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2'-dATP + L-leucine + tRNALeu
2'-dAMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
3'-dATP + L-leucine + tRNALeu
3'-dAMP + diphosphate + L-leucyl-tRNALeu
8-azaadenosine 5'-triphosphate + L-leucine + tRNALeu
8-azaadenosine 5'-monophosphate + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
8-bromoadenosine 5'-triphosphate + L-leucine + tRNALeu
8-bromoadenosine 5'-monophosphate + diphosphate + L-leucyl-tRNALeu
8-methylaminoadenosine 5'-triphosphate + L-leucine + tRNALeu
8-methylaminoadenosine 5'-monophosphate + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
Adenosine 5'-O-(3-thio)triphosphate + L-leucine + tRNALeu
adenosine 5'-monophosphate + thiodiphosphate + L-leucyl-tRNALeu
Adenylyl beta,gamma-imido diphosphonate + L-leucine + tRNALeu
Adenylic acid + imido-diphosphate + L-leucyl-tRNALeu
AMP + diphosphate + Ile-tRNALeu
ATP + L-isoleucine + tRNALeu
-
-
-
?
AMP + diphosphate + L-leucyl-Pyrococcus horikoshii tRNALeu(GAG)
ATP + L-leucine + Pyrococcus horikoshii tRNALeu(GAG)
ATP + 2-butynylalanine + tRNALeu
AMP + diphosphate + 2-butynylalanyl-tRNALeu
-
aminoacylation by mutant T252Y
-
?
ATP + allylglycine + tRNALeu
AMP + diphosphate + allylglycyl-tRNALeu
-
aminoacylation by mutant T252Y
-
?
ATP + homoallylglycine + tRNALeu
AMP + diphosphate + homoallylglycyl-tRNALeu
-
aminoacylation by mutant T252Y
-
?
ATP + homopropargylglycine + tRNALeu
AMP + diphosphate + homopropargylglycyl-tRNALeu
-
aminoacylation by mutant T252Y
-
?
ATP + L-didehydroleucine + tRNALeu
AMP + diphosphate + didehydroleucyl-tRNALeu
-
reaction is catalyzed by mutant T252Y, not by wild-type
-
-
?
ATP + L-isoleucine + 2'-deoxaadenosine-tRNALeu
AMP + ?
-
2'-deoxyadenosine-tRNA clearly stimulates AMP production in the presence of isoleucine, but not the cognate leucine substrate
-
-
?
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
ATP + L-leucine + Natrialba magadii tRNALeu(CAA)
AMP + diphosphate + L-leucyl-Natrialba magadii tRNALeu(CAA)
ATP + L-leucine + Natrialba magadii tRNALeu(GAG)
AMP + diphosphate + L-leucyl-Natrialba magadii tRNALeu(GAG)
ATP + L-leucine + Pyrococcus horikoshii tRNALeu(GAG)
AMP + diphosphate + L-leucyl-Pyrococcus horikoshii tRNALeu(GAG)
ATP + L-leucine + tRNACAALeu
AMP + diphosphate + L-leucyl-tRNAUAALeu
ATP + L-leucine + tRNACAGLeu
AMP + diphosphate + L-leucyl-tRNACAGLeu
human cytoplasmic tRNACAGLeu (hctRNACAG)
-
-
?
ATP + L-leucine + tRNAGAGLeu
AMP + diphosphate + L-leucyl-tRNAGAGLeu
ATP + L-leucine + tRNAIle
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
ATP + L-leucine + tRNALeu from Aquifex aeolicus
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu from Escherichia coli
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu(GAG)
AMP + diphosphate + L-leucyl-tRNALeu(GAG)
ATP + L-leucine + tRNALeu(UAA)
AMP + diphosphate + L-leucyl-tRNALeu(UAA)
-
-
-
-
?
ATP + L-leucine + tRNALeu(UAG)
AMP + diphosphate + L-leucyl-tRNALeu(UAG)
Mesomycoplasma mobile
-
-
-
-
?
ATP + L-leucine + tRNALeu(UUR)
AMP + diphosphate + L-leucyl-tRNALeu(UUR)
-
leucyl-tRNA synthetase contacts tRNALeu(UUR) in the amino acid acid acceptor stem, the anticodon stem, and the D-loop
-
-
?
ATP + L-leucine + tRNALeuA35G
AMP + diphosphate + L-leucyl-tRNALeuA35G
-
-
-
-
?
ATP + L-leucine + tRNALeuA73
AMP + diphosphate + L-leucyl-tRNALeuA73
-
class II tRNALeu, recognition requires the discriminator base A73 and the long variable arm of appropriate stem length, especially the specific loop sequence A47CG47D and U47H at the base of the helix
-
?
