Difference between revisions of "Part:BBa K5034217:Design"
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===Design Notes===
 
===Design Notes===
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n order to improve the efficiency of energy production and phosphorus accumulation of Shewanella, the element of E. coli was migrated to Shewanella. The tandem connection of the two enzymes actually promoted the synthesis of NADK, and by maintaining some polyp reserves. We believe that the introduction of NADP and PPK1 can promote electron transport in Shewanella.
+
In order to improve the efficiency of energy production and phosphorus accumulation of Shewanella, the element of E. coli was migrated to Shewanella. The tandem connection of the two enzymes actually promoted the synthesis of NADK, and by maintaining some polyp reserves. We believe that the introduction of NADP and PPK1 can promote electron transport in Shewanella.
  
  

Revision as of 11:53, 27 September 2024


PolyP <->Pi, Poly P -> NADP


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Design Notes

In order to improve the efficiency of energy production and phosphorus accumulation of Shewanella, the element of E. coli was migrated to Shewanella. The tandem connection of the two enzymes actually promoted the synthesis of NADK, and by maintaining some polyp reserves. We believe that the introduction of NADP and PPK1 can promote electron transport in Shewanella.


Source

BBa_K5034205: Polyphosphate kinase 2(PPK2) from Pseudomonas paraeruginosa. NCBI reference sequence: NZ_CP020560.1:c164262-163366

BBa_K5034206: Inorganic polyphosphate/ATP-NAD kinase(PPNK) from Mycobacterium tuberculosis H37Rv. NCBI reference sequence: NC_000962.3:1918746-1919669

References

Zhang, H., Ishige, K., & Kornberg, A. (2002). A polyphosphate kinase (PPK2) widely conserved in bacteria. Proceedings of the National Academy of Sciences, 99(26), 16678-16683. doi:10.1073/pnas.262655199

Neville, N., Roberge, N., & Jia, Z. (2022). Polyphosphate Kinase 2 (PPK2) Enzymes: Structure, Function, and Roles in Bacterial Physiology and Virulence. International Journal of Molecular Sciences, 23(2), 670. doi:10.3390/ijms23020670

Itoh, H., & Shiba, T. (2004). Polyphosphate synthetic activity of polyphosphate:AMP phosphotransferase in Acinetobacter johnsonii 210A. Journal of Bacteriology, 186(15), 5178-5181. doi:10.1128/jb.186.15.5178-5181.2004