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- W2051900539 abstract "Glycosylation is a prevalent posttranslational process capable of augmenting and modulating protein function. Efficient synthesis of high-purity, homogeneous glycoproteins is essential for the study of unique protein glycoforms and for the manufacture of therapeutically relevant forms. A promising new strategy for controlled in vivo synthesis of glycoproteins was recently established using suppressor tRNA technology. Using an evolved tRNA aminoacyl synthetase-tRNA pair from Methanococcus jannaschii, the glycosyl amino acid, N-acetylglucosamine-β-O-serine (GlcNAc-β-Ser), was site-specifically introduced into proteins cotranslationally in Escherichia coli. Herein, we report the evolution of a new tRNA aminoacyl synthetase-tRNA pair that has expanded the repertoire of glycoproteins that can be expressed in E. coli to contain the other major O-linked glycan, N-acetylgalactosamine-α-O-threonine (GalNAc-a-Thr)." @default.
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- W2051900539 date "2004-11-11" @default.
- W2051900539 modified "2023-10-11" @default.
- W2051900539 title "Site-Specific Incorporation of the Mucin-Type <i>N</i>-Acetylgalactosamine-α-<i>O</i>-threonine into Protein in <i>Escherichia </i><i>c</i><i>oli</i>" @default.
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- W2051900539 doi "https://doi.org/10.1021/ja044711z" @default.
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