Stieglitz, Jessica T.’s team published research in ACS Synthetic Biology in 2022 | CAS: 2418-95-3

H-Lys(Boc)-OH(cas: 2418-95-3) belongs to amino acids. Amino acids are not generally considered to be electrochemically active because products of the oxidation accumulate on the electrode surface and prevent it from participating in any further electrochemical processes.Formula: C11H22N2O4

Formula: C11H22N2O4On May 20, 2022 ,《Exploration of Methanomethylophilus alvus pyrrolysyl-tRNA synthetase activity in yeast》 appeared in ACS Synthetic Biology. The author of the article were Stieglitz, Jessica T.; Lahiri, Priyanka; Stout, Matthew I.; Van Deventer, James A.. The article conveys some information:

Archaeal pyrrolysyl-tRNA synthetases (PylRSs) have been used to genetically encode over 200 distinct noncanonical amino acids (ncAAs) in proteins in Escherichia coli and mammalian cells. This vastly expands the range of chem. functionality accessible within proteins produced in these organisms. Despite these clear successes, explorations of PylRS function in yeast remain limited. In this work, we demonstrate that the Methanomethylophilus alvus PylRS (MaPylRS) and its cognate tRNACUAMaPyl support the incorporation of ncAAs into proteins produced in Saccharomyces cerevisiae using stop codon suppression methodologies. Addnl., we prepared three MaPylRS mutants originally engineered in E. coli and determined that all three were active with one or more ncAAs, although with low efficiencies of ncAA incorporation in comparison to the parent MaPylRS. Alongside MaPylRS variants, we evaluated the activity of previously reported Methanosarcina mazei, Methanosarcina barkeri, and chimeric M. mazei and M. barkeri PylRSs. Using S. cerevisiae RJY100 and pairing these PylRSs with the M. mazei tRNACUA, we did not observe any detectable stop codon suppression activity under the same conditions that produced moderately efficient ncAA incorporation with MaPylRS. The addition of MaPylRS/tRNACUAMaPyl to the orthogonal translation machinery toolkit in S. cerevisiae potentially opens the door to hundreds of ncAAs that have not previously been genetically encodable using other aminoacyl-tRNA synthetase/tRNA pairs. Extending the scope of ncAA incorporation in yeast could powerfully advance chem. and biol. research for applications ranging from basic biol. discovery to enzyme engineering and therapeutic protein lead discovery. The experimental process involved the reaction of H-Lys(Boc)-OH(cas: 2418-95-3Formula: C11H22N2O4)

H-Lys(Boc)-OH(cas: 2418-95-3) belongs to amino acids. Amino acids are not generally considered to be electrochemically active because products of the oxidation accumulate on the electrode surface and prevent it from participating in any further electrochemical processes.Formula: C11H22N2O4

Referemce:
Amide – Wikipedia,
Amide – an overview | ScienceDirect Topics