Difference between revisions of "Part:BBa K2549013:Design"

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===Design Notes===
 
===Design Notes===
 
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].
 
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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<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>
  
  
 
===Source===
 
===Source===
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from IDT(gBlock), codon optimized for human
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IDT(gBlock)
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===References===
 
===References===
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[1]Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency.
 
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Kapust RB, Tözsér J, Fox JD, ..., Copeland TD, Waugh DS.
 
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Protein Eng, 2001 Dec;14(12):993-1000  PMID: 11809930
 

Revision as of 03:23, 7 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 219 residue of the wild-type TEV protease is mutated from serine to valine to remove autoinactivation and perform a more efficient catalyst[1]. [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