ATP + L-leucine + tRNALeuA73G
AMP + diphosphate + L-leucyl-tRNALeuA73G
-
-
-
-
?
ATP + L-leucine + tRNALeuCUN
AMP + diphosphate + L-leucyl-tRNALeuCUN
ATP + L-leucine + tRNALeuGAG
AMP + diphosphate + L-leucyl-tRNALeuGAG
-
-
-
-
?
ATP + L-leucine + tRNALeuU73
AMP + diphosphate + L-leucyl-tRNALeuU73
-
class II tRNALeu isoacceptor, 17fold lower activity compared to tRNALeuA73
-
?
ATP + L-leucine + tRNALeuUUR
AMP + diphosphate + L-leucyl-tRNALeuUUR
ATP + L-leucine + tRNASer mutant
AMP + diphosphate + L-leucyl-tRNASer mutant
-
transplantation of both the discriminator base and the variable arm of tRNALeu are not sufficient to introduce leucylation activity to tRNASer, but additional insertion of additional a nucleotide into the D-loop, which is not involved in the direct interaction with the enzyme, converts tRNASer to an efficient leucine acceptor
-
?
ATP + L-leucine + tRNAUAALeu
AMP + diphosphate + L-leucyl-tRNACAALeu
ATP + L-leucine + tRNAUAALeu
AMP + diphosphate + L-leucyl-tRNAUAALeu
Mycoplasma mobile MmtRNAUAALeu (Mmt-RNAUAALeu)
-
-
?
ATP + L-methionine + tRNALeu
AMP + diphosphate + L-methionyl-tRNALeu
ATP + L-norisoleucine + tRNALeu
AMP + diphosphate + L-norisoleucyl-tRNALeu
-
aminoacylation by mutant T252Y
-
?
ATP + L-norvaline + tRNALeu
AMP + diphosphate + L-norvalyl-tRNALeu
ATP + L-oxonorvaline + tRNALeu
AMP + diphosphate + oxonorvalyl-tRNALeu
-
reaction is catalyzed by mutant T252Y, not by wild-type
-
-
?
L-isoleucyl-tRNALeu + H2O
t-RNALeu + isoleucine
-
-
editing activity
-
?
L-isoleucyl-tRNALeu + H2O
t-RNALeu + L-isoleucine
-
editing activity
-
?
tubercidin 5'-triphosphate + L-leucine + tRNALeu
tubercidin 5'-phosphate + diphosphate + L-leucyl-tRNALeu
additional information
?
-
3'-dATP + L-leucine + tRNALeu
3'-dAMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
3'-dATP + L-leucine + tRNALeu
3'-dAMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
3'-dATP + L-leucine + tRNALeu
3'-dAMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
8-bromoadenosine 5'-triphosphate + L-leucine + tRNALeu
8-bromoadenosine 5'-monophosphate + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
8-bromoadenosine 5'-triphosphate + L-leucine + tRNALeu
8-bromoadenosine 5'-monophosphate + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
Adenosine 5'-O-(3-thio)triphosphate + L-leucine + tRNALeu
adenosine 5'-monophosphate + thiodiphosphate + L-leucyl-tRNALeu
-
-
-
-
?
Adenosine 5'-O-(3-thio)triphosphate + L-leucine + tRNALeu
adenosine 5'-monophosphate + thiodiphosphate + L-leucyl-tRNALeu
-
-
-
-
?
Adenylyl beta,gamma-imido diphosphonate + L-leucine + tRNALeu
Adenylic acid + imido-diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
Adenylyl beta,gamma-imido diphosphonate + L-leucine + tRNALeu
Adenylic acid + imido-diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
AMP + diphosphate + L-leucyl-Pyrococcus horikoshii tRNALeu(GAG)
ATP + L-leucine + Pyrococcus horikoshii tRNALeu(GAG)
-
-
-
-
r
AMP + diphosphate + L-leucyl-Pyrococcus horikoshii tRNALeu(GAG)
ATP + L-leucine + Pyrococcus horikoshii tRNALeu(GAG)
-
-
-
-
r
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
-
-
-
-
?
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
-
-
-
-
?
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
-
mutant D345A, not the wild-type which performs only the misacetylation with isoleucine, but eliminates the incorrect isoleucyl-AMP
-
r
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
-
wild-type and CP1 domain mutant enzyme, the mischarged product can be edited by the wild-type enzyme, but not by a recombinant isolated CP1 domain
-
?
