Composite
davBA-AK

Part:BBa_K3776006:Design

Designed by: Helene Heling Huang   Group: iGEM21_HK_SSC   (2021-10-01)


davB-davA-AK


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NotI site found at 800
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 1889
    Illegal BglII site found at 4844
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 2049
    Illegal NgoMIV site found at 3816
    Illegal AgeI site found at 1456
    Illegal AgeI site found at 1705
    Illegal AgeI site found at 3040
    Illegal AgeI site found at 5043
  • 1000
    COMPATIBLE WITH RFC[1000]


Design Notes

The genes have been codon optimized for Synechococcus elongatus UTEX 2973.

Source

Pcpc560, PsbA2 and TrbcL are from the genome of Synechocystis sp PCC6803.(Li et al., 2018)(Gao et al., 2021) DavB and DavA are from the 5-aminovalerate pathway in Pseudomonas putida KT2440.(Liu et al., 2014) The feedback insensitive AK was mutated from WT AK in Xenorhabdus bovienii.(Qi et al., 2011)

References

Li, S., Sun, T., Xu, C., Chen, L., & Zhang, W. (2018). Development and optimization of genetic toolboxes for a fast-growing cyanobacterium Synechococcus elongatus UTEX 2973. Metabolic Engineering, 48, 163–174. https://doi.org/10.1016/j.ymben.2018.06.002

Gao, E. B., Kyere-Yeboah, K., Wu, J., & Qiu, H. (2021). Photoautotrophic production of p-Coumaric acid using genetically engineered Synechocystis sp. Pasteur Culture Collection 6803. Algal Research, 54, 102180. https://doi.org/10.1016/j.algal.2020.102180

Liu, P., Zhang, H., Lv, M., Hu, M., Li, Z., Gao, C., Xu, P., & Ma, C. (2014). Enzymatic production of 5-aminovalerate from l-lysine using l-lysine monooxygenase and 5-aminovaleramide amidohydrolase. Scientific Reports, 4(1). https://doi.org/10.1038/srep05657

Qi, Q., Huang, J., Crowley, J., Ruschke, L., Goldman, B. S., Wen, L., & Rapp, W. D. (2011). Metabolically engineered soybean seed with enhanced threonine levels: biochemical characterization and seed-specific expression of lysine-insensitive variants of aspartate kinases from the enteric bacterium Xenorhabdus bovienii. Plant Biotechnology Journal, 9(2), 193–204. https://doi.org/10.1111/j.1467-7652.2010.00545.x