Difference between revisions of "Part:BBa K5034217:Design"
(2 intermediate revisions by the same user not shown) | |||
Line 7: | Line 7: | ||
===Design Notes=== | ===Design Notes=== | ||
− | + | In order to improve the efficiency of energy production and phosphorus accumulation of ''S. oneidensis'', the element of ''E. coli'' was migrated to ''S. oneidensis''. 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 ''NADK'' and ''PPK2'' can promote electron transport in ''S. oneidensis''. | |
Latest revision as of 11:46, 1 October 2024
PolyP <->Pi, Poly P -> NADP
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
In order to improve the efficiency of energy production and phosphorus accumulation of S. oneidensis, the element of E. coli was migrated to S. oneidensis. 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 NADK and PPK2 can promote electron transport in S. oneidensis.
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