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Literature summary for 6.3.4.19 extracted from

  • Suzuki, T.; Miyauchi, K.
    Discovery and characterization of tRNAIle lysidine synthetase (TilS) (2010), FEBS Lett., 584, 272-277.
    View publication on PubMed

Application

Application Comment Organism
medicine lysidine/TilS is a eubacterial-specific system of AUA decoding. Therefore, TilS is an ideal target for a broad-spectrum antibacterial agent Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[tRNAIle2]-cytidine34 + L-lysine + ATP Escherichia coli
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[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
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?

Organism

Organism UniProt Comment Textmining
Escherichia coli P52097
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[tRNAIle2]-cytidine34 + L-lysine + ATP
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Escherichia coli [tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
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?
[tRNAIle2]-cytidine34 + L-lysine + ATP TilS specifically interacts with the isolated Escherichia coli tRNAIle2. Molecular mechanism of lysidine formation consists of two consecutive reactions involving the adenylated tRNA intermediate. TilS activates the C-2 position of C34 by forming an adenylate intermediate. Second, nucleophilic attack of the C-2 position of the intermediate by the epsilon-amino group of lysine completes the reaction Escherichia coli [tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
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?

Synonyms

Synonyms Comment Organism
TilS
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Escherichia coli
tRNAIle lysidine synthetase
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Escherichia coli

General Information

General Information Comment Organism
physiological function the single 2-lysylcytidine modification converts the codon-specificity from AUG to AUA, and the amino acid specificity from Met to Ile Escherichia coli