Part:BBa_K4179018
SnoaL-like cyclase - XimE
XimE is part of the xiamenmycin biosynthesis gene cluster in addition to XimA, XimB, XimC, and XimD[1]. Xiamenmycin is a benzopyran compound that was shown as having anti fibrotic and anti-inflammatory activity[1]. XimE is an SnoaL-like cyclase that catalyzes the formation of a pyran product from an epoxide intermediate generated by XimD (Part:BBa_K4179016)[2].
Use and purpose
The team of Technion 2022 used this part in a construct (Part:BBa_K4179019). The purpose of the composite part is to introduce XimD and XimE into E. coli to allow the formation of decursinol (a pyran) from 7-methyldesuberosin. To ensure more of the pyran product (decursinol) in comparison with the furan product (marmesin), the team constrained a surplus of XimE via genetic manipulations.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal EcoRI site found at 160
- 12INCOMPATIBLE WITH RFC[12]Illegal EcoRI site found at 160
- 21INCOMPATIBLE WITH RFC[21]Illegal EcoRI site found at 160
- 23INCOMPATIBLE WITH RFC[23]Illegal EcoRI site found at 160
- 25INCOMPATIBLE WITH RFC[25]Illegal EcoRI site found at 160
Illegal AgeI site found at 139 - 1000COMPATIBLE WITH RFC[1000]
References
1. Yang, Y., Fu, L., Zhang, J., Hu, L., Xu, M., & Xu, J. (2014). Characterization of the xiamenmycin biosynthesis gene cluster in Streptomyces xiamenensis 318. PLoS One, 9(6), e99537.
2. He, B. B., Zhou, T., Bu, X. L., Weng, J. Y., Xu, J., Lin, S., ... & Xu, M. J. (2019). Enzymatic pyran formation involved in xiamenmycin biosynthesis. ACS Catalysis, 9(6), 5391-5399.
3. Bu, X. L., He, B. B., Weng, J. Y., Jiang, C. C., Zhao, Y. L., Li, S. M., ... & Xu, M. J. (2020). Constructing microbial hosts for the production of benzoheterocyclic derivatives. ACS Synthetic Biology, 9(9), 2282-2290.
4. He, B., Zhou, T., Bu, X., Weng, J., Xu, J., Lin, S., Zheng, J., Zhao, Y., & Xu, M. (2019). Snoal-like cyclase xime. https://doi.org/10.2210/pdb6isk/pdb
5. Pettersen, Eric F., et al. “UCSF Chimerax: Structure Visualization for Researchers, Educators, and Developers.” Protein Science, vol. 30, no. 1, 2020, pp. 70–82., https://doi.org/10.1002/pro.3943.
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