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
-
activity with mutant enzymes T252E and T252D, no activity with wild-type enzyme and with mutant enzyme T252G
-
-
?
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
-
the ratio of turnover number to KM-value for L-leucine is 1600fold higher than the ratio observed for L-isoleucine
-
-
?
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
-
-
-
-
?
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
-
-
-
-
?
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
-
-
-
?
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
-
the ratio of turnover number to KM-value for L-leucine is 3000fold higher than the ratio observed for L-isoleucine
-
-
?
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
-
-
-
-
?
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
-
activity with mutant enzyme D332A, no activity with wild-type full-length enzyme
-
-
?
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
-
-
-
?
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
-
mutant D419A, not the wild-type, which performs only the misacetylation with isoleucine, but eliminates the incorrect isoleucyl-AMP
-
r
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
mutant D345A, not the wild-type which performs only the misacetylation with isoleucine, but eliminates the incorrect isoleucyl-AMP
-
r
ATP + L-leucine + Natrialba magadii tRNALeu(CAA)
AMP + diphosphate + L-leucyl-Natrialba magadii tRNALeu(CAA)
-
-
-
-
?
ATP + L-leucine + Natrialba magadii tRNALeu(CAA)
AMP + diphosphate + L-leucyl-Natrialba magadii tRNALeu(CAA)
-
-
-
-
?
ATP + L-leucine + Natrialba magadii tRNALeu(GAG)
AMP + diphosphate + L-leucyl-Natrialba magadii tRNALeu(GAG)
-
highest activity
-
-
?
ATP + L-leucine + Natrialba magadii tRNALeu(GAG)
AMP + diphosphate + L-leucyl-Natrialba magadii tRNALeu(GAG)
-
highest activity
-
-
?
ATP + L-leucine + Pyrococcus horikoshii tRNALeu(GAG)
AMP + diphosphate + L-leucyl-Pyrococcus horikoshii tRNALeu(GAG)
-
100% activity
-
-
r
ATP + L-leucine + Pyrococcus horikoshii tRNALeu(GAG)
AMP + diphosphate + L-leucyl-Pyrococcus horikoshii tRNALeu(GAG)
-
100% activity
-
-
r
ATP + L-leucine + tRNACAALeu
AMP + diphosphate + L-leucyl-tRNAUAALeu
Mesomycoplasma mobile
Mycoplasma mobile tRNACAALeu (MmtRNACAALeu) and mutat derivatives
-
-
?
ATP + L-leucine + tRNACAALeu
AMP + diphosphate + L-leucyl-tRNAUAALeu
Mesomycoplasma mobile ATCC 43663 / 163K / NCTC 11711
Mycoplasma mobile tRNACAALeu (MmtRNACAALeu) and mutat derivatives
-
-
?
ATP + L-leucine + tRNAGAGLeu
AMP + diphosphate + L-leucyl-tRNAGAGLeu
Aquifex aeolicus tRNAGAGLeu (AatRNAGAGLeu)
-
-
?
ATP + L-leucine + tRNAGAGLeu
AMP + diphosphate + L-leucyl-tRNAGAGLeu
Escherichia coli tRNAGAGLeu (Ect-RNAGAGLeu)
-
-
?
ATP + L-leucine + tRNAGAGLeu
AMP + diphosphate + L-leucyl-tRNAGAGLeu
Pyrococcus horikoshii tRNAGAGLeu (PhtRNAGAGLeu)
-
-
?
ATP + L-leucine + tRNAGAGLeu
AMP + diphosphate + L-leucyl-tRNAGAGLeu
Pyrococcus horikoshii tRNAGAGLeu (PhtRNAGAGLeu)
-
-
?
ATP + L-leucine + tRNALeu
?
-
esterifies L-leucine to the cognate tRNA in the initial step of protein biosynthesis
-
-
?
ATP + L-leucine + tRNALeu
?
