Difference between revisions of "Part:BBa K2201205"
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<partinfo>BBa_K2201205 short</partinfo> | <partinfo>BBa_K2201205 short</partinfo> | ||
| − | This cysteinyl-lysinyl-tRNA | + | This cysteinyl-lysinyl-tRNA synthetase is based on the work of Nguyen <i>et al</i>. (2011). It is originated from the pyrrolysyl-tRNA synthetase of <i>Methanosarcina barkeri</i> containing a C313V mutation. |
| − | + | <br> | |
| − | N<sup> | + | N<sup>ε</sup>-L-cysteinyl-L-lysine (CL) is an amino acid containing a free 1,2-aminothiol group at its side chain. 1,2-aminothiols are an important part of the synthesis of D-Luciferin. D-Luciferin is the substrate of |
the luciferase of the firefly <i>Photinus pyralis</i>. The synthesis of D-Luciferin is based on a condensation reaction between CL and a cyanobenzothiazole derivative resulting in a covalent bond between two thiazole | the luciferase of the firefly <i>Photinus pyralis</i>. The synthesis of D-Luciferin is based on a condensation reaction between CL and a cyanobenzothiazole derivative resulting in a covalent bond between two thiazole | ||
| − | residues. We designed and synthesized the novel amino acid <i>N</i><sup> | + | residues. We designed and synthesized the novel amino acid <i>N</i><sup>γ</sup>‑2‑cyanobenzothiazol‑6‑yl‑L‑asparagine which contains 6-amino-2-cyanobenzothiazole at its side chain. |
Additionally, we showed that both amino acids are able to undergo the mentioned condensation reaction enabling a system for highly specific binding between peptides and enzymes. | Additionally, we showed that both amino acids are able to undergo the mentioned condensation reaction enabling a system for highly specific binding between peptides and enzymes. | ||
| − | + | <br> | |
So this synthetase is an important part of our <html><a href="http://2017.igem.org/Team:Bielefeld-CeBiTec/Project/toolbox/fusing">fusing tool</a></html>. Together with the CLtRNA | So this synthetase is an important part of our <html><a href="http://2017.igem.org/Team:Bielefeld-CeBiTec/Project/toolbox/fusing">fusing tool</a></html>. Together with the CLtRNA | ||
(<html><a href="https://parts.igem.org/Part:BBa_K2201206">K2201206</a></html>) we developed a aminoacyl-tRNA synthetase/tRNA pair (<html><a href="https://parts.igem.org/Part:BBa_K2201208">K2201208</a></html>) to incorporate | (<html><a href="https://parts.igem.org/Part:BBa_K2201206">K2201206</a></html>) we developed a aminoacyl-tRNA synthetase/tRNA pair (<html><a href="https://parts.igem.org/Part:BBa_K2201208">K2201208</a></html>) to incorporate | ||
Latest revision as of 16:07, 1 November 2017
Cysteinyl-lysinyl-tRNA Synthetase
This cysteinyl-lysinyl-tRNA synthetase is based on the work of Nguyen et al. (2011). It is originated from the pyrrolysyl-tRNA synthetase of Methanosarcina barkeri containing a C313V mutation.
Nε-L-cysteinyl-L-lysine (CL) is an amino acid containing a free 1,2-aminothiol group at its side chain. 1,2-aminothiols are an important part of the synthesis of D-Luciferin. D-Luciferin is the substrate of
the luciferase of the firefly Photinus pyralis. The synthesis of D-Luciferin is based on a condensation reaction between CL and a cyanobenzothiazole derivative resulting in a covalent bond between two thiazole
residues. We designed and synthesized the novel amino acid Nγ‑2‑cyanobenzothiazol‑6‑yl‑L‑asparagine which contains 6-amino-2-cyanobenzothiazole at its side chain.
Additionally, we showed that both amino acids are able to undergo the mentioned condensation reaction enabling a system for highly specific binding between peptides and enzymes.
So this synthetase is an important part of our fusing tool. Together with the CLtRNA
(K2201206) we developed a aminoacyl-tRNA synthetase/tRNA pair (K2201208) to incorporate
CL.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 492
- 1000COMPATIBLE WITH RFC[1000]