Difference between revisions of "Part:BBa K3634000"
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This part has been previously categorised by the Minnesota iGEM team of 2012 who also sought to express the enzyme in E.coli (BBa_K814000). Here, by using the IDT codon optimisation tool, we have optimised the GC content of the sequence taken from A.variabilis to improve production efficiency of the final product shinorine. We have further made the part biobrick assembly standard RFC[10] & RFC[1000] compatible by removing EcoR1 and SapI restriction sites introduced by this optimisation step. | This part has been previously categorised by the Minnesota iGEM team of 2012 who also sought to express the enzyme in E.coli (BBa_K814000). Here, by using the IDT codon optimisation tool, we have optimised the GC content of the sequence taken from A.variabilis to improve production efficiency of the final product shinorine. We have further made the part biobrick assembly standard RFC[10] & RFC[1000] compatible by removing EcoR1 and SapI restriction sites introduced by this optimisation step. | ||
| − | The part should be used alongside the additional optimised parts (BBa_K3634001, BBa_K3634002 and BBa_K3634003) responsible for ultimate conversion of the substrate sedoheptulose 7-phosphate to the final product shinorine. | + | The part should be used alongside the additional optimised parts (BBa_K3634001, BBa_K3634002 and BBa_K3634003) responsible for ultimate conversion of the substrate sedoheptulose 7-phosphate to the final product shinorine. Shinorine is a UV absorbing compound which absorbs light of wavelength 333nm. It is produced by aquatic bacteria and algae species as a source of protection in regions of high UV intensity. Shinorine is just one of a whole selection of mycosporine-like amino acids (MAAs) which provide UV photoprotection across a range of different wavelengths in the UV portion of the EM spectrum. |
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Latest revision as of 16:17, 20 July 2020
3-Dehydroquinate Synthase (DHQS) (Codon Optimised for E.coli)
Codon optimised 3-dehydroquinate synthase (DHQS) CDS for use in E.coli as part of the shinorine synthesis gene cluster. The original gene for DHQS (Ava_3858) can be taken from the cyanobacteria species Anabaena variabilis ATCC 29413. The enzyme catalyses the conversion of sedoheptulose 7-phosphate, an intermediate of the pentose phosphate pathway (PPP), to (R)-demethyl-4-deoxygadusol.
This part has been previously categorised by the Minnesota iGEM team of 2012 who also sought to express the enzyme in E.coli (BBa_K814000). Here, by using the IDT codon optimisation tool, we have optimised the GC content of the sequence taken from A.variabilis to improve production efficiency of the final product shinorine. We have further made the part biobrick assembly standard RFC[10] & RFC[1000] compatible by removing EcoR1 and SapI restriction sites introduced by this optimisation step.
The part should be used alongside the additional optimised parts (BBa_K3634001, BBa_K3634002 and BBa_K3634003) responsible for ultimate conversion of the substrate sedoheptulose 7-phosphate to the final product shinorine. Shinorine is a UV absorbing compound which absorbs light of wavelength 333nm. It is produced by aquatic bacteria and algae species as a source of protection in regions of high UV intensity. Shinorine is just one of a whole selection of mycosporine-like amino acids (MAAs) which provide UV photoprotection across a range of different wavelengths in the UV portion of the EM spectrum.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]