Difference between revisions of "Part:BBa M50054"

Latest revision as of 07:29, 12 December 2016

PETase double mutant I208V and R90A

This is a mutant of PETase that combines two mutations designed by the 2016 iGEM Tianjin team. Wild-type PETase shows the ability to hydrolyze Polyethylene terephthalate (PET), commonly used for plastics. The two mutations are the 208th amino acid (changed from isoleucine(I) to valine(V)) and the 90th amino acid (changed from arginine (R) to alanine (A)), and each individual mutant has been showed by the Tianjin team to improve the catalytic activity of PET. This sequence combines both two mutations and is added 6 his tag at the end. The sequence is optimized for Escherichia coli.

Sequence and Features

Assembly Compatibility:

10
INCOMPATIBLE WITH RFC[10]
Illegal EcoRI site found at 633
Illegal PstI site found at 864
12
INCOMPATIBLE WITH RFC[12]
Illegal EcoRI site found at 633
Illegal PstI site found at 864
21
INCOMPATIBLE WITH RFC[21]
Illegal EcoRI site found at 633
23
INCOMPATIBLE WITH RFC[23]
Illegal EcoRI site found at 633
Illegal PstI site found at 864
25
INCOMPATIBLE WITH RFC[25]
Illegal EcoRI site found at 633
Illegal PstI site found at 864
Illegal NgoMIV site found at 220
1000
INCOMPATIBLE WITH RFC[1000]
Illegal SapI site found at 388

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 <partinfo>BBa_M50054 short</partinfo>
-This is a mutant of PETase that combines two mutations designed by the 2016 iGEM Tianjin team. Wild type PETase shows emzyme ability to hydrolyze Polyethylene terephthalate (PET), commonly used for plastics. The two mutations are the 208th amino acid (changed from isoleucine(I) to valine(V)) and the 90th amino acid (changed from arginine (R) to alanine (A)), and each individual mutant has been showed by the Tianjin team to improve the catalytic activity of PET. This sequence combines both mutations, and is added a 6 his tag at the end. The sequence is optimized for Escherichia coli.
+This is a mutant of PETase that combines two mutations designed by the 2016 iGEM Tianjin team. Wild-type PETase shows the ability to hydrolyze Polyethylene terephthalate (PET), commonly used for plastics. The two mutations are the 208th amino acid (changed from isoleucine(I) to valine(V)) and the 90th amino acid (changed from arginine (R) to alanine (A)), and each individual mutant has been showed by the Tianjin team to improve the catalytic activity of PET. This sequence combines both two mutations and is added 6 his tag at the end. The sequence is optimized for Escherichia coli.
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