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Team:Washington/Celiacs/Parts
From 2011.igem.org
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| - | <center><big><big><big><big>Gluten Destruction: Parts Submitted</big></big></big></big></center><br><br> | + | <center><big><big><big><big>'''Gluten Destruction: Parts Submitted'''</big></big></big></big></center><br><br> |
Gluten Destruction submitted four parts to the registry: Wild-type Kumamolisin-As and three of our promising mutants. A short description for each part is provided below. | Gluten Destruction submitted four parts to the registry: Wild-type Kumamolisin-As and three of our promising mutants. A short description for each part is provided below. | ||
Revision as of 02:36, 23 September 2011
Gluten Destruction submitted four parts to the registry: Wild-type Kumamolisin-As and three of our promising mutants. A short description for each part is provided below.
[http://partsregistry.org/wiki/index.php?title=Part:BBa_K590021 BBa_K590021: Kumamolisin-As]
An enzyme from the sedolisin family native to Alicyclobacillus sendaiensis with known collagenase activity at low pH and elevated temperatures.
[http://partsregistry.org/wiki/index.php?title=Part:BBa_K590022 BBa_K590022: Kumamolisin-As_G319S, D358G, D368H]
A mutated Kumamolisin-As enzyme aimed to combat gluten intolerance by increased activity with the PQLP peptide, an antigenic epitope in gliadin. This mutant has point mutations at residues 319, 358, and 368 from Glycine to Serine, Aspartate to Glycine, and Aspartate to Histidine, respectively.
[http://partsregistry.org/wiki/index.php?title=Part:BBa_K590023 BBa_K590023: Kumamolisin-As_N291D]
A mutated Kumamolisin-As enzyme aimed to combat gluten intolerance by increased activity with the PQLP peptide, an antigenic epitope in gliadin. This mutant has a point mutation at residue 291 from Asparagine to Aspartate.
[http://partsregistry.org/wiki/index.php?title=Part:BBa_K590024 BBa_K590024: Kumamolisin-As_S354N, D358G, D368H]
A mutated Kumamolisin-As enzyme aimed to combat gluten intolerance by increased activity with the PQLP peptide, an antigenic epitope in gliadin. This mutant has point mutations at residue 354, 358, and 368 from Serine to Asparagine, Aspartate to Glycine, and Aspartate to Histidine, respectively.
