Difference between revisions of "Part:BBa K1689012"
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β-Lactamase(Amp) is produced by some bacteria, providing resistance against penicilins and so on. Theβ-Lactamase hydrolyzes β-lactam's conservative ring region, deactivating the antibiotic, and it can be use for the treatment of bacterial infection. <br/> | β-Lactamase(Amp) is produced by some bacteria, providing resistance against penicilins and so on. Theβ-Lactamase hydrolyzes β-lactam's conservative ring region, deactivating the antibiotic, and it can be use for the treatment of bacterial infection. <br/> | ||
In our project, β-Lactamase is used to catalyze the hydrolysis of penicillin to penicillinoic acid, leading to current changes to be detected using A3 electrode system. We can dissect β-Lactamase between Gly196 and Leu198, for this is opposite to the active site; meanwhile we can acquire a more active and metabolically stable pattern by introducing a mutation M182T, which disrupts an inactive molten-globule intermediate of β-Lactamase.<br/> | In our project, β-Lactamase is used to catalyze the hydrolysis of penicillin to penicillinoic acid, leading to current changes to be detected using A3 electrode system. We can dissect β-Lactamase between Gly196 and Leu198, for this is opposite to the active site; meanwhile we can acquire a more active and metabolically stable pattern by introducing a mutation M182T, which disrupts an inactive molten-globule intermediate of β-Lactamase.<br/> | ||
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[https://static.igem.org/mediawiki/parts/4/4a/Peking-speculation-Amp.png]<br/><br/><br/> | [https://static.igem.org/mediawiki/parts/4/4a/Peking-speculation-Amp.png]<br/><br/><br/> | ||
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Revision as of 18:08, 18 September 2015
dCas9-Nlact
Nterminal of β-lactamase fused with dCas9
β-Lactamase(Amp) is produced by some bacteria, providing resistance against penicilins and so on. Theβ-Lactamase hydrolyzes β-lactam's conservative ring region, deactivating the antibiotic, and it can be use for the treatment of bacterial infection.
In our project, β-Lactamase is used to catalyze the hydrolysis of penicillin to penicillinoic acid, leading to current changes to be detected using A3 electrode system. We can dissect β-Lactamase between Gly196 and Leu198, for this is opposite to the active site; meanwhile we can acquire a more active and metabolically stable pattern by introducing a mutation M182T, which disrupts an inactive molten-globule intermediate of β-Lactamase.
[1]
Sequence and Features
![[1]](https://static.igem.org/mediawiki/parts/4/4a/Peking-speculation-Amp.png){kind=link}
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 1150
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 4
Illegal BamHI site found at 3429 - 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]