Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Isoleucine-transfer RNA ligase
Isoleucine-tRNA synthetase
isoleucyl tRNA synthetase
Isoleucyl-transfer ribonucleate synthetase
Isoleucyl-transfer RNA synthetase
Isoleucyl-tRNA synthetase
mitochondrial isoleucyl-tRNA synthetase
-
mt isoleucyl-tRNA synthetase
-
Mupirocin resistance protein
Synthetase, isoleucyl-transfer ribonucleate
additional information
-
the enzyme is a class I aminoacyl-tRNA synthetase
IleRS
-
-
-
-
ileS
-
IRS
-
-
-
-
Isoleucine translase
-
-
-
-
Isoleucine--tRNA ligase
-
-
-
-
Isoleucine--tRNA ligase
-
-
Isoleucine--tRNA ligase
-
-
Isoleucine--tRNA ligase
-
-
Isoleucine--tRNA ligase
-
Isoleucine--tRNA ligase
-
-
Isoleucine--tRNA ligase
-
-
Isoleucine--tRNA ligase
-
Isoleucine--tRNA ligase
-
Isoleucine--tRNA ligase
-
-
Isoleucine--tRNA ligase
-
Isoleucine-transfer RNA ligase
-
-
-
-
Isoleucine-transfer RNA ligase
-
-
Isoleucine-transfer RNA ligase
-
-
Isoleucine-transfer RNA ligase
-
-
Isoleucine-transfer RNA ligase
-
Isoleucine-transfer RNA ligase
-
-
Isoleucine-transfer RNA ligase
-
-
Isoleucine-transfer RNA ligase
-
-
Isoleucine-transfer RNA ligase
-
Isoleucine-transfer RNA ligase
-
Isoleucine-transfer RNA ligase
-
-
-
Isoleucine-transfer RNA ligase
-
-
Isoleucine-transfer RNA ligase
-
Isoleucine-transfer RNA ligase
-
-
-
Isoleucine-tRNA synthetase
-
-
-
-
Isoleucine-tRNA synthetase
-
-
Isoleucine-tRNA synthetase
-
-
Isoleucine-tRNA synthetase
-
-
Isoleucine-tRNA synthetase
-
Isoleucine-tRNA synthetase
-
-
Isoleucine-tRNA synthetase
-
-
Isoleucine-tRNA synthetase
-
Isoleucine-tRNA synthetase
-
Isoleucine-tRNA synthetase
-
-
Isoleucine-tRNA synthetase
-
isoleucyl tRNA synthetase
-
-
isoleucyl tRNA synthetase
-
-
Isoleucyl-transfer ribonucleate synthetase
-
-
-
-
Isoleucyl-transfer ribonucleate synthetase
-
-
Isoleucyl-transfer ribonucleate synthetase
-
-
Isoleucyl-transfer ribonucleate synthetase
-
-
Isoleucyl-transfer ribonucleate synthetase
-
Isoleucyl-transfer ribonucleate synthetase
-
-
Isoleucyl-transfer ribonucleate synthetase
-
-
Isoleucyl-transfer ribonucleate synthetase
-
-
Isoleucyl-transfer ribonucleate synthetase
-
Isoleucyl-transfer ribonucleate synthetase
-
Isoleucyl-transfer ribonucleate synthetase
-
-
-
Isoleucyl-transfer ribonucleate synthetase
-
-
Isoleucyl-transfer ribonucleate synthetase
-
Isoleucyl-transfer ribonucleate synthetase
-
-
-
Isoleucyl-transfer RNA synthetase
-
-
-
-
Isoleucyl-transfer RNA synthetase
-
-
Isoleucyl-transfer RNA synthetase
-
-
Isoleucyl-transfer RNA synthetase
-
-
Isoleucyl-transfer RNA synthetase
-
Isoleucyl-transfer RNA synthetase
-
-
Isoleucyl-transfer RNA synthetase
-
-
Isoleucyl-transfer RNA synthetase
-
-
Isoleucyl-transfer RNA synthetase
-
Isoleucyl-transfer RNA synthetase
-
Isoleucyl-transfer RNA synthetase
-
-
-
Isoleucyl-transfer RNA synthetase
-
-
Isoleucyl-transfer RNA synthetase
-
Isoleucyl-transfer RNA synthetase
-
-
-
Isoleucyl-tRNA synthetase
-
-
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
Isoleucyl-tRNA synthetase
-
-
-
Isoleucyl-tRNA synthetase
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
Isoleucyl-tRNA synthetase
-
Isoleucyl-tRNA synthetase
-
-
-
Isoleucyl-tRNA synthetase
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
Isoleucyl-tRNA synthetase
-
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
-
-
Mupirocin resistance protein
-
-
-
-
Mupirocin resistance protein
-
-
Mupirocin resistance protein
-
-
Mupirocin resistance protein
-
-
Mupirocin resistance protein
-
Mupirocin resistance protein
-
-
Mupirocin resistance protein
-
-
Mupirocin resistance protein
-
Mupirocin resistance protein
-
Mupirocin resistance protein
-
-
Mupirocin resistance protein
-
ScIleRS
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
Synthetase, isoleucyl-transfer ribonucleate
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
ATP + L-valine + tRNAIle
AMP + diphosphate + L-valyl-tRNAIle
-
CP1 domain of the enzyme deacylates or edits the mischarged Val-tRNAIle
r
Formycin 5'-triphosphate + isoleucine + tRNAIle
?
-
-
-
-
?
Ile-tRNAIle + 3-mercaptopropionate
S-Isoleucyl-3-mercaptopropionate + tRNAIle
-
-
-
?
Ile-tRNAIle + cysteamine
tRNAIle + isoleucylcysteamine
-
-
-
?
Ile-tRNAIle + cysteine
tRNAIle + isoleucylcysteine
-
D- and L-isomer of Lys
D-isoleucylcysteine and L-isoleucylcysteine
?
Ile-tRNAIle + DTT
Thioester of Ile and DTT + tRNAIle
-
-
-
?
Ile-tRNAIle + L-cysteine methyl ester
tRNAIle + isoleucyl-L-cysteine methyl ester
-
-
-
?
Ile-tRNAIle + N-acetylcysteine
S-isoleucyl-N-acetylcysteine + tRNAIle
-
-
-
?
Tubercidin 5'-triphosphate + isoleucine + tRNAIle
?
-
-
-
-
?
additional information
?
-
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-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
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-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
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
the reaction plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
the anticodon for methionine and isoleucine tRNAs differ by a single nucleotide, changing this nucleotide in an isoleucine tRNA is sufficient to change aminoacylation specificity to methionine
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
formation of an aminoacyl adenylate reaction intermediate
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
the binding region of the adenine moiety contains a wide hydrophobic pocket large enough to afford three linear aromatic rings
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
physiological function is Thr formation of Ile-tRNA and editing of inadvertently misactivated homocysteine
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
a two-step reaction, the first of which, the amino acid activation step, is reversible, while the second aminoacylation step is not, the amino acid editing site for LeuRS resides within the homologous CP1 domain containing a conserved threonine conferring amino acid substrate recognition, editing mechanism, some positions of the site are idiosyncratic to IleRS, residues Arg249, Asp251, Thr252, Met336, and Val338 are involved,overview
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
usage of purified recombinant tRNAGAU Ile (with G1-C72 instead of the wild-type A1-U72 sequence) overexpressed in Escherichia coli strain BL21(DE3)
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
0.3% or less of the activity with isoleucine is measured with other amino acids
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
tRNAIle from Pseudomonas fluorescens and Escherichia coli
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
tRNAIle from Pseudomonas fluorescens and Escherichia coli
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
enzyme has specificity for E. coli tRNAIle
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
formation of a enzyme-bound aminoacyl adenylate intermediate
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
reaction intermediate is the Ile-AMP-enzyme complex
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
enzyme shows a common recognition mode of aminoacyl-adenylate for a class I aminoacyl-tRNA synthetase, formation of high-energy reaction intermediate Ile-AMP
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
substrate recognition mechanisms of IleRS are characterized by the active-site rearrangement between the two editing modes, overview, the editing domain contributes to accurate aminoacylation by hydrolyzing the mis-synthesized intermediate, valyl-adenylate, in the pre-transfer editing mode and the incorrect final product, valyl-tRNAIle, in the post-transfer editing mode, Trp227 with its aromatic ring is important
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
enzyme shows a common recognition mode of aminoacyl-adenylate for a class I aminoacyl-tRNA synthetase, formation of high-energy reaction intermediate Ile-AMP
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
-
discrimination of 20 amino acids in aminoacylation of modified tRNAIle-C-C-A(3'NH2)
-
-
?
additional information
?
