 
<!-- -->

Revision as of 09:03, 9 October 2022


MtCDH-t

MtCDH-t, fused with a dockerin, is a cellobiose dehydrogenase, one of the five cellulose-related enzymes fixed on type I cohesion, and thus on the scaffold composed of CipA2B9C and OlpB. Its reductive nature enables it to act as an electron donor to the “cellulase booster”, TaLPMO-t, another cellulose-related enzyme on the scaffold which boosts the efficiency of crystalline cellulose degradation. By fusing a type 1 dockerin through a CBM and a 36-bp glycine-rich linker at the C terminal of MtCDH, the free fungal reductase is converted into the cellulosomal mode. Synergizing with the other four cellulose-related enzymes and cellulose binding modules, MtCDH-t is an important contributor to the enhanced efficiency of cellulose degradation. This is a part in a part collection where we enable efficient degradation of cellulose in textile waste.


Usage and Biology

MtCDH-t, fused with a dockerin, is a cellobiose dehydrogenase that enhances cellulose degradation by coupling the oxidation of cellobiose to the reductive activation of polysaccharide monooxygenases (PMO) that catalyze the insertion of oxygen into C−H bonds adjacent to the glycosidic linkage. MtCDH has a heme domain at the N-terminal and a flavin domain at the C-terminal. The flavin domain is the site of oxidation of cellobiose, and subsequently, electrons are transferred to the heme domain. The reduced heme domain reduced the PMOs. MtCDH-t is fused with a type 1 dockerin through a CBM and a 36-bp glycine-rich linker, thus can bind to type 1 cohesin of the scaffold, immobilizing the enzyme.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 2706
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 1507
    Illegal AgeI site found at 358
    Illegal AgeI site found at 745
    Illegal AgeI site found at 871
    Illegal AgeI site found at 1420
  • 1000
    COMPATIBLE WITH RFC[1000]