muramidase and vinthionine

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.

Topics: Amino Acids; Bacteriophage lambda; Escherichia coli; Escherichia coli Proteins; Ethionine; Halogenation; Homocysteine; Methionine; Methionine-tRNA Ligase; Models, Molecular; Muramidase; Protein Biosynthesis; Viral Proteins