Difference between revisions of "Part:BBa K2933170"
Line 18: | Line 18: | ||
<partinfo>BBa_K2933170 parameters</partinfo> | <partinfo>BBa_K2933170 parameters</partinfo> | ||
<!-- --> | <!-- --> | ||
+ | ===Usage and Biology=== | ||
+ | <br> | ||
+ | |||
+ | ===Molecular cloning=== | ||
+ | <p style="text-align: center;"> | ||
+ | [[File:GIM-2-PCR.jpeg|400px|]] [[File:GIM-2-veri.jpeg|250px|]]<br> | ||
+ | |||
+ | '''Figure 1.''' Left: The result of PCR, Right:The result of double enzyme digestion verification | ||
+ | |||
+ | |||
+ | |||
+ | ==References== | ||
+ | 1. Skagseth S , Akhter S , Paulsen M H , et al. Metallo-β-lactamase inhibitors by bioisosteric replacement: Preparation, activity and binding[J]. European Journal of Medicinal Chemistry, 2017, 135:159-173. | ||
+ | |||
+ | 2. Wendel AF, MacKenzie CR. 2015. Characterization of a novel metallo-lactamase variant, GIM-2, from a clinical isolate of Enterobacter cloacae in Germany. Antimicrob Agents Chemother 59:1824 –1825. | ||
+ | |||
+ | 3. Borra P S , Samuelsen O , Spencer J , et al. Crystal Structures of Pseudomonas aeruginosa GIM-1: Active-Site Plasticity in Metallo-beta-Lactamases[J]. Antimicrobial Agents and Chemotherapy, 2013, 57(2):848-854. | ||
+ | |||
+ | 4. Susann S, Trine J C, Gro Elin K B, James S, Ørjan S, Hanna-Kirsti S. L. Role of Residues W228 and Y233 in the Structure and Activity of Metallo-β-Lactamase GIM-1. Antimicrobial Agents and Chemotherapy Jan 2016, 60 (2) 990-1002 |
Revision as of 12:38, 21 September 2019
Tac promoter+RBS a+Linker g+GST+Linker e+GIM-2
This part consists of Tac promoter,RBS and protein coding sequence (GST+Linker e+GIM-2),and the biological module can be built into E.coli for protein expression.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 1525
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 1525
- 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 1525
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 1525
- 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI.rc site found at 181
Usage and Biology
Molecular cloning
Figure 1. Left: The result of PCR, Right:The result of double enzyme digestion verification
References
1. Skagseth S , Akhter S , Paulsen M H , et al. Metallo-β-lactamase inhibitors by bioisosteric replacement: Preparation, activity and binding[J]. European Journal of Medicinal Chemistry, 2017, 135:159-173.
2. Wendel AF, MacKenzie CR. 2015. Characterization of a novel metallo-lactamase variant, GIM-2, from a clinical isolate of Enterobacter cloacae in Germany. Antimicrob Agents Chemother 59:1824 –1825.
3. Borra P S , Samuelsen O , Spencer J , et al. Crystal Structures of Pseudomonas aeruginosa GIM-1: Active-Site Plasticity in Metallo-beta-Lactamases[J]. Antimicrobial Agents and Chemotherapy, 2013, 57(2):848-854.
4. Susann S, Trine J C, Gro Elin K B, James S, Ørjan S, Hanna-Kirsti S. L. Role of Residues W228 and Y233 in the Structure and Activity of Metallo-β-Lactamase GIM-1. Antimicrobial Agents and Chemotherapy Jan 2016, 60 (2) 990-1002