-
-
Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
wild-type an dmutant enzymes IleRS are tested in reactions with both L-valine and L-isoleucine, neither wild-type nor D342A IleRS significantly deacylates Ile-tRNAIle under steady-state conditions
-
-
?
additional information
?
-
-
wild-type an dmutant enzymes IleRS are tested in reactions with both L-valine and L-isoleucine, neither wild-type nor D342A IleRS significantly deacylates Ile-tRNAIle under steady-state conditions
-
-
?
additional information
?
-
-
Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
discrimination of 20 amino acids in aminoacylation of modified tRNAIle-C-C-A(3'NH2)
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-
?
additional information
?
-
-
Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
-
position 2,6,7,8,9,2' and 3' of ATP are important for catalytic action of isleucyl-tRNA synthetase
-
-
?
additional information
?
-
-
discrimination of 20 amino acids in aminoacylation of modified tRNAIle-C-C-A(3'NH2)
-
-
?
additional information
?
-
-
Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
the enzyme is also active with L-valine instead of L-isoleucine
-
-
?
additional information
?
-
-
the enzyme is also active with L-valine instead of L-isoleucine
-
-
?
additional information
?
-
analysed are ATP-PPi exchange assay, aminoacylation, and editing in the presence of tRNA of the recombinant wild-type and mutant enzymes. The enzyme is also active with L-valine instead of L-isoleucine, kinetics
-
-
?
additional information
?
-
-
analysed are ATP-PPi exchange assay, aminoacylation, and editing in the presence of tRNA of the recombinant wild-type and mutant enzymes. The enzyme is also active with L-valine instead of L-isoleucine, kinetics
-
-
?
additional information
?
-
the enzyme is also active with L-valine instead of L-isoleucine
-
-
?
additional information
?
-
analysed are ATP-PPi exchange assay, aminoacylation, and editing in the presence of tRNA of the recombinant wild-type and mutant enzymes. The enzyme is also active with L-valine instead of L-isoleucine, kinetics
-
-
?
additional information
?
-
-
enzyme also performs the reversible ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
enzyme also performs the reversible ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
enzyme also performs the reversible ATP-diphosphate exchange reaction
-
?
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
-
-
?
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
-
-
?
additional information
?
-
analysis of the aminoacylation profiles of class I isoleucyl-tRNA synthetase (IleRS)
-
-
?
additional information
?
-
-
analysis of the aminoacylation profiles of class I isoleucyl-tRNA synthetase (IleRS)
-
-
?
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
-
-
?
additional information
?
-
analysis of the aminoacylation profiles of class I isoleucyl-tRNA synthetase (IleRS)
-
-
?
additional information
?
-
-
the enzyme is also active with L-valine instead of L-isoleucine
-
-
?
additional information
?
-
-
the enzyme is also active with L-valine instead of L-isoleucine, kinetics
-
-
?
additional information
?
-
-
Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain
-
-
?
additional information
?
-
-
Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain
-
-
?
additional information
?
-
-
Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
additional information
?
-
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-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
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-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
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
the reaction plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
physiological function is Thr formation of Ile-tRNA and editing of inadvertently misactivated homocysteine
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
-
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
the enzyme is also active with L-valine instead of L-isoleucine
-
-
?
additional information
?
-
-
the enzyme is also active with L-valine instead of L-isoleucine
-
-
?
additional information
?
-
the enzyme is also active with L-valine instead of L-isoleucine
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
the enzyme is also active with L-valine instead of L-isoleucine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2E,4E)-5-[(2S,3R,6S,8R,9S)-3-butyl-3-[(3-carboxypropanoyl)oxy]-8-(2-hydroxyethyl)-9-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-3-methylpenta-2,4-dienoic acid
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): not determined
(2E,4E)-5-[(2S,3R,6S,8R,9S)-3-butyl-3-[(3-carboxypropanoyl)oxy]-8-[(2E)-4-hydroxy-3-methylbut-2-en-1-yl]-9-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-3-methylpenta-2,4-dienoic acid
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): not determined
(2E,4E)-5-[(2S,3R,6S,8R,9S)-3-butyl-3-[(3-carboxypropanoyl)oxy]-8-[(2E)-4-[(3-carboxypropanoyl)oxy]-3-methylbut-2-en-1-yl]-9-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-3-methylpenta-2,4-dienoic acid
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): above 15
(2E,4E)-5-[(2S,3R,6S,8R,9S)-3-butyl-3-[(3-carboxypropanoyl)oxy]-8-[(2E,4E)-6-hydroxy-3-methylhexa-2,4-dien-1-yl]-9-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-3-methylpenta-2,4-dienoic acid
-
IC50 (ng/ml): 560.3. Cell death inducibility of osteoclasts (microgram/ml): not determined
(2E,4E)-5-[(2S,3R,6S,8R,9S)-3-butyl-3-[(3-carboxypropanoyl)oxy]-8-[(2E,4E,6S,7S)-6,8-dihydroxy-3,7-dimethylocta-2,4-dien-1-yl]-9-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-3-methylpenta-2,4-dienoic acid
-
IC50 (ng/ml): 22.9. Cell death inducibility of osteoclasts (microgram/ml): 6.31
(2E,4E)-6-[(2R,3S,6S,8S,9R)-9-butyl-8-[(1E,3E)-4-carboxy-3-methylbuta-1,3-dien-1-yl]-9-[(3-carboxypropanoyl)oxy]-3-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-4-methylhexa-2,4-dienoic acid
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): not determined
(2E,4S,5S,6E,8E)-10-[(2R,3S,6S,8S,9R)-9-butyl-8-[(1E,3E)-4-carboxy-3-methylbuta-1,3-dien-1-yl]-3-methyl-9-[(methylsulfanyl)methoxy]-1,7-dioxaspiro[5.5]undec-2-yl]-5-hydroxy-4,8-dimethyldeca-2,6,8-trienoic acid
-
IC50 (ng/ml): 497.4. Cell death inducibility of osteoclasts (microgram/ml): 9.6
(2E,4S,5S,6E,8E)-10-[(2R,3S,6S,8S,9R)-9-butyl-8-[(1E,3E)-4-carboxy-3-methylbuta-1,3-dien-1-yl]-9-hydroxy-3-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-5-hydroxy-4,8-dimethyldeca-2,6,8-trienoic acid
-
IC50 (ng/ml): 94.6. Cell death inducibility of osteoclasts (microgram/ml): 11.5
(2E,4S,5S,6E,8E)-10-[(2R,3S,6S,8S,9R)-9-butyl-8-[(1E,3E)-4-carboxy-3-methylbuta-1,3-dien-1-yl]-9-methoxy-3-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-5-hydroxy-4,8-dimethyldeca-2,6,8-trienoic acid
-
IC50 (ng/ml): 57.9. Cell death inducibility of osteoclasts (microgram/ml): not determined
