Difference between revisions of "Part:BBa K4620012"
| Line 6: | Line 6: | ||
In the nature, QLLVW is conjugated to the N-terminal domain of Cca-BURP. iGEM 2023 team Latvia-Riga produced this peptide separately in order to make trans-cyclisation reaction where the cyclisation substrate is not attached to the catalytic domain. | In the nature, QLLVW is conjugated to the N-terminal domain of Cca-BURP. iGEM 2023 team Latvia-Riga produced this peptide separately in order to make trans-cyclisation reaction where the cyclisation substrate is not attached to the catalytic domain. | ||
| + | |||
| + | < img src="https://static.igem.wiki/teams/4620/wiki/wiki-illustrations/wiki-illustrations/team-members/qllvw.jpg" > | ||
<!-- Add more about the biology of this part here | <!-- Add more about the biology of this part here | ||
===Usage and Biology=== | ===Usage and Biology=== | ||
| − | |||
<!-- --> | <!-- --> | ||
Revision as of 15:14, 12 October 2023
CcaBURP2 core peptide
QLLVW is a peptide that can be cyclised by BURP domain protein from eastern redbud (Cercis canadensis (BBa_K4620007), forming stephanotic acid. This side chain macrocyclisation reaction is catalysed by copper (II) ions. Cyclisation happens between the Cβ of leucine and indole cycle 6- position of tryptophan residue. As of this day, mechanism of this reaction has not been fully characterised.
In the nature, QLLVW is conjugated to the N-terminal domain of Cca-BURP. iGEM 2023 team Latvia-Riga produced this peptide separately in order to make trans-cyclisation reaction where the cyclisation substrate is not attached to the catalytic domain.
< img src="
" >
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]
- 1000COMPATIBLE WITH RFC[1000]