Difference between revisions of "Part:BBa K4765011"
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− | | '''Figure1 The biosynthetic pathway of shinorine, porphyra-334, palythine-Ser, and palythine-Thr | + | | '''Figure1 The biosynthetic pathway of shinorine, porphyra-334, palythine-Ser, and palythine-Thr''' |
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Revision as of 06:58, 2 October 2023
MysB codon optimized
Introduction
MysB (O-MT), an O-methyltrans-ferase, converts Demethyl 4-deoxygadusol into 4-deoxygadusol (4-DG), completing the production of 4-DG, the basic substrate of MAAs[1].
Figure1 The biosynthetic pathway of shinorine, porphyra-334, palythine-Ser, and palythine-Thr |
Usage and Biology
We performed codon optimization on BBa_K4273005 (NpR5599) specifically for the Escherichia coli K12 strain, resulting in the creation of this part. The enzyme MysB catalyzes the second 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 532
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.