(2E,4S,5S,6E,8E)-10-[(2R,3S,6S,8S,9R)-9-butyl-8-[(1E,3E)-4-carboxy-3-methylbuta-1,3-dien-1-yl]-9-[(3-carboxypropanoyl)oxy]-3-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-4,5-dihydroxy-8-methyldeca-2,6,8-trienoic acid
-
IC50 (ng/ml): 14.4. Cell death inducibility of osteoclasts (microgram/ml): 1.01
(2E,4S,5S,6E,8E)-10-[(2R,3S,6S,8S,9R)-9-butyl-8-[(1E,3E)-4-carboxy-3-methylbuta-1,3-dien-1-yl]-9-[(4-methoxy-4-oxobutanoyl)oxy]-3-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-5-hydroxy-4,8-dimethyldeca-2,6,8-trienoic acid
-
IC50 (ng/ml): 292.8. Cell death inducibility of osteoclasts (microgram/ml): 2.5
(3S)-3-amino-1-bromo-4-methylhexan-2-one
-
labeling reagent
(3S)-3-amino-1-bromo-4-methylpentan-2-one
-
labeling reagent
(3S)-3-amino-1-bromo-4-phenylbutan-2-one
-
labeling reagent
(3S)-3-amino-1-bromoheptan-2-one
-
labeling reagent
2',3'-dialdehyde of tRNAile
-
used to label the binding site for the 3'end of tRNA on the synthetase, incubation of the reagent with IleRS results in a rapid loss of tRNAIle aminoacylation and isoleucine-dependent isotopic ATP-PPi exchange activities
-
2,3-dideoxy-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamate
-
IC50: 0.0064 mM
2,3-Dihydro-5-epireveromycin A
-
IC50 (ng/ml): 58.3. Cell death inducibility of osteoclasts (microgram/ml): 0.82
2,3-Dihydroreveromycin A
-
IC50 (ng/ml): 11.6. Cell death inducibility of osteoclasts (microgram/ml): 0.22
2-deoxy-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamate
-
IC50: 0.28 mM
2-fluoro-9-(5-O-phosphono-alpha-L-arabinofuranosyl)-9H-purin-6-amine
-
-
2-iodo-L-isoleucine-NHSO2-AMP
-
highly potent inhibitor, hydrophobic interaction of the 2-substituent of the inhibitor with the adenine binding site of the enzyme
3'-amino-3'-deoxy-N,N-dimethyladenosine
-
-
3'-deoxyadenosine
-
i.e. cordycepin
3-deoxy-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamate
-
IC50: 0.035 mM
4,6-dideoxy-4-[[N-(14-methylpentadecanoyl)glycyl]amino]-N-9H-purin-6-ylhexopyranosylamine
-
-
5'-N-[N-(L-isoleucyl)sulfamoyl]adenosine
-
non-hydrolyzable analogue of the reaction intermediate Ile-AMP
5-acetyl-Reveromycin A
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): 0.46
5-Epireveromycin A
-
IC50 (ng/ml): 378.3. Cell death inducibility of osteoclasts (microgram/ml): 21.5
5-methoxy-Reveromycin A
-
IC50 (ng/ml): 374. Cell death inducibility of osteoclasts (microgram/ml): above 15
5-O-succinyl-Spirofungin A
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): 12.4
5-tert-butyl-dimethylsilyl-Reveromycin A
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): 5.9
7-[3-[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]propanoyl-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 10% inhibition at 0.1 mM
7-[4-[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]butanoyl-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]acetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 17% inhibition at 0.1 mM
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxylic acid methyl ester
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-4,4a,5,6,7,7a-hexahydro-1-methyl-1H-cyclopenta[b]pyridine-3-carboxylic acid methyl ester
7-[[(S)-2-amino-1-oxo-5-thiahexyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
7-[[(S)-2-amino-1-oxo-hexyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
7-[[(S)-2-amino-3-methyl-1-oxobutyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxylic acid methyl ester
7-[[(S)-2-amino-3-methyl-1-oxobutyl]amino]sulfonylacetyloxy-4,4a,5,6,7,7a-hexahydro-1-methyl-1H-cyclopenta[b]pyridine-3-carboxylic acid methyl ester
7-[[(S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-4,4a,5,6,7,7a-hexahydro-1-methyl-1H-cyclopenta[b]pyridine-3-carboxylic acid methyl ester
7-[[(S)-2-amino-4-methyl-1-oxopentyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxylic acid methyl ester
-
derivative of SB-203207, 14% inhibition at 0.1 mM
8-azidoadenosine 5'-triphosphate
-
-
9-(3-deoxy-alpha-L-threo-pentofuranosyl)-9H-purin-6-amine
-
-
9-(5-O-acetyl-alpha-L-arabinofuranosyl)-9H-purin-6-amine
-
-
9-(alpha-D-arabinofuranosyl)-9H-purin-6-amine
-
competitive inhibition
9-(alpha-L-arabinofuranosyl)-9H-purin-6-amine
-
-
9-(alpha-L-arabinofuranosyl)-N-(3-methylbut-2-en-1-yl)-9H-purin-6-amine
-
-
9-(beta-D-arabinofuranosyl)-9H-purin-6-amine
-
-
9-[5-deoxy-5-[(methylsulfonyl)amino]-alpha-L-arabinofuranosyl]-9H-purin-6-amine
-
-
9-[5-O-(dimethoxyphosphoryl)-alpha-L-arabinofuranosyl]-9H-purin-6-amine
-
-
9-[5-O-[tert-butyl(dimethyl)silyl]-alpha-L-arabinofuranosyl]-9H-purin-6-amine
-
-
adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamate
-
IC50: 0.000265 mM
chloride
100 mM KCl causes 50% inhibition if the ionic strength is kept constant with potassium acetate. The KappM (tRNA) value is increased from 570 nm to 1370 nM when the KCl concentration is increased from 0 to 200 mM. Potassium acetate inhibits weakly, but K2SO4 inhibits stronger than KCl
chymotrypsin
-
proteolytic inactivation patterns, bound Ile-AMP or inhibitors isoleucinol adenylate and pseudomonic acid protect, 50fold higher concentration is needed for digestion of Ile-AMP-enzyme complex than for the free enzyme at 37°C
-
diphosphate
-
partly inhibits the binding of tRNA
ester analogues of isoleucyl adenylate
-
with or without cyclic substitutents at the adenine moiety
hydroxamate analogues of isoleucyl adenylate
-
with or without cyclic substitutents at the adenine moiety
Ile-NHSO2-AMP
-
non-hydrolyzable reaction intermediate analogue, slow-tight binding, competitive and inhibition mechanism, reversible
isoleucinol adenylate
-
determination of binding structures, bound inhibitor protects against proteolytic inactivation by trypsin or chymotrypsin and specifically alters the proteolytic cleavage pattern
isoleucinyl adenylate
-
i.e. Ile-ol-AMP, nonhydrolyzable reaction intermediate analogue, competitive with respect to both ATP and Ile
isoleucinyl-adenylate
-
i.e. Ile-ol-AMP, non-hydrolyzable reaction intermediate analogue, slow-tight binding, competitive and inhibition mechanism, reversible
isoleucyl isovanilloids
-
e.g. the isovanillic hydroxamate and amide analogue
isoleucyl sulfamate analogues
-
-
isoleucyl vanilloids
-
e.g. the vanillic hydroxamate with a phenolic hydoxyl at the para-position
isoleucyl-N'-adenosyl-N'-hydroxy sulfamide
-
-
isoleucyl-N'-adenosyloxy sulfamide
-
-
Mg2+
-
in presence of 50 mM K+ and in absence of polyamines, the optimal Mg2+ concentration for Ile-tRNA formation is 1 mM, an increase in Mg2+ concentration markedly inhibits
N8,N8-dimethyl-9-pentofuranosyl-9H-purine-6,8-diamine
-
-
purineriboside
-
i.e. nebularin
pyridoxal 5'-diphospho-5'-adenosine
-
affinity labeling reagent for the ATP-binding site, incubation of the reagent with IleRS results in a rapid loss of tRNAIle aminoacylation and isoleucine-dependent isotopic ATP-PPi exchange activities
Reveromycin A
-
IC50 (ng/ml): 2.95. Cell death inducibility of osteoclasts (microgram/ml): 0.06
Reveromycin A 1-methyl ester
-
IC50 (ng/ml): 211. Cell death inducibility of osteoclasts (microgram/ml): 2
