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Literature summary extracted from

  • Shepherd, J.; Ibba, M.
    Relaxed substrate specificity leads to extensive tRNA mischarging by Streptococcus pneumoniae class I and class II aminoacyl-tRNA synthetases (2014), mBio, 5, e01656-14 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.5 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

EC Number Metals/Ions Comment Organism Structure
6.1.1.5 Mg2+ required Streptococcus pneumoniae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.5 ATP + L-isoleucine + tRNAIle Streptococcus pneumoniae
-
AMP + diphosphate + L-isoleucyl-tRNAIle
-
?
6.1.1.5 ATP + L-isoleucine + tRNAIle Streptococcus pneumoniae D39 / NCTC 7466
-
AMP + diphosphate + L-isoleucyl-tRNAIle
-
?
6.1.1.5 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 ?
-
?
6.1.1.5 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

EC Number Organism UniProt Comment Textmining
6.1.1.5 Streptococcus pneumoniae Q04JB0
-
-
6.1.1.5 Streptococcus pneumoniae D39 / NCTC 7466 Q04JB0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.5 recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Streptococcus pneumoniae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.5 ATP + L-isoleucine + tRNAIle
-
Streptococcus pneumoniae AMP + diphosphate + L-isoleucyl-tRNAIle
-
?
6.1.1.5 ATP + L-isoleucine + tRNAIle
-
Streptococcus pneumoniae D39 / NCTC 7466 AMP + diphosphate + L-isoleucyl-tRNAIle
-
?
6.1.1.5 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 ?
-
?
6.1.1.5 additional information analysis of the aminoacylation profiles of class I isoleucyl-tRNA synthetase (IleRS) Streptococcus pneumoniae ?
-
?
6.1.1.5 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 ?
-
?
6.1.1.5 additional information analysis of the aminoacylation profiles of class I isoleucyl-tRNA synthetase (IleRS) Streptococcus pneumoniae D39 / NCTC 7466 ?
-
?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.5 IleRS
-
Streptococcus pneumoniae
6.1.1.5 ileS
-
Streptococcus pneumoniae
6.1.1.5 Isoleucyl-tRNA synthetase
-
Streptococcus pneumoniae

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.5 ATP
-
Streptococcus pneumoniae

General Information

EC Number General Information Comment Organism
6.1.1.5 evolution the enzyme belongs to the class I amino acyl-tRNA synthetases (aaRS) Streptococcus pneumoniae
6.1.1.5 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