EC Number |
Natural Substrates |
---|
6.1.1.5 | ATP + L-isoleucine + tRNAIle |
- |
6.1.1.5 | ATP + L-isoleucine + tRNAIle |
physiological function is Thr formation of Ile-tRNA and editing of inadvertently misactivated homocysteine |
6.1.1.5 | ATP + L-isoleucine + tRNAIle |
the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm |
6.1.1.5 | ATP + L-isoleucine + tRNAIle |
the reaction plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm |
6.1.1.5 | ATP + L-isoleucine + tRNAIle |
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 IleRS |
6.1.1.5 | more |
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I |
6.1.1.5 | more |
enzymatic reactions catalyzed by IleRS include amino acid activation, tRNA binding, aminoacyl transfer, and dissociation of aminoacylated tRNA from the enzyme, in the synthetic pathway. Pretransfer editing may proceed through enhanced dissociation of noncognate aminoacyl-AMP (1) or through its enzymatic hydrolysis, which may be tRNA-independent (2) ortRNA-dependent (3). Misacylated tRNA is deacylated through posttransferediting, overview |
6.1.1.5 | more |
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 | more |
the enzyme is also active with L-valine instead of L-isoleucine |