Reveromycin A 24-methyl ester
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): 3.1
Reveromycin B
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): above 15
spermine
-
catalyzes ATP-diphosphate exchange, no inhibition of specific aminoacylation of tRNAIle
Spirofungin A
-
IC50 (ng/ml): 564.5. Cell death inducibility of osteoclasts (microgram/ml): above 30
Spirofungin B
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): above 30
thiaisoleucine
-
directly competes with isoleucine for a target, irreversible inhibition, inhibits ring-stage parasites in development
tRNA
-
partly inhibits the binding of diphosphate
Trypsin
-
proteolytic inactivation patterns, bound Ile-AMP or inhibitors isoleucinol adenylate and pseudomonic acid protect, 50fold higher concentration is needed for digestion of Ile-AMP-enzyme complex than for the free enzyme at 37°C
-
7-[4-[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]butanoyl-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 18% inhibition at 0.1 mM
7-[4-[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]butanoyl-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 26% inhibition at 0.1 mM
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
-
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
-
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxylic acid methyl ester
-
derivative of SB-203207, 49% inhibition at 0.1 mM
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxylic acid methyl ester
-
derivative of SB-203207, 31% inhibition at 0.1 mM
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-4,4a,5,6,7,7a-hexahydro-1-methyl-1H-cyclopenta[b]pyridine-3-carboxylic acid methyl ester
-
derivative of SB-203207, 46% inhibition at 0.1 mM
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-4,4a,5,6,7,7a-hexahydro-1-methyl-1H-cyclopenta[b]pyridine-3-carboxylic acid methyl ester
-
derivative of SB-203207, 34% inhibition at 0.1 mM
7-[[(S)-2-amino-1-oxo-5-thiahexyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 31% inhibition at 0.1 mM
7-[[(S)-2-amino-1-oxo-5-thiahexyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 38% inhibition at 0.1 mM
7-[[(S)-2-amino-1-oxo-hexyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 17% inhibition at 0.1 mM
7-[[(S)-2-amino-1-oxo-hexyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 46% inhibition at 0.1 mM
7-[[(S)-2-amino-3-methyl-1-oxobutyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxylic acid methyl ester
-
derivative of SB-203207, 31% inhibition at 0.1 mM
7-[[(S)-2-amino-3-methyl-1-oxobutyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxylic acid methyl ester
-
derivative of SB-203207, 38% inhibition at 0.1 mM
7-[[(S)-2-amino-3-methyl-1-oxobutyl]amino]sulfonylacetyloxy-4,4a,5,6,7,7a-hexahydro-1-methyl-1H-cyclopenta[b]pyridine-3-carboxylic acid methyl ester
-
derivative of SB-203207, 33% inhibition at 0.1 mM
7-[[(S)-2-amino-3-methyl-1-oxobutyl]amino]sulfonylacetyloxy-4,4a,5,6,7,7a-hexahydro-1-methyl-1H-cyclopenta[b]pyridine-3-carboxylic acid methyl ester
-
derivative of SB-203207, 10% inhibition at 0.1 mM
7-[[(S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-4,4a,5,6,7,7a-hexahydro-1-methyl-1H-cyclopenta[b]pyridine-3-carboxylic acid methyl ester
-
derivative of SB-203207, 13% inhibition at 0.1 mM
7-[[(S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-4,4a,5,6,7,7a-hexahydro-1-methyl-1H-cyclopenta[b]pyridine-3-carboxylic acid methyl ester
-
derivative of SB-203207, 15% inhibition at 0.1 mM
K+
potassium acetate inhibits weakly, but K2SO4 inhibits stronger than KCl. KCl and potassium acetate inhibit above 50 mM concentrations when high enough K+ concentration for full activity is reached
muciproin
-
muciproin
-
inhibition by blockage of the binding site of high energy intermediate Ile-AMP, the inhibitor contains a moiety that morphologically resembles the hydrophobic side chain of L-isoleucine, recognition is mediated by Pro46, Trp518, and Trp558
mupirocin
-
irreversible inhibition, inhibits development of invasion-competent parasites in the second asexual cycle, delayed death phenotype
mupirocin
inhibition of isoleucine activation by mupirocin, competitive inhibition, analyzed with ATP-diphosphate exchange reaction
mupirocin
-
Mup, an isoleucyl-adenylate analogue that inhibits the essential enzyme, isoleucyl-tRNA synthetase
mupirocin
a specific inhibitor of IleRS, which binds in the vicinity of an ATP-binding subsite, and is a bifunctional inhibitor with characteristics of both isoleucine and ATP, i.e. an analogue of isoleucyladenylate, binding structure, overview, mupirocin resistance is phenotypically divided into two groups: low-level and high-level. Highlevel resistance is mediated by a plasmid containing the ileS-2 gene that encodes a distinct isoleucyl-tRNA synthetase enzyme, whereas low-level resistance usually results from alteration of the native IleS as a consequence of spontaneous mutations in the ileS gene
mupirocin
-
poor inhibition of isoleucine activation by mupirocin, competitive inhibition, analyzed with ATP-diphosphate exchange reaction. SgIleRS synthetic site is highly resistant to mupirocin
pseudomonic acid
-
bifunctional inhibitor with characteristics of both isoleucine and ATP
pseudomonic acid
-
wild-type enzyme strongly inhibited, pseudomonic acid-resistant mutant only marginally
pseudomonic acid
i.e. muciproin
pseudomonic acid
-
pseudomonic acid A: Saccharomyces cerevisiae enzyme is 10000 times less sensitive than Escherichia coli enzyme
pseudomonic acid
-
forms a non-hydrolyzable reaction intermediate analogue, competitive inhibition
pseudomonic acid
-
competitive, determination of binding structures, bound inhibitor protects against proteolytic inactivation by trypsin or chymotrypsin and specifically alters the proteolytic cleavage pattern
SB-203207
-
anti-infective agent, isolated from Streptomyces NCIMB 40513, analogous to the reaction intermediate
SB-203207
-
anti-infective agent, isolated from Streptomyces NCIMB 40513, analogous to the reaction intermediate
SB-205952
-
a semisynthetic analogue of monic acid, possesing a nitrofuryl chromophore
SB-205952
-
a semisynthetic analogue of monic acid
additional information
-
inhibition mechanism and structural determinants
-
additional information
-
the ribose of ATP/AMP can be substituted by its biosteres acyclic amide, hydroxamate, dihydroisooxazole, and dihydrooxazole, binding structure, overview
-
additional information
-
no inhibition of isozyme IleRS-R2 by pseudomonic acid, i.e. muciproin
-
additional information
no inhibition of isozyme IleRS-R2 by pseudomonic acid, i.e. muciproin
-
additional information
-
diverse analogues of SB-203207 are not inhibitory, overview
-
additional information
-
diverse analogues of SB-203207 are not inhibitory, overview
-
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Aortic Aneurysm, Abdominal
Up regulation of isoleucyl-tRNA synthetase promotes vascular smooth muscle cells dysfunction via p38 MAPK/PI3K signaling pathways.
