Difference between revisions of "Part:BBa K2549013:Design"
 
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<partinfo>BBa_K2549013 short</partinfo>
 
<partinfo>BBa_K2549013 short</partinfo>
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<partinfo>BBa_K2549013 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K2549013 SequenceAndFeatures</partinfo>
  
  
 
===Design Notes===
 
===Design Notes===
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The 219 residue of the wild-type TEV protease is mutated from serine to valine to remove autoinactivation and perform a more efficient catalyst[1].
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The residue 219 of the wild-type TEV protease is mutated from serine to valine (S219V) to remove autoinactivation and perform a more efficient catalyst<ref>Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency. Kapust RB, Tözsér J, Fox JD, ..., Copeland TD, Waugh DS. Protein Eng, 2001 Dec;14(12):993-1000  PMID: 11809930</ref>.
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<ref>Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency. Kapust RB, Tözsér J, Fox JD, ..., Copeland TD, Waugh DS. Protein Eng, 2001 Dec;14(12):993-1000  PMID: 11809930</ref>
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===Source===
 
===Source===
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from IDT(gBlock), codon optimized for human
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From IDT (gBlock), codon optimized for human
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===References===
 
===References===

Latest revision as of 11:03, 17 October 2018


TEV protease


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal SapI.rc site found at 316


Design Notes

The residue 219 of the wild-type TEV protease is mutated from serine to valine (S219V) to remove autoinactivation and perform a more efficient catalyst[1].


Source

From IDT (gBlock), codon optimized for human


References

  1. ↑ Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency. Kapust RB, Tözsér J, Fox JD, ..., Copeland TD, Waugh DS. Protein Eng, 2001 Dec;14(12):993-1000 PMID: 11809930