-
mitochondrial enzyme is involved in protein synthesis and mRNA splicing
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
enzyme activity only appears when both gene products, of leuS and leuS', coexist
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
the cross-species-specific recognition occurs at the alpha-subunit, tRNALeu substrates from Escherichia coli and Aquifex aeolicus
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
tRNALeu from Aquifex aeolicus and Escherichia coli, native and recombinant wild-type, the recombinant isolated beta-subunit is inactive in catalysis
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
two-step reaction, the beta-subunit alone is responsible for cognate tRNA recognition, enzyme activity requires both subunits
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
two distinct domains of the beta subunit of Aquifex aeolicus leucyl-tRNA synthetase are involved in tRNA binding as revealed by a three-hybrid selection
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
recombinant tRNALeu substrate, two peptides of eight and nine amino acid residues in the domain located in the alpha subunit are essential for the enzymes activity
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
the enzyme hydrolyzes mischarged tRNAs through a post-transfer editing mechanism, the enzyme from Aquifex aeolicus edits the complete set of aminoacylated tRNAs generated by the three enzymes, leucyl-, isoleucyl-, and valyl-tRNA synthetases: Ile-tRNAIle, Val-tRNAIle, ValtRNAVal, Thr-tRNAVal, and Ile-tRNALeu, model of a primitive editing system containing a composite minihelix carrying the triple leucine, isoleucine, and valine identity mimicking the primitive tRNA precursor, overview
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
recognition of tRNALeu by the leucyl-tRNA synthetase (LeuRS) is studied by RNA probing and mutagenesis. Results show that the base A73, the core structure of tRNA formed by the tertiary interactions U8-A14, G18-U55 and G19-C56, and the orientation of the variable arm are critical elements for tRNALeu aminoacylation. Although dispensable for aminoacylation, the anticodon arm carries discrete editing determinants that are required for stabilizing the conformation of the post-transfer editing state and for promoting translocation of the tRNA acceptor arm from the synthetic to the editing site
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
apart from the homologous substrate the enzyme is able to aminoacylate pure E. coli tRNALeu
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
apart from the homologous substrate the enzyme is able to aminoacylate pure E. coli tRNALeu
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
Drosophila sp. (in: flies)
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
r
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
r
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
mutant T252A edits correctly charged Leu-tRNALeu
-
r
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
the connecting peptide CP1 domain is crucial for the editing function
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
the peptide bond between Glu292 and Ala293 in the large connecting polypeptide CP1 is essential for activity
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
tRNALeu substrates from Escherichia coli and Aquifex aeolicus
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
two-step reaction, the connecting peptide CP1 domain is crucial for the editing function
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
two-step reaction, the first step is reversible, the second is not, tRNA discrimination by a double-sieve mechansim
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
it is proposed that the enzyme uses a lock-and-key mechanism to recognize and discriminate the amino acids
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
two functions of the enzyme in splicing and aminoacylation in vivo, overview
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
a two step reaction, the first of which is reversible, overview, the unique inserted leucine-specific domain of LeuRS is required for aminoacylation and not amino acid editing, the domain interacts with the tRNA during amino acid activation and/or tRNA aminoacylation, it might aid the dynamic translocation process that moves tRNA from the aminoacylation to the editing complex, overview
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
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, some positions are idiosyncratic to LeuRS including a conserved arginine conferring amino acid substrate recognition, it complements other sites in the amino acid binding pocket of the editing active site of Escherichia coli LeuRS, including Thr252 and Val338, the latter is second to the first, which collectively fine-tune amino acid specificity to confer fidelity, editing mechanism, residues Arg249, Asp251, Thr252, Met336, and Val338 are involved, overview
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
L570 strongly impacts aminoacylation in two ways: it affects both amino acid discrimination and tRNA binding, overview
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
the editing domain called CP1 is required for hydrolyzing the incorrectly misaminoacylated noncognate amino acids Ile and Val, the beta-strands, which link the CP1 domain to the aminoacylation core of LeuRS, are required for editing of mischarged tRNALeu, hydrolytic activity is also enhanced by inclusion of short flexible peptides, called hinges, at the end of both LeuRS beta-strands, overview
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
substrate is tRNALeuTAA, overexpressed in and purified from Escherichia coli
