Difference between revisions of "Part:BBa K4765010"
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===Usage and Biology=== | ===Usage and Biology=== | ||
− | We performed codon optimization on [https://parts.igem.org/Part:BBa_K4273004 BBa_K4273004 | + | We performed codon optimization on [https://parts.igem.org/Part:BBa_K4273004 BBa_K4273004(NpR5600)]specifically for the ''Escherichia coli'' K12 strain, resulting in the creation of this part. The enzyme MysA catalyzes the initial reaction involved in the biosynthesis of Mycosporine-like amino acids (MAAs) within ''E. coli''. |
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==References== | ==References== | ||
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Revision as of 06:53, 2 October 2023
MysA codon optimized
Introduction
MysA (DDGS) is a dimethyl 4-degadusol synthase that converts Sedoheptulose 7-phosphate (S7P) into Demethyl 4-deoxygadusol[1].
Figure1 The biosynthetic pathway of shinorine, porphyra-334, palythine-Ser, and palythine-Thr. 1 |
Usage and Biology
We performed codon optimization on BBa_K4273004(NpR5600)specifically for the Escherichia coli K12 strain, resulting in the creation of this part. The enzyme MysA catalyzes the initial reaction involved in the biosynthesis of Mycosporine-like amino acids (MAAs) within E. coli.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 1198
References
- ↑ Chen, M., Rubin, G. M., Jiang, G., Raad, Z., & Ding, Y. (2021). Biosynthesis and heterologous production of mycosporine-like amino acid palythines. The Journal of Organic Chemistry, 86(16), 11160–11168.