Difference between revisions of "Part:BBa K3989002"

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   <figcaption><b>Fig. 1 </b>. - Sub-structure at the binding site of eTEV. The blue amino acids are mutated and the purple one represents the cut site amino acid residue</figcaption>
 
   <figcaption><b>Fig. 1 </b>. - Sub-structure at the binding site of eTEV. The blue amino acids are mutated and the purple one represents the cut site amino acid residue</figcaption>
 
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Revision as of 09:38, 16 October 2021


eTEV, efficiency-enhanced TEV protease variant

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.


Structure and binding site

<figure> 

 <img src="21_UZurich_eTEV_binding_site.jpeg">
 <figcaption>Fig. 1 . - Sub-structure at the binding site of eTEV. The blue amino acids are mutated and the purple one represents the cut site amino acid residue</figcaption>

</figure> Sequence and Features BBa_K3989002 SequenceAndFeatures ===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.