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
chloroplastic enzyme: high specificity towards tRNAs, in contrast the cytoplasmic enzyme recognizes tRNAs from the bleached mutant and from yeast, but also some tRNALeu isoacceptors from E. coli
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
tRNAs from Homo sapiens and Giardia lamblia
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
tRNALeu substrate from Escherichia coli, 2-step reaction, the first step is reversible, while the second step is not
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
human cytosolic leucyl-tRNA synthetase is one component of a macromolecular aminoacyl-tRNA synthetase complex. The C-terminal peptide of hcLeuRS is critical for the interaction with hcArgRS and the interaction in the multi-tRNA synthetase complex
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
human mitochondrial LeuRS achieves high aminoacylation fidelity without a functional editing active site, representing a rare example of a class I aminoacyl-tRNA synthetase that does not proofread its products, K600 strongly impacts aminoacylation in two ways: it affects both amino acid discrimination and tRNA binding, overview
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
Mesomycoplasma mobile
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
Mesomycoplasma mobile
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
Mesomycoplasma mobile ATCC 43663 / 163K / NCTC 11711
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
a complex between prolyl-tRNA synthetase, ProRS, and LeuRS in Methanothermobacter thermautotrophicus enhances tRNAPro aminoacylation, overview
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
cytoplasmic enzyme shows less strict specificity towards tRNA than the chloroplastic enzyme
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
a two step reaction, the C-terminal domain recognizes the long variable arm of tRNALeu for aminoacylation, and the so-called editing domain deacylates incorrectly formed Ile-tRNALeu, structural superposition of tRNAIle onto the LeuRS-tRNALeu complex indicated that Ile911, Lys912, and Glu913 of the LeuRS C-terminal domain clash with U20 of tRNAIle, which is bulged out as compared to the corresponding nucleotide of tRNALeu, mechanism for prevention of misediting, overview
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
r
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
possibly the yeast mitochondria have evolved to tolerate lower levels of fidelity in protein synthesis or have developed alternate mechanisms to enhance discrimination of leucine from non-cognate amino acids that can be misactivated by leucyl-tRNA synthetase
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
two functions of the enzyme in splicing and aminoacylation in vivo, overview
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
a two step reaction, the first of which is reversible, aminoacylation and editing by LeuRS require migration of the tRNA acceptor stem end between the canonical aminoacylation core and a separate domain called CP1 that is responsible for amino acid editing, post-transfer editing mechanism., overview
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
LeuRS has a hydrolytic active site that resides in a discrete amino acid editing domain called CP1, LeuRS misactivates many non-leucine amino acids, including isoleucine, valine, methionine, and also structurally similar metabolic cellular intermediate, but the enzyme has an editing active site that is competent for post-transfer editing of mischarged tRNA
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
r
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
the editing active site hydrolytically cleaves the misactivated aminoacyl-adenylate, called pre-transfer editing, or the mischarged tRNA, called post-transfer editing
-
r
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
acceptor activity with Tritrichomonas augusta tRNA is 8-fold higher than with yeast tRNA and 25-fold higher than with E. coli tRNA
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
ATP + L-leucine + tRNALeu(GAG)
AMP + diphosphate + L-leucyl-tRNALeu(GAG)
-
-
-
-
?
ATP + L-leucine + tRNALeu(GAG)
AMP + diphosphate + L-leucyl-tRNALeu(GAG)
Mesomycoplasma mobile
-
-
-
-
?
ATP + L-leucine + tRNALeuCUN
AMP + diphosphate + L-leucyl-tRNALeuCUN
-
-
-
-
?
ATP + L-leucine + tRNALeuCUN
AMP + diphosphate + L-leucyl-tRNALeuCUN
-
-
-
-
?
ATP + L-leucine + tRNALeuUUR
AMP + diphosphate + L-leucyl-tRNALeuUUR
-
-
-
-
?
ATP + L-leucine + tRNALeuUUR
AMP + diphosphate + L-leucyl-tRNALeuUUR
-
-
-
-
?
ATP + L-leucine + tRNAUAALeu
AMP + diphosphate + L-leucyl-tRNACAALeu
Mesomycoplasma mobile
Mycoplasma mobile tRNAUAALeu (MmtRNAUAALeu) and mutat derivatives
-
-
?
ATP + L-leucine + tRNAUAALeu
AMP + diphosphate + L-leucyl-tRNACAALeu
Mesomycoplasma mobile ATCC 43663 / 163K / NCTC 11711
Mycoplasma mobile tRNAUAALeu (MmtRNAUAALeu) and mutat derivatives
-
-
?
ATP + L-methionine + tRNALeu
AMP + diphosphate + L-methionyl-tRNALeu
-
-
-
-
?
ATP + L-methionine + tRNALeu
AMP + diphosphate + L-methionyl-tRNALeu
-
mutant D345A, not the wild-type enzyme
-
r
ATP + L-methionine + tRNALeu
AMP + diphosphate + L-methionyl-tRNALeu
-
wild-type and CP1 domain mutant enzyme, the mischarged product can be edited by the wild-type enzyme, but not by a recombinant isolated CP1 domain
-
?
ATP + L-methionine + tRNALeu
AMP + diphosphate + L-methionyl-tRNALeu
-
mutant D419A, not the wild-type enzyme
-
r
ATP + L-norvaline + tRNALeu
AMP + diphosphate + L-norvalyl-tRNALeu
-
-
-
-
?
ATP + L-norvaline + tRNALeu
AMP + diphosphate + L-norvalyl-tRNALeu
-
aminoacylation by mutant T252Y
-
?