Aphasia
Novel IARS2 mutations in Japanese siblings with CAGSSS, Leigh, and West syndrome.
Bacterial Infections
Enzymatic glycosylation of the topical antibiotic mupirocin.
Bone Resorption
Reveromycin A, an agent for osteoporosis, inhibits bone resorption by inducing apoptosis specifically in osteoclasts.
Candidiasis
Efficacy of PLD-118, a novel inhibitor of candida isoleucyl-tRNA synthetase, against experimental oropharyngeal and esophageal candidiasis caused by fluconazole-resistant C. albicans.
Candidiasis
Efficacy, plasma pharmacokinetics, and safety of icofungipen, an inhibitor of Candida isoleucyl-tRNA synthetase, in treatment of experimental disseminated candidiasis in persistently neutropenic rabbits.
Carcinogenesis
The Oncogene IARS2 Promotes Non-small Cell Lung Cancer Tumorigenesis by Activating the AKT/MTOR Pathway.
Carcinoma, Non-Small-Cell Lung
IARS2 silencing induces non-small cell lung cancer cells proliferation inhibition, cell cycle arrest and promotes cell apoptosis.
Carcinoma, Non-Small-Cell Lung
The Oncogene IARS2 Promotes Non-small Cell Lung Cancer Tumorigenesis by Activating the AKT/MTOR Pathway.
Cardiomyopathy, Hypertrophic
Isoleucyl-tRNA synthetase levels modulate the penetrance of a homoplasmic m.4277T>C mitochondrial tRNA(Ile) mutation causing hypertrophic cardiomyopathy.
Cataract
Clinical and genetic characteristics of Chinese patients with familial or sporadic pediatric cataract.
Cataract
Expanding the clinical phenotype of IARS2-related mitochondrial disease.
Cataract
Mutation in the nuclear-encoded mitochondrial isoleucyl-tRNA synthetase IARS2 in patients with cataracts, growth hormone deficiency with short stature, partial sensorineural deafness, and peripheral neuropathy or with Leigh syndrome.
Cataract
Novel IARS2 mutations in Japanese siblings with CAGSSS, Leigh, and West syndrome.
Colonic Neoplasms
Expression of IARS2 gene in colon cancer and effect of its knockdown on biological behavior of RKO cells.
Deafness
Mutation in the nuclear-encoded mitochondrial isoleucyl-tRNA synthetase IARS2 in patients with cataracts, growth hormone deficiency with short stature, partial sensorineural deafness, and peripheral neuropathy or with Leigh syndrome.
Hearing Loss, Sensorineural
Novel IARS2 mutations in Japanese siblings with CAGSSS, Leigh, and West syndrome.
Hepatitis
Refractory very early-onset inflammatory bowel disease associated with cytosolic isoleucyl-tRNA synthetase deficiency: A case report.
Hip Dislocation
Confirmation of CAGSSS syndrome as a distinct entity in a Danish patient with a novel homozygous mutation in IARS2.
Infections
Expression of IARS2 gene in colon cancer and effect of its knockdown on biological behavior of RKO cells.
Infections
Inhibition of isoleucyl-tRNA synthetase as a potential treatment for human African Trypanosomiasis.
Infections
Mupirocin: biosynthesis, special features and applications of an antibiotic from a Gram-negative bacterium.
Infections
Phenyltriazole-functionalized sulfamate inhibitors targeting tyrosyl- or isoleucyl-tRNA synthetase.
Inflammatory Bowel Diseases
Refractory very early-onset inflammatory bowel disease associated with cytosolic isoleucyl-tRNA synthetase deficiency: A case report.
Influenza, Human
Effects of a minor isoleucyl tRNA on heterologous protein translation in Escherichia coli.
isoleucine-trna ligase deficiency
Does IARS2 deficiency cause an intrinsic disorder of bone development (skeletal dysplasia) or are the reported skeletal changes secondary to growth hormone deficiency and neuromuscular involvement?
isoleucine-trna ligase deficiency
Does IARS2 Deficiency Cause an Intrinsic Disorder of Bone Development (Skeletal Dysplasia) or Are the Reported Skeletal Changes Secondary to Growth Hormone Deficiency and Neuromuscular Involvement?
isoleucine-trna ligase deficiency
Refractory very early-onset inflammatory bowel disease associated with cytosolic isoleucyl-tRNA synthetase deficiency: A case report.
isoleucine-trna ligase deficiency
Response to: does IARS2 deficiency cause an intrinsic disorder of bone development (skeletal dysplasia) or are the reported skeletal changes secondary to growth hormone deficiency and neuromuscular involvement?
Leigh Disease
Confirmation of CAGSSS syndrome as a distinct entity in a Danish patient with a novel homozygous mutation in IARS2.
Leigh Disease
Mutation in the nuclear-encoded mitochondrial isoleucyl-tRNA synthetase IARS2 in patients with cataracts, growth hormone deficiency with short stature, partial sensorineural deafness, and peripheral neuropathy or with Leigh syndrome.
Leigh Disease
Novel IARS2 mutations in Japanese siblings with CAGSSS, Leigh, and West syndrome.
Leukemia
Knockdown of IARS2 Inhibited Proliferation of Acute Myeloid Leukemia Cells by Regulating p53/p21/PCNA/eIF4E Pathway.
Leukemia, Myeloid, Acute
Knockdown of IARS2 Inhibited Proliferation of Acute Myeloid Leukemia Cells by Regulating p53/p21/PCNA/eIF4E Pathway.
Lung Neoplasms
IARS2 silencing induces non-small cell lung cancer cells proliferation inhibition, cell cycle arrest and promotes cell apoptosis.
Lung Neoplasms
The Oncogene IARS2 Promotes Non-small Cell Lung Cancer Tumorigenesis by Activating the AKT/MTOR Pathway.
Melanoma
RNAi-mediated IARS2 knockdown inhibits proliferation and promotes apoptosis in human melanoma A375 cells.
Neoplasm Metastasis
Inhibitory mechanism of reveromycin A at the tRNA binding site of a class I synthetase.
Neoplasm Metastasis
The Oncogene IARS2 Promotes Non-small Cell Lung Cancer Tumorigenesis by Activating the AKT/MTOR Pathway.
Neoplasms
Alterations of repeated sequences in 5' upstream and coding regions in colorectal tumors from patients with hereditary nonpolyposis colorectal cancer and Turcot syndrome.
Neoplasms
Expression of IARS2 gene in colon cancer and effect of its knockdown on biological behavior of RKO cells.
Neoplasms
RNAi-mediated IARS2 knockdown inhibits proliferation and promotes apoptosis in human melanoma A375 cells.
Neoplasms
The Oncogene IARS2 Promotes Non-small Cell Lung Cancer Tumorigenesis by Activating the AKT/MTOR Pathway.
Neoplasms
Transcriptional profiling of genes at the human common fragile site FRA1H in tumor-derived cell lines.
Nervous System Diseases
Expanding the clinical phenotype of IARS2-related mitochondrial disease.
