Difference between revisions of "Part:BBa K4275005"

Revision as of 10:44, 12 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 cohesin, 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[1]. This is a part in a part collection where we enable efficient degradation of cellulose in textile waste.

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

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[1]. 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]

References

1. Phillips, Christopher M. et al. "Cellobiose Dehydrogenase And A Copper-Dependent Polysaccharide Monooxygenase Potentiate Cellulose Degradation By Neurospora Crassa". ACS Chemical Biology, vol 6, no. 12, 2011, pp. 1399-1406. American Chemical Society (ACS), https://doi.org/10.1021/cb200351y.

@@ Line 3: / Line 3: @@
 <partinfo>BBa_K4275005 short</partinfo>
-MtCDH-t, fused with a dockerin, is a cellobiose dehydrogenase, one of the five cellulose-related enzymes fixed on type I cohesin, 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.
+MtCDH-t, fused with a dockerin, is a cellobiose dehydrogenase, one of the five cellulose-related enzymes fixed on type I cohesin, 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[1]. This is a part in a part collection where we enable efficient degradation of cellulose in textile waste.
 [[File:GreatBay SCIE--3D MtCDH-t.png|950px]]
@@ Line 9: / Line 9: @@
 ===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.
+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[1]. 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===