ATP + L-norvaline + tRNALeu
AMP + diphosphate + L-norvalyl-tRNALeu
-
-
-
?
tubercidin 5'-triphosphate + L-leucine + tRNALeu
tubercidin 5'-phosphate + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
tubercidin 5'-triphosphate + L-leucine + tRNALeu
tubercidin 5'-phosphate + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
tubercidin 5'-triphosphate + L-leucine + tRNALeu
tubercidin 5'-phosphate + diphosphate + L-leucyl-tRNALeu
-
-
-
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzymes forms also perform the reversible ATP-diphosphate exchange reaction, which corresponds to the first reaction step
-
?
additional information
?
-
-
aminoacylation of minihelices is strongly dependent on the presence of the A73 identity nucleotide and greatly stimulated by destabilization of the first base pair. Addition of RNA helices that mimic the anticodon domain stimulates minihelixLeu charging by alphabeta-LeuRS indicating possible domain-domain communication. MinihelixLeu cannot be misaminoacylated, perhaps because of the tRNA-independent pretransfer editing activity of alphabeta-LeuRS
-
-
?
additional information
?
-
-
isolated editing domain of leucyl-tRNA synthetase from the deep-rooted bacterium Aquifex aeolicus catalyzes the hydrolytic editing of both mischarged tRNALeu and minihelixLeu
-
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
-
leucine-dependent ATP-diphosphate exchange, leucine + ATP + enzyme/Ile-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
-
proteolytically derived 34 kDa peptide fragment has lost most of its aminoacylation activity, but retains the ATP-dihosphate exchnage activity, the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction, the enzyme has an editing function to correct misaminoacylation of tRNALeu by isoleucine and methionine, T252 is involved
-
?
additional information
?
-
-
fidelity of translation is dependent on the specificity of the aminoacyl-tRNA synthetases
-
?
additional information
?
-
-
Thr247 and Thr248 are two key residues in the Escherichia coli LeuRS editing active site and appear to collaborate in the hydrolytic cleavage mechanism
-
-
?
additional information
?
-
-
isolated LeuRS CP1 domain requires idiosyncratic adaptations to confer editing activity independent of the full-length enzyme, overview
-
-
?
additional information
?
-
the enzyme has evolved both tRNA-dependent pre- and post-transfer editing capabilities to ensure catalytic specificity
-
-
?
additional information
?
-
kinetic origin of substrate specificity in post-transfer editing by leucyl-tRNA synthetase, overview. Binding and catalysis is analyzed independently using cognate leucyl- and non-cognate norvalyl-tRNALeu and their non-hydrolyzable analogues. The amino acid part (leucine versus norvaline) of (mis)aminoacyl-tRNAs can contribute approximately 10fold to ground-state discrimination at the editing site, while the rate of deacylation of leucyl- and norvalyl-tRNALeu differs by about 104fold. Critical role for the A76 3'-OH group of the tRNALeu in post-transfer editing. Molecular dynamics simulations reveals that the wild-type enzyme, but not the T252A mutant, enforces leucine to adopt the side-chain conformation that promotes the steric exclusion of a putative catalytic water. Editing can be distiguished from the synthetic site, which relies on ground-state discrimination in amino acid selection
-
-
?
additional information
?
-
-
kinetic origin of substrate specificity in post-transfer editing by leucyl-tRNA synthetase, overview. Binding and catalysis is analyzed independently using cognate leucyl- and non-cognate norvalyl-tRNALeu and their non-hydrolyzable analogues. The amino acid part (leucine versus norvaline) of (mis)aminoacyl-tRNAs can contribute approximately 10fold to ground-state discrimination at the editing site, while the rate of deacylation of leucyl- and norvalyl-tRNALeu differs by about 104fold. Critical role for the A76 3'-OH group of the tRNALeu in post-transfer editing. Molecular dynamics simulations reveals that the wild-type enzyme, but not the T252A mutant, enforces leucine to adopt the side-chain conformation that promotes the steric exclusion of a putative catalytic water. Editing can be distiguished from the synthetic site, which relies on ground-state discrimination in amino acid selection
-
-
?
additional information
?
-
-
residues Y515 and Y520 outside the editing active site of CP1 domain of Giardia lamblia LeuRS are crucial for post-transfer editing by influencing the binding affinity with mischarged tRNALeu
-
-
?
additional information
?
-
-
measurement of ATP-PPi exchange activity by wild-type and mutant enzymes
-
-
?
additional information
?
-
-
substrate specificty with diverse class II tRNALeu isoacceptors and mutants, overview, no activity with tRNALeuG73 and C73, no activity with tRNALeu, tRNASer and tRNATyr from Escherichia coli and Saccharomyces cerevisiae, differences in the tertiary structure of tRNALeu and tRNASer play a key role for inactivity and therefore elimination of native tRNASer as leucine acceptor
-
?
additional information
?