Peripheral Nervous System Diseases
Mutation in the nuclear-encoded mitochondrial isoleucyl-tRNA synthetase IARS2 in patients with cataracts, growth hormone deficiency with short stature, partial sensorineural deafness, and peripheral neuropathy or with Leigh syndrome.
Spasms, Infantile
Expanding the clinical phenotype of IARS2-related mitochondrial disease.
Spasms, Infantile
Novel IARS2 mutations in Japanese siblings with CAGSSS, Leigh, and West syndrome.
Stomach Neoplasms
Knockdown of IARS2 suppressed growth of gastric cancer cells by regulating the phosphorylation of cell cycle-related proteins.
Trypanosomiasis, African
Inhibition of isoleucyl-tRNA synthetase as a potential treatment for human African Trypanosomiasis.
Tuberculosis
A eubacterial Mycobacterium tuberculosis tRNA synthetase is eukaryote-like and resistant to a eubacterial-specific antisynthetase drug.
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evolution
enzyme IleRS is a class I aaRS enzyme built around the conserved N-terminal Rossmann fold catalytic domain, which encloses the synthetic site. Phylogenetic analysis suggests that the ileS1 and ileS2 genes of contemporary bacteria are the descendants of genes that might have arisen by an ancient duplication event before the separation of bacteria and archaea. The accuracy of Ile-tRNAIle synthesis may be entirely ensured by the powerful post-transfer editing domain, which is absolutely conserved through evolution. The origin of discrimination against valine in the synthetic reaction is evolutionarily conserved in IleRS, overview
evolution
-
phylogenetic analysis, the origin of discrimination against valine in the synthetic reaction is evolutionarily conserved in IleRS, overview
evolution
phylogenetic analysis, the origin of discrimination against valine in the synthetic reaction is evolutionarily conserved in IleRS, overview
evolution
the enzyme belongs to the class I amino acyl-tRNA synthetases (aaRS)
evolution
the enzyme belongs to the class I amino acyl-tRNA synthetases (aaRS)
evolution
-
phylogenetic analysis, the origin of discrimination against valine in the synthetic reaction is evolutionarily conserved in IleRS, overview
-
evolution
-
the enzyme belongs to the class I amino acyl-tRNA synthetases (aaRS)
-
malfunction
constitutive high levels of mt isoleucyl-tRNA synthetase (mt-IleRS) are associated with reduced penetrance of the homoplasmic m.4277T>C mt-tRNAIle mutation, causing hypertrophic cardiomyopathy, which is paralleled by results in mutant transmitochondrial cybrids following overexpression of mt-IleRS. Interchangeable ability of three human mt-aaRS, namely mt-ValRS, mt-LeuRS and mt-IleRS, to suppress the mitochondrial functional defects associated with pathogenic homoplasmic mutations in mt-tRNAIle gene (MTTI). Transient overexpression of cognate mt-IleRS causes a 1.5fold increase in the viability of m.4277T>C MTTI mutant cybrids grown in galactose medium. The carboxy-terminal domain of human mt-leucyl-tRNA synthetase is both necessary and sufficient to improve the pathologic phenotype associated either with the mild mutations or with the severe m.3243A>G mutation in the mt-tRNALeu(UUR) gene. This small, non-catalytic domain is able to directly and specifically interact in vitro with human mt-tRNALeu(UUR) with high affinity and stability and, with lower affinity, with mt-tRNAIle
malfunction
-
mutant ileS(T233P) allows tRNAIle mischarging while retaining wild-type Ile-tRNAIle synthesis activity. The growth rate of the ileS(T233P) strain BAL4571 is not significantly different from wild-type strain BAL4574. The ileS(T233P) strain is observed to exhibit a significant defect in formation of environmentally resistant spores. The sporulation defect ranges from 3fold to 30fold and is due to a delay in activation of early sporulation genes. The loss of aminoacylation quality control in the ileS(T233P) strain results in the inability to compete with a wild-type strain under selective conditions that require sporulation. The quality control-defective IleRS mutant is defective in expressing genes activated by the master regulator of sporulation, Spo0A. Phenotype, overview. Spo0A is the first transcription factor to become active, through phosphorylation by a phosphorelay, in the sporulation regulatory cascade
malfunction
mutations in the nuclear-encoded mitochondrial aminoacyltRNA synthetases are associated with a range of clinical phenotypes. A recessive disorder CAGSSS in three adult French-Canadian patients with a phenotype including cataracts, short-stature secondary to growth hormone deficiency, sensorineural hearing deficit, peripheral sensory neuropathy, and skeletal dysplasia is caused by a single missense mutation P909L in a conserved residue of the nuclear gene IARS2, encoding mitochondrial isoleucyl-tRNA synthetase. The mutation is homozygous in the affected patients, heterozygous in carriers, and absent in control chromosomes. IARS2 protein level is reduced in skin cells cultured from one of the patients, consistent with a pathogenic effect of the mutation. Compound heterozygous mutations in IARS2 are independently identified in a patient with a more severe mitochondrial phenotype diagnosed as Leigh syndrome. Phenotypes, overview
malfunction
under error-prone conditions Streptomyces griseus IleRS is able to rescue the growth of an Escherichia coli lacking functional IleRS, providing the first evidence that tRNA-dependent pre-transfer editing in IleRS is not essential for cell viability
malfunction
-
mutant ileS(T233P) allows tRNAIle mischarging while retaining wild-type Ile-tRNAIle synthesis activity. The growth rate of the ileS(T233P) strain BAL4571 is not significantly different from wild-type strain BAL4574. The ileS(T233P) strain is observed to exhibit a significant defect in formation of environmentally resistant spores. The sporulation defect ranges from 3fold to 30fold and is due to a delay in activation of early sporulation genes. The loss of aminoacylation quality control in the ileS(T233P) strain results in the inability to compete with a wild-type strain under selective conditions that require sporulation. The quality control-defective IleRS mutant is defective in expressing genes activated by the master regulator of sporulation, Spo0A. Phenotype, overview. Spo0A is the first transcription factor to become active, through phosphorylation by a phosphorelay, in the sporulation regulatory cascade
-
physiological function
-
hydrolytic editing activities are present in aminoacyl-tRNA synthetases possessing reduced amino acid discrimination in the synthetic reactions. Post-transfer hydrolysis of misacylated tRNA in class I editing enzymes, e.g. IleRS, occurs in a spatially separate domain inserted into the catalytic Rossmann fold. tRNA-dependent hydrolysis of noncognate valyl-adenylate by IleRS is largely insensitive to mutations in the editing domain of the enzyme and that noncatalytic hydrolysis after release is too slow to account for the observed rate of clearing. Pre-transfer editing in IleRS is an enzyme-catalyzed activity residing in the synthetic active site. Balance between pretransfer and post-transfer editing pathways is controlled by kinetic partitioning of the noncognate aminoacyl-adenylate, overview. In IleRS both pre- and post-transfer editing are important
physiological function
-
the single trypanosomal IleRS gene is essential for normal growth and for charging of cytosolic and mitochondrial tRNAIle
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
physiological function
-
isoleucyl-tRNA synthetase (IleRS) is an aminoacyl-tRNA synthetase whose essential function is to aminoacylate tRNAIle with isoleucine. Like some other aminoacyl-tRNA synthetases, IleRS can mischarge tRNAIle and correct this misacylation through a separate post-transfer editing function, biological significance of this editing function. The quality control function of IleRS is required in Bacillus subtilis for efficient sporulation and editing by aminoacyl-tRNA synthetases may be important for survival under starvation/nutrient limitation conditions. Isoleucine-tRNA synthetase (IleRS) possesses quality control functions that discriminate between isoleucine, the non-cognate amino acid valine, and the non-proteinogenic amino acids, norvaline, a by-product of branched-chain amino acid synthesis, and homocysteine (Hcy), a by-product from degradation of S-adenosylhomocysteine by LuxS in bacteria
physiological function
