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- W2127371122 abstract "The lipase from the thermophilic anaerobic bacterium Thermoanaerobacter thermohydrosulfuricus expressed in E. coli was used as a model protein for studies on genetic code engineering. All methionine residues in the protein were replaced with different amino acid analogs. The resulting protein congeners showed remarkable differences in enzyme activity when compared to the parent lipase. Additionally, the first efforts toward the development of a method for the position-specific replacements of Met residues are described. To this end, the host methionyl-tRNA synthetase (MetRS) along its cognate initiator tRNAfMet can be used to initiate protein synthesis, while an exogenous MetRS:tRNAMet pair is used to translate internal AUG codons more efficiently. The goal is to design biocatalysts with differential decoding at the N-terminus and internal positions for applications in biotechnology." @default.
- W2127371122 created "2016-06-24" @default.
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- W2127371122 date "2010-07-23" @default.
- W2127371122 modified "2023-09-24" @default.
- W2127371122 title "Genetic code engineering with methionine analogs for synthetic biotechnology" @default.
- W2127371122 hasPublicationYear "2010" @default.
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