-
-
activity with mitochondrial tRNA mutants associated with some human mitochondrion-related neuromuscular disorders
-
?
additional information
?
-
enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
LeuRS misactivates several non-cognate amino acids, e.g. Ile and Met as well as the non-standard amino acids norvaline and alpha-amino butyrate. It uses mainly pre-transfer editing to edit alpha-amino butyrate and a tRNA-dependent mechanism to edit norvaline, although both amino acids can be charged to tRNALeu, overview. Separation of the norvaline-editing pathways
-
-
?
additional information
?
-
Mesomycoplasma mobile
-
the enzyme maintains weak pretransfer editing activities
-
-
?
additional information
?
-
-
the enzyme maintains weak pre-transfer editing activities
-
-
?
additional information
?
-
-
leucine-dependent ATP-diphosphate exchange, leucine + ATP + enzyme/Ile-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
-
leucine-dependent ATP-diphosphate exchange, leucine + ATP + enzyme/Ile-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
-
wild-type, full-length enzyme deacylates the pre-formed Ile-tRNALeu
-
-
?
additional information
?
-
-
measurement of ATP-PPi exchange activity by wild-type and mutant enzymes
-
-
?
additional information
?
-
-
no substrates: dATP, GTP, dGTP
-
-
?
additional information
?
-
-
the LeuRS CP1 domain can also support group I intron RNA splicing in the yeast mitochondria, overview, the RDW peptide, a highly conserved peptide within an RDW-containing motif, is important for enzyme interactions, the RDW peptide is dynamic and forms unique sets of interactions with the aminoacylation and editing complexes, overview
-
-
?
additional information
?
-
-
leucine-dependent ATP-diphosphate exchange, leucine + ATP + enzyme/Ile-AMP-enzyme + diphosphate
-
-
?
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(2E)-3-(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)-1-phenylprop-2-en-1-one
-
-
(2E)-3-(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-7-yl)-1-phenylprop-2-en-1-one
-
-
(E)-[3-(1,3-dihydro-1-hydroxy-2,1-benzoxaborol-7-yl)]acrylic acid ethyl ester
-
-
1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl cyclohexylcarbamate
-
-
1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl phenylcarbamate
-
-
1-hydroxy-1,3-dihydro-2,1-benzoxaborole-7-carbaldehyde
-
-
1-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]-4-methylpentan-2-one
-
-
1-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]butan-2-one
-
-
1-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]pentan-2-one
-
-
2,1-benzoxaborol-1(3H)-ol
-
-
2,1-benzoxaborole-1,6(3H)-diol
-
-
2-(2,5-dimethylanilino)-5,6,7,8-tetrahydroquinazolin-4(3H)-one
residual activity compared to wild-type enzyme is 71%
2-(2-hydroxy-5-methylanilino)-3,5,6,7-tetrahydro-4H-cyclopenta[d]pyrimidin-4-one
residual activity compared to wild-type enzyme is 40%
2-(2-hydroxy-5-methylanilino)-6-propylpyrimidin-4(3H)-one
residual activity compared to wild-type enzyme is 93%
2-(2-hydroxy-5-methylanilino)quinazolin-4(3H)-one
residual activity compared to wild-type enzyme is 26%
2-(2-hydroxyanilino)-6-methylpyrimidin-4(3H)-one
residual activity compared to wild-type enzyme is 42%
2-(2-hydroxyanilino)pyrimidin-4(3H)-one
residual activity compared to wild-type enzyme is 37%
2-(2-hydroxyanilino)quinazolin-4(3H)-one
residual activity compared to wild-type enzyme is 36%
2-(3-hydroxy-4-methylanilino)-6-propylpyrimidin-4(3H)-one
residual activity compared to wild-type enzyme is 36%
2-(3-hydroxyanilino)-6-methylpyrimidin-4(3H)-one
residual activity compared to wild-type enzyme is 39%
2-(3-hydroxyanilino)quinazolin-4(3H)-one
residual activity compared to wild-type enzyme is 26%
2-(4-hydroxy-2-methylanilino)-5,6,7,8-tetrahydroquinazolin-4(3H)-one
residual activity compared to wild-type enzyme is 70%
2-(4-hydroxy-2-methylanilino)-6-(propan-2-yl)pyrimidin-4(3H)-one
residual activity compared to wild-type enzyme is 29%
