Difference between revisions of "Part:BBa K3989002"
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<partinfo>BBa_K3989002 short</partinfo>
 
<partinfo>BBa_K3989002 short</partinfo>
  
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eTEV protease is mutant from the original TEV protease. Seven amino acids(S3I, P8Q, S31T, E79G, T173A, V219R, A231V) are mutated in this variant and the catalytic efficiency is 2-fold higher than the original one.
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eTEV protease is a mutant from the original TEV protease. Seven amino acids(S3I, P8Q, S31T, E79G, T173A, V219R, A231V) are mutated in this variant and the catalytic efficiency is 2-fold higher than the original one.
  
  

Revision as of 15:26, 16 October 2021


eTEV, efficiency-enhanced TEV protease variant

eTEV protease is a mutant from the original TEV protease. Seven amino acids(S3I, P8Q, S31T, E79G, T173A, V219R, A231V) are mutated in this variant and the catalytic efficiency is 2-fold higher than the original one.


Structure and binding site

This variant is generated via a directed evaluation system called YESS 2.0 (Yeast Endoplasmic Reticulum (ER) Sequestration Screening). The structure is shown below.(Fig.A) Particularly, the sub-structure of at the binding site is shown as well.(Fig. B) The blue amino acid residues represent the mutated sites and the purple residue represent the binding and cutting site of the ligand.

Fig. A Structural model of eTEV
Fig. B Sub-structure at the binding site of eTEV.

Performance

Besides this variant, the author also reported some other variants(for instance, BBa_K3989001) with different mutations. Different mutations in the TEV protease ligand-binding site show different catalytic efficincy. The results are shown in Fig. C.

Fig. C Catalytic efficiencies of different TEV protease variants.

Reference

1) Denard, C. A., Paresi, C., Yaghi, R., McGinnis, N., Bennett, Z., Yi, L., ... & Iverson, B. L. (2021). YESS 2.0, a Tunable Platform for Enzyme Evolution, Yields Highly Active TEV Protease Variants. ACS Synthetic Biology, 10(1), 63-71.