isoleucyl-tRNA synthetase (IleRS) is responsible for decoding of isoleucine codons in all three domains of life. Besides isoleucine, IleRS also activates non-cognate valine with a discrimination factor as low as 200 and thus it requires editing to enhance accuracy of isoleucyltRNAIle (Ile-tRNAIle) synthesis. Enzyme IleRS is unusual among aminoacyl-tRNA synthetases in having a tRNA-dependent pre-transfer editing activity as an optional property. Some bacteria also have the enzymes (eukaryote-like) that cluster with eukaryotic IleRSs and exhibit low sensitivity to the antibiotic mupirocin. tRNA-dependent pre-transfer editing in IleRS is not essential for cell viability. Specificity of the editing pathways, overview
physiological function
isoleucyl-tRNA synthetase (IleRS) is responsible for decoding of isoleucine codons in all three domains of life. Besides isoleucine, IleRS also activates non-cognate valine with a discrimination factor as low as 200 and thus it requires editing to enhance accuracy of isoleucyltRNAIle (Ile-tRNAIle) synthesis. Enzyme IleRS is unusual among aminoacyl-tRNA synthetases in having a tRNA-dependent pre-transfer editing activity. The main tRNA-dependent pre-transfer editing pathway in ScIleRS is the enzyme-based aa-AMP hydrolysis. Specificity of the editing pathways, overview
physiological function
-
isoleucyl-tRNA synthetase (IleRS) is responsible for decoding of isoleucine codons in all three domains of life. Besides isoleucine, IleRS also activates non-cognate valine with a discrimination factor as low as 200 and thus it requires editing to enhance accuracy of isoleucyltRNAIle (Ile-tRNAIle) synthesis. The eukaryote-like enzyme from Streptomyces griseus IleRS lacks the tRNA-dependent pre-transfer editing activity, an unusual capacity of isoleucyl-tRNA synthetases (IleRS). At the same time, its synthetic site displays the 103fold drop in sensitivity to antibiotic mupirocin relative to the yeast enzyme. Under error-prone conditions Streptomyces griseus IleRS is able to rescue the growth of an Escherichia coli lacking functional IleRS, providing the first evidence that tRNA-dependent pre-transfer editing in IleRS is not essential for cell viability
physiological function
the accuracy of protein synthesis relies on the capacity of aminoacyl-tRNA synthetases (aaRS) to couple cognate amino acids and tRNAs in a two-step reaction that defines the genetic code. In the first step, the amino acid is activated by condensation with ATP to form an enzyme-bound aminoacyl-adenylate (aa-AMP) intermediate with release of pyrophosphate. The second step comprises attack by the terminal 2'- or 3'-OH group of tRNA on the carbonyl carbon atom of aa-AMP, followed by transfer of the aminoacyl moiety to tRNA and release of AMP. The amino acid activation and transfer steps occur within the synthetic active site located in the catalytic domain. Enzyme IleRS possesses an inactivated post-transfer editing domain still capable of robust tRNA-dependent editing. The pretransfer editing activity resides within the synthetic site. Specific recognition of tRNAs by cognate aaRSs is ensured by a network of interactions, based on direct and indirect recognition elements that are embedded in all levels of tRNA structure. Noncognate amino acids that structurally and chemically resemble the cognate substrates are often not well-distinguished in the synthetic reactions alone, so that discrimination is based in part on inherent aaRS-based hydrolytic editing
physiological function
-
isoleucyl-tRNA synthetase (IleRS) is an aminoacyl-tRNA synthetase whose essential function is to aminoacylate tRNAIle with isoleucine. Like some other aminoacyl-tRNA synthetases, IleRS can mischarge tRNAIle and correct this misacylation through a separate post-transfer editing function, biological significance of this editing function. The quality control function of IleRS is required in Bacillus subtilis for efficient sporulation and editing by aminoacyl-tRNA synthetases may be important for survival under starvation/nutrient limitation conditions. Isoleucine-tRNA synthetase (IleRS) possesses quality control functions that discriminate between isoleucine, the non-cognate amino acid valine, and the non-proteinogenic amino acids, norvaline, a by-product of branched-chain amino acid synthesis, and homocysteine (Hcy), a by-product from degradation of S-adenosylhomocysteine by LuxS in bacteria
-
physiological function
-
isoleucyl-tRNA synthetase (IleRS) is responsible for decoding of isoleucine codons in all three domains of life. Besides isoleucine, IleRS also activates non-cognate valine with a discrimination factor as low as 200 and thus it requires editing to enhance accuracy of isoleucyltRNAIle (Ile-tRNAIle) synthesis. Enzyme IleRS is unusual among aminoacyl-tRNA synthetases in having a tRNA-dependent pre-transfer editing activity. The main tRNA-dependent pre-transfer editing pathway in ScIleRS is the enzyme-based aa-AMP hydrolysis. Specificity of the editing pathways, overview
-
physiological function
-
the single trypanosomal IleRS gene is essential for normal growth and for charging of cytosolic and mitochondrial tRNAIle
-
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
-
additional information
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in mupirocin-resistant strains, e.g. evolved strain C12 that carried several copies of ileS, the antibiotic resistance leads also to reduced growth rates, these can be restored by the organism via increased expression of the original mutant ileS gene, also improving fitness while maintaining resistance, a process of adaptation initiated by common amplifications and followed by later acquisition of rare point mutations. A point mutation in one copy relaxes selection and allows loss of defective ileS copies, overview. Model for genetic adaptation of cells to the growth limitation caused by their MupR, overview
additional information
-
thiaisoleucine-resistant parasites possess a mutation in the cytoplasmic isoleucyl-tRNA synthetase, mutational analysis, overview
additional information
a Rossmann fold peptide is loacted directly N-terminal to the strictly conserved HIGH motif. The class I IleRS Rossmann fold accommodates both synthetic and tRNA-dependent pretransfer hydrolysis pathways within the synthetic site. Residue Y59 acts as a gatekeeper of the IleRS synthetic site
additional information
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a Rossmann fold peptide is loacted directly N-terminal to the strictly conserved HIGH motif. The class I IleRS Rossmann fold accommodates both synthetic and tRNA-dependent pretransfer hydrolysis pathways within the synthetic site. Residue Y59 acts as a gatekeeper of the IleRS synthetic site
additional information
the simultaneous presence of Ile-tRNA and Ile-AMP can cause additional possibilities to proofreading mechanisms of the enzyme, existence of an additional activation step, formation of a new isoleucyl-AMP before the isoleucyl-tRNA is freed from the enzyme. The removal of Ile-tRNA is possible without the formation of Ile-AMP if both isoleucine and ATP are bound to the E-Ile-tRNA complex, but this route covers only 11% of the total formation of Ile-tRNA
additional information
three human mitochondrial aminoacyl-tRNA syntethases, namely leucyl-, valyl-, and isoleucyl-tRNA synthetase are able to improve both viability and bioenergetic proficiency of human transmitochondrial cybrid cells carrying pathogenic mutations in the mt-tRNAIle gene
additional information
-
three human mitochondrial aminoacyl-tRNA syntethases, namely leucyl-, valyl-, and isoleucyl-tRNA synthetase are able to improve both viability and bioenergetic proficiency of human transmitochondrial cybrid cells carrying pathogenic mutations in the mt-tRNAIle gene
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AIleRS
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mutant enzymes IleRS(C922S) and AIleRS with replacement of Cys922 through Ala939 with a 33 amino acid peptide unable to bind zinc. Mutant enzymes have altered zinc binding and aminoacylation activity
IleRS(C922S)
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mutant enzymes IleRS(C922S) and AIleRS with replacement of Cys922 through Ala939 with a 33 amino acid peptide unable to bind zinc. Mutant enzymes have altered zinc binding and aminoacylation activity
T243R
-
site-directed mutagenesis, the mutant retains tRNA-independent editing at a level identical to the WT enzyme and shows increased ATP hydrolysis compared to the wild-type enzyme
