An efficient pyrrolysyl-tRNA synthetase for economical production of MeHis-containing enzymes.

ABSTRACT: Genetic code expansion has emerged as a powerful tool in enzyme design and engineering, providing new insights into sophisticated catalytic mechanisms and enabling the development of enzymes with new catalytic functions. In this regard, the non-canonical histidine analogue N_δ-methylhistidine (MeHis) has proven especially versatile due to its ability to serve as a metal coordinating ligand or a catalytic nucleophile with a similar mode of reactivity to small molecule catalysts such as 4-dimethylaminopyridine (DMAP). Here we report the development of a highly efficient aminoacyl tRNA synthetase (G1PylRS^MIFAF) for encoding MeHis into proteins, by transplanting five known active site mutations from Methanomethylophilus alvus (MaPylRS) into the single

SUBMITTER: Hutton AE 

PROVIDER: S-EPMC11389853 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature