EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   6.3.4.19 | mature [tRNAIle2]-cytidine34 + L-lysine + ATP |
TilS can modify both types of tRNA, pre-tRNAIle2 and mature tRNAIle2, with comparable efficiencies. TilS specifically recognizes the entire L-shape structure in pre-tRNAIle2 through extensive interactions coupled with sequential domain movements. TilS prevents the recognition of tRNAIle2 by methionyl-tRNA synthetase and achieves high specificity for its substrate |
Geobacillus kaustophilus |
mature [tRNAIle2]-2-lysylcytidine34 + AMP + diphosphate |
- |
? |
| 6.3.4.19 | more |
no substrate: N1-methyladenosine-5'-triphosphate, 2-aminoadenosine-5'-triphosphate, 2-amino-6-chloropurineriboside-5'-triphosphate, and 6-chloropurineriboside-5'-triphosphate |
Escherichia coli |
? |
- |
? |
| 6.3.4.19 | precursor [tRNAIle2]-cytidine34 + L-lysine + ATP |
TilS can modify both types of tRNA, pre-tRNAIle2 and mature tRNAIle2, with comparable efficiencies. TilS specifically recognizes the entire L-shape structure in pre-tRNAIle2 through extensive interactions coupled with sequential domain movements. TilS prevents the recognition of tRNAIle2 by methionyl-tRNA synthetase and achieves high specificity for its substrate |
Geobacillus kaustophilus |
precursor [tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate |
- |
? |
| 6.3.4.19 | [tRNAIle2]-cytidine34 + L-isoleucine + ATP |
the tRNAIle2(CAU) gene products are modified by TilS to produce tRNAIle2(LAU), while tRNAIle2(UAU) lacks modification especially in the anticodon sequence. tRNAIle2(LAU) is charged with isoleucine but tRNAIle2(UAU) is not |
Lactiplantibacillus plantarum |
[tRNAIle2]-2-L-isoleucylcytidine34 + AMP + diphosphate |
- |
? |
| 6.3.4.19 | [tRNAIle2]-cytidine34 + L-lysine + 7-deazaadenosine 5'-triphosphate |
Vmax/Km is 8.6% of Vmax/Km for ATP |
Escherichia coli |
[tRNAIle2]-2-L-lysylcytidine34 + 7-deazaadenosine 5'-phosphate + diphosphate |
- |
? |
| 6.3.4.19 | [tRNAIle2]-cytidine34 + L-lysine + 8-azidoadenosine 5'-triphosphate |
Vmax/Km is 2.3% of Vmax/Km for ATP |
Escherichia coli |
[tRNAIle2]-2-L-lysylcytidine34 + 8-azidoadenosine 5'-phosphate + diphosphate |
- |
? |
| 6.3.4.19 | [tRNAIle2]-cytidine34 + L-lysine + ATP |
- |
Escherichia coli |
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate |
- |
? |
| 6.3.4.19 | [tRNAIle2]-cytidine34 + L-lysine + ATP |
- |
Aquifex aeolicus |
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate |
- |
? |
| 6.3.4.19 | [tRNAIle2]-cytidine34 + L-lysine + ATP |
- |
Geobacillus kaustophilus |
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate |
- |
? |
| 6.3.4.19 | [tRNAIle2]-cytidine34 + L-lysine + ATP |
bacteria decode the isoleucine codon AUA using a tRNA species that is posttranscriptionally modified at the wobble position of the anticodon with a lysine-containing cytidine derivative called lysidine. The lysidine modification of tRNAIle2 is an essential identity determinant for proper aminoacylation by isoleucyl tRNA synthetase and codon recognition on the ribosome. The ATP- and lysine-dependent formation of lysidine is catalyzed by tRNAIle-lysidine synthetase |
Escherichia coli |
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate |
- |
? |