T243R/D342A
-
site-directed mutagenesis, the IleRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations
Y59F
site-directed mutagenesis, mutation of a conserved residue located within the active site of bacterial IleRS, directly adjacent to the binding site for the 3'-terminal hydroxyl group of tRNA, aminacylation activity is about 35fold reduced compared to the wild-type enzyme
Y59F/D342A
site-directed mutagenesis, the mutant activity is similar to the wild-type
Y59T
site-directed mutagenesis, mutation of a conserved residue located within the active site of bacterial IleRS, directly adjacent to the binding site for the 3'-terminal hydroxyl group of tRNA, Km and kcat values measured for Y59T are increased by 10fold and decreased by 5fold, respectively, for both isoleucine and valine substrates compared to the wild-type enzyme, aminacylation activity is about 12fold reduced
Y59T/D342A
site-directed mutagenesis, kinetic analysis of Y59F/D342A IleRS does not provide reliable results because of the very slow aminoacylation/misacylation
E708K
naturally occuring mutation found in a heterozygous patient, the mutation is at the junction of the catalytic core domain and the anticodon-binding domain, and is predicted to be disease-causing
P909L
naturally occuring mutation causing the recessive disorder CAGSSS, phenotype, overview
W607X
naturally occuring mutation found in a heterozygous patient, the mutation truncates the protein removing 405 amino acids and is expected to be severely pathogenic
L810F
-
naturally occuring mutation in the cytoplasmic IleRS responsible for thiaisoleucine-resistance in the parasite, phenotype, overview
P184T
-
naturally occuring mutation that restores fitness in mupirocin resistant strains
Q420H
-
naturally occuring mutation that restores fitness in mupirocin resistant strains
F227L
the naturally occuring mutation affects the muciprocin binding
H581L/L583H
site-directed mutagenesis, slightly reduced enzyme activity
K226T
the naturally occuring mutation affects the muciprocin binding
P187F
the naturally occuring mutation affects the muciprocin binding
Q612H
the naturally occuring mutation is involved in stabilizing the conformation of the catalytic loop containing the KMSKS motif
V588F
the naturally occuring mutation affects the Rossman fold and leads to low-level mupirocin resistance
V767D
the naturally occuring mutation affects the muciprocin binding
D334A
-
site-directed mutagenesis, the post-transfer editing-defective mutant of SgIleRS displays the similar rates of aminoacylation and AMP formation in the presence of valine, exhibiting a kAMP/kVal-tRNA ratio of 1.1. Stoichiometric ATP consumption in Val-tRNAIle synthesis demonstrates the lack of proofreading by D334A SgIleRS, arguing against hydrolysis of Val-AMP alongside aminoacylation within the synthetic site, SgIleRS naturally lacks tRNA-dependent pre-transfer editing
H319A
site-directed mutagenesis, Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain, but the mutant shows detectable editing activities against the cognate isoleucine, mechanism, overview
T223A
site-directed mutagenesis, Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain, but the mutant shows detectable editing activities against the cognate isoleucine, mechanism, overview
W227A
site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme
W227F
site-directed mutagenesis, the mutant shows editing activities which are unaltered compared to the wild-type enzyme
W227H
site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme
W227L
site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme
W227V
site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme
W227Y
site-directed mutagenesis, the mutant shows editing activities which are unaltered compared to the wild-type enzyme
D539A/W541A
-
catalytically inactive
T233P
-
site-directed mutagenesis, mutant ileS(T233P) allows tRNAIle mischarging while retaining wild-type Ile-tRNAIle synthesis activity. The growth rate of the ileS(T233P)strain is not significantly different from wild-type. The ileS(T233P) strain is observed to exhibit a significant defect in formation of environmentally resistant spores. The sporulation defect ranges from 3fold to 30fold and is due to a delay in activation of early sporulation genes. The loss of aminoacylation quality control in the ileS(T233P) strain results in the inability to compete with a wild-type strain under selective conditions that require sporulation
T233P
-
site-directed mutagenesis, mutant ileS(T233P) allows tRNAIle mischarging while retaining wild-type Ile-tRNAIle synthesis activity. The growth rate of the ileS(T233P)strain is not significantly different from wild-type. The ileS(T233P) strain is observed to exhibit a significant defect in formation of environmentally resistant spores. The sporulation defect ranges from 3fold to 30fold and is due to a delay in activation of early sporulation genes. The loss of aminoacylation quality control in the ileS(T233P) strain results in the inability to compete with a wild-type strain under selective conditions that require sporulation
-
D342A
-
site-directed mutagenesis, the IleRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations
D342A
site-directed mutagenesis, the mutant exhibits slightly reduced aminoacylation activity compared to the wild-type enzyme, the post-transfer editing deficient D342A IleRS accumulates AMP by pretransfer editing and by tRNA misacylation when the noncognate aa-AMP evades this hydrolytic reaction, neither wild-type nor D342A IleRS significantly deacylates Ile-tRNAIle under steady-state conditions
G590D
-
pseudomonic-acid resistant mutant MBT10, with a Gly590 to aspartic acid transition
G590D
-
pseudomonic-acid resistant mutant MBT10, with a Gly590 to aspartic acid transition
-
D333A
site-directed mutagenesis, solution-based Val-AMP hydrolysis is 25fold slower than the rate of AMP formation assigned to editing in mutant D333A ScIleRS, non-enzymatic hydrolysis only weakly contributes to AMP accumulation
D333A
-
site-directed mutagenesis, solution-based Val-AMP hydrolysis is 25fold slower than the rate of AMP formation assigned to editing in mutant D333A ScIleRS, non-enzymatic hydrolysis only weakly contributes to AMP accumulation
-
additional information
-
mutant enzymes with altered metal-binding sites
additional information
-
pseudomonic acid resistant mutant strain PS102
additional information
-
pseudomonic acid-resistant mutant
additional information
-
pseudomonic acid-resistant mutant
-
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Kohda, D.; Yokoyama, S; Miyazawa, T.
Thermostable valyl-tRNA, isoleucyl-tRNA and methionyl-tRNA synthetases from an extreme thermophile Thermus thermophilus HB8. Protein structure and Zn2+ binding
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C-terminal zinc-containing peptide required for RNA recognition by a class I tRNA synthetase
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Proofreading in trans by an aminoacyl-tRNA synthetase. A model for single site editing by isoleucyl-tRNA synthetase
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Switching recognition of two tRNA synthetases with an amino acid swap in a designed peptide
Science
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Thiol ligation of two zinc atoms to a class I tRNA synthetase. Evidence for unshared thiols and role in amino acid binding and utilization
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1994
Escherichia coli
brenda
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Probing the metal binding sites of E. coli isoleucyl-tRNA synthetase
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Escherichia coli
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Analysis of the isoleucyl-tRNA synthetase reaction by total rate equation. Magnesium and spermidine in the tRNA kinetics
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210
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Escherichia coli, Escherichia coli B / ATCC 11303
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Evidence for distinct locations for metal binding sites in two closely related class I tRNA synthetases
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Zinc-dependent tRNA binding by a peptide element within a tRNA synthetase
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-
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