Difference between revisions of "Part:BBa K936033"

 
 
Line 1: Line 1:
 
 
__NOTOC__
 
__NOTOC__
 
<partinfo>BBa_K936033 short</partinfo>
 
<partinfo>BBa_K936033 short</partinfo>
  
Mutant of the Polyetheylene Terephtalate degrading protein LC Cutinase (Bba_K936000). The phenylalanine at the 125th amino acid position is changed to a tyrosine. This part was created using site directed mutagenesis to change a "TTC" codon to a "TAT" codon.
+
Mutant of the Polyetheylene Terephtalate degrading protein LC Cutinase (Bba_K936000). The phenylalanine at the 125th amino acid position is changed to a tyrosine. This part was created using site directed mutagenesis to change a "TTC" codon to a "TAT" codon. <br>
 +
https://static.igem.org/mediawiki/2012/a/aa/UC_Davis_First_pNPB_Run.png <br>(Above Graph) Results of pNPB assay detailing the constitutive construct as having the highest esterase activity.https://static.igem.org/mediawiki/2012/6/62/UC_Davis_Third_pNPB_Run.png<br>(Above Graphs) The graphs above detail higher activity among the constitutive construct and some mutant variants in esterase activity compared to the control and wild type per unit cell. <br>https://static.igem.org/mediawiki/2012/5/59/UC_Davis_Last_pNPB_Run.png<br> (Above graph) This graph represents a possible production of cutinase by the cells upon entering stationary phase.<br><br>
  
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here

Latest revision as of 02:26, 4 October 2012

LC Cutinase mutant F125Y

Mutant of the Polyetheylene Terephtalate degrading protein LC Cutinase (Bba_K936000). The phenylalanine at the 125th amino acid position is changed to a tyrosine. This part was created using site directed mutagenesis to change a "TTC" codon to a "TAT" codon.
UC_Davis_First_pNPB_Run.png
(Above Graph) Results of pNPB assay detailing the constitutive construct as having the highest esterase activity.UC_Davis_Third_pNPB_Run.png
(Above Graphs) The graphs above detail higher activity among the constitutive construct and some mutant variants in esterase activity compared to the control and wild type per unit cell.
UC_Davis_Last_pNPB_Run.png
(Above graph) This graph represents a possible production of cutinase by the cells upon entering stationary phase.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 600
  • 1000
    COMPATIBLE WITH RFC[1000]