Intriguing cellular processing of a fluorinated amino acid during protein biosynthesis in Escherichia coli

Abstract

Bioincorporation of the methionine analogue S-(2-fluoroethyl)-L-homocysteine (L-MFE) into bacteriophage lysozyme overproduced in Escherichia coli results not only in the expected L-MFE incorporation but surprisingly substantial L-vinthionine incorporation into the labeled lysozymes. Synthetic L-vinthionine itself however is not activated by purified Escherichia coli methionyl-tRNA synthetase. The indirect preparation of vinthionine-containing proteins has the potential to be an alternate strategy to prepare vinyl thioether moieties for click chemistry applications on proteins.