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Literature summary for 6.1.1.5 extracted from
- Relaxed substrate specificity leads to extensive tRNA mischarging by Streptococcus pneumoniae class I and class II aminoacyl-tRNA synthetases (2014), mBio, 5, e01656-14 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ileS, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3), and overexpression in Escherichia coli strain B834(DE3) as selenomethionine-labeled protein | Streptococcus pneumoniae |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Streptococcus pneumoniae |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-isoleucine + tRNAIle | Streptococcus pneumoniae | - |
AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
| ATP + L-isoleucine + tRNAIle | Streptococcus pneumoniae D39 / NCTC 7466 | - |
AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
| additional information | Streptococcus pneumoniae | pneumococcal enzyme IleRS robustly mischarges its cognate tRNA with Leu and Val, comparative Streptomyces pneumoniae IleRS-catalyzed (mis)charging of wild-type and G16C tRNAIle with isoleucine, leucine, or valine, overview. IleRS has a weak posttransfer editing activity against LeutRNAIle. The G16C mutation in pneumococcal tRNAIle, is implicated in the editing of Val-tRNAIle by IleRS | ? | - |
? | |
| additional information | Streptococcus pneumoniae D39 / NCTC 7466 | pneumococcal enzyme IleRS robustly mischarges its cognate tRNA with Leu and Val, comparative Streptomyces pneumoniae IleRS-catalyzed (mis)charging of wild-type and G16C tRNAIle with isoleucine, leucine, or valine, overview. IleRS has a weak posttransfer editing activity against LeutRNAIle. The G16C mutation in pneumococcal tRNAIle, is implicated in the editing of Val-tRNAIle by IleRS | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptococcus pneumoniae | Q04JB0 | - |
- |
| Streptococcus pneumoniae D39 / NCTC 7466 | Q04JB0 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Streptococcus pneumoniae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-isoleucine + tRNAIle | - |
Streptococcus pneumoniae | AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
| ATP + L-isoleucine + tRNAIle | - |
Streptococcus pneumoniae D39 / NCTC 7466 | AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
| additional information | pneumococcal enzyme IleRS robustly mischarges its cognate tRNA with Leu and Val, comparative Streptomyces pneumoniae IleRS-catalyzed (mis)charging of wild-type and G16C tRNAIle with isoleucine, leucine, or valine, overview. IleRS has a weak posttransfer editing activity against LeutRNAIle. The G16C mutation in pneumococcal tRNAIle, is implicated in the editing of Val-tRNAIle by IleRS | Streptococcus pneumoniae | ? | - |
? | |
| additional information | analysis of the aminoacylation profiles of class I isoleucyl-tRNA synthetase (IleRS) | Streptococcus pneumoniae | ? | - |
? | |
| additional information | pneumococcal enzyme IleRS robustly mischarges its cognate tRNA with Leu and Val, comparative Streptomyces pneumoniae IleRS-catalyzed (mis)charging of wild-type and G16C tRNAIle with isoleucine, leucine, or valine, overview. IleRS has a weak posttransfer editing activity against LeutRNAIle. The G16C mutation in pneumococcal tRNAIle, is implicated in the editing of Val-tRNAIle by IleRS | Streptococcus pneumoniae D39 / NCTC 7466 | ? | - |
? | |
| additional information | analysis of the aminoacylation profiles of class I isoleucyl-tRNA synthetase (IleRS) | Streptococcus pneumoniae D39 / NCTC 7466 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| IleRS | - |
Streptococcus pneumoniae |
| ileS | - |
Streptococcus pneumoniae |
| Isoleucyl-tRNA synthetase | - |
Streptococcus pneumoniae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Streptococcus pneumoniae | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the class I amino acyl-tRNA synthetases (aaRS) | Streptococcus pneumoniae |
| physiological function | aminoacyl-tRNA synthetases provide the first step in protein synthesis quality control by discriminating cognate from noncognate amino acid and tRNA substrates. While substrate specificity is enhanced in many instances by cis- and transediting pathways, it has been revealed that in organisms such as Streptococcus pneumoniae some aminoacyl tRNA synthetases display significant tRNA mischarging activity. Pneumococcal IleRS mischarges tRNAIle with both Val and Leu in a tRNA sequence-dependent manner. IleRS substrate specificity is achieved in an editing-independent manner, indicating that tRNA mischarging is only significant under growth conditions where Ile is depleted. Adaptive misaminoacylation may contribute significantly to the viability of this pathogen during amino acid starvation | Streptococcus pneumoniae |
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