Difference between revisions of "Part:BBa K4863005"

 
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<partinfo>BBa_K4863005 short</partinfo>
 
<partinfo>BBa_K4863005 short</partinfo>
  
alpha type carbonic anhydrase fused with s-layer protein via a flexible linker for surface display of hpCA on the cell surface of <i>Synechocystis</i> PCC6803. Surface display maximizes hpCA's binding to substrate and ensures its stability.  
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alpha type carbonic anhydrase fused with s-layer protein via a flexible linker for surface display of hpCA on the cell surface of <i>Synechocystis</i> PCC6803. This yields a cell completely covered in the fusion protein. Surface display maximizes hpCA's binding to substrate and ensures its stability.  
  
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===Usage and Biology===
 
===Usage and Biology===
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The fusion of a protein to the Slp N-terminus has proved to be an effective system for the functional surface display of cyanobacteria. For the project of this year, we displayed α-carbonic anhydrase hpCA on the Synechocystis PCC6803 cell surface with the fusion with Slp on the cell surface for the production of calcium carbonate precipitates.
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hpCA is a metalloenzymes responsible for catalyzing the interconversion of carbon dioxide (CO2) to bicarbonate ions (HCO3−). It is an α-carbonic anhydrase isolated from the bacterium <i>Helicobacter pylori</i> 26695, codon optimized for expression in <i>E. Coli</i> BL21(DE3). Slp forms the paracrystalline S-layer by forming a regular lattice through an entropy-driven process. It has an undefined signal peptide at the C-terminus.
  
 
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Revision as of 04:14, 11 October 2023


T7_hpCA_Slp

alpha type carbonic anhydrase fused with s-layer protein via a flexible linker for surface display of hpCA on the cell surface of Synechocystis PCC6803. This yields a cell completely covered in the fusion protein. Surface display maximizes hpCA's binding to substrate and ensures its stability.

Usage and Biology

The fusion of a protein to the Slp N-terminus has proved to be an effective system for the functional surface display of cyanobacteria. For the project of this year, we displayed α-carbonic anhydrase hpCA on the Synechocystis PCC6803 cell surface with the fusion with Slp on the cell surface for the production of calcium carbonate precipitates.

hpCA is a metalloenzymes responsible for catalyzing the interconversion of carbon dioxide (CO2) to bicarbonate ions (HCO3−). It is an α-carbonic anhydrase isolated from the bacterium Helicobacter pylori 26695, codon optimized for expression in E. Coli BL21(DE3). Slp forms the paracrystalline S-layer by forming a regular lattice through an entropy-driven process. It has an undefined signal peptide at the C-terminus.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 443
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]