Difference between revisions of "Part:BBa K4765013"

(Introduction)
Line 6: Line 6:
  
 
===Introduction===
 
===Introduction===
MAA analogues like shinorine or porphyra-334 is transformed from MG by a D-Ala-D-Ala ligaselike enzyme gene MysD<ref>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.</ref>.
+
A D-Ala-D-Ala ligaselike enzyme gene MysD converts Mycosporine-glycine(MG) tO MAA analogues like shinorine or porphyra-334 <ref>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.</ref>.
 
+
  
 
===Usage and Biology===
 
===Usage and Biology===

Revision as of 07:04, 2 October 2023


MysD codon optimized contributed by Fudan iGEM 2023

Introduction

A D-Ala-D-Ala ligaselike enzyme gene MysD converts Mycosporine-glycine(MG) tO MAA analogues like shinorine or porphyra-334 [1].

Usage and Biology

We performed codon optimization on BBa_K4273013 (NlmysD) specifically for the Escherichia coli K12 strain, resulting in the creation of this part. The enzyme MysD catalyzes the fourth reaction involved in the biosynthesis of Mycosporine-like amino acids (MAAs) within E. coli.

contributed by Fudan iGEM 2023
Figure1 The biosynthetic pathway of shinorine, porphyra-334, palythine-Ser, and palythine-Thr. 1

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 1003


References

  1. 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.