2-(4-hydroxy-2-methylanilino)-6-methylpyrimidin-4(3H)-one
residual activity compared to wild-type enzyme is 61%
2-(4-hydroxy-2-methylanilino)-6-phenylpyrimidin-4(3H)-one
residual activity compared to wild-type enzyme is 94%
2-(4-hydroxyanilino)-6-methylpyrimidin-4(3H)-one
residual activity compared to wild-type enzyme is 28%
2-(5-chloro-2-hydroxyanilino)-6-propylpyrimidin-4(3H)-one
residual activity compared to wild-type enzyme is 86%
2-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]pentan-3-one
-
-
2-[3-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]propyl]-1H-isoindole-1,3(2H)-dione
-
-
3'-Amino-3'-deoxy adenosine 5'-triphosphate
-
-
3-(2-hydroxy-5-methylanilino)-1,2,4-triazin-5(4H)-one
residual activity compared to wild-type enzyme is 70%
3-(2-hydroxy-5-methylanilino)-6-methyl-1,2,4-triazin-5(4H)-one
residual activity compared to wild-type enzyme is 44%
3-(2-hydroxy-5-methylanilino)-6-phenyl-1,2,4-triazin-5(4H)-one
residual activity compared to wild-type enzyme is 36%
3-(2-hydroxyanilino)-6-methyl-1,2,4-triazin-5(4H)-one
residual activity compared to wild-type enzyme is 38%
3-(3-hydroxy-4-methylanilino)-6-methyl-1,2,4-triazin-5(4H)-one
residual activity compared to wild-type enzyme is 83%
3-(3-hydroxyanilino)-6-methyl-1,2,4-triazin-5(4H)-one
residual activity compared to wild-type enzyme is 40%
3-(3-hydroxyanilino)-6-phenyl-1,2,4-triazin-5(4H)-one
residual activity compared to wild-type enzyme is 57%
3-(4-hydroxy-2-methylanilino)-1,2,4-triazin-5(4H)-one
residual activity compared to wild-type enzyme is 51%
3-(4-hydroxy-2-methylanilino)-6-methyl-1,2,4-triazin-5(4H)-one
residual activity compared to wild-type enzyme is 70%
3-(4-hydroxyanilino)-6-methyl-1,2,4-triazin-5(4H)-one
residual activity compared to wild-type enzyme is 55%
3-(4-hydroxyanilino)-6-phenyl-1,2,4-triazin-5(4H)-one
residual activity compared to wild-type enzyme is 36%
3-(5-chloro-2-hydroxyanilino)-1,2,4-triazin-5(4H)-one
residual activity compared to wild-type enzyme is 45%
3-(5-chloro-2-hydroxyanilino)-6-methyl-1,2,4-triazin-5(4H)-one
residual activity compared to wild-type enzyme is 42%
3-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]-3-methylbutan-2-one
-
-
3-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]-4-methylpentan-2-one
-
-
3-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]butan-2-one
-
-
3-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]heptan-4-one
-
-
3-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]hexan-2-one
-
-
3-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]pentan-2-one
-
-
3-[(3-oxo-2,3-dihydro-1,2,4-triazin-5-yl)amino]benzoic acid
residual activity compared to wild-type enzyme is 69%
3-[(4-oxo-3,4-dihydroquinazolin-2-yl)amino]benzoic acid
residual activity compared to wild-type enzyme is 36%
3-[(6-methyl-3-oxo-2,3-dihydro-1,2,4-triazin-5-yl)amino]benzoic acid
residual activity compared to wild-type enzyme is 57%
3-[4-(2-oxopropyl)anilino]-6-phenyl-1,2,4-triazin-5(4H)-one
residual activity compared to wild-type enzyme is 52%
4-methyl-3-[(3-oxo-2,3-dihydro-1,2,4-triazin-5-yl)amino]benzoic acid
residual activity compared to wild-type enzyme is 65%
4-methyl-3-[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)amino]benzoic acid
residual activity compared to wild-type enzyme is 56%
4-[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)amino]benzoic acid
residual activity compared to wild-type enzyme is 70%
4-[(5-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)amino]benzoic acid
residual activity compared to wild-type enzyme is 71%
4-[(5-oxo-4,5-dihydro-1,2,4-triazin-3-yl)amino]benzoic acid
residual activity compared to wild-type enzyme is 70%
4-[(6-methyl-3-oxo-2,3-dihydro-1,2,4-triazin-5-yl)amino]benzoic acid
residual activity compared to wild-type enzyme is 64%
5-(2-hydroxy-4-methylanilino)-1,2,4-triazin-3(2H)-one
residual activity compared to wild-type enzyme is 73%
5-(2-hydroxy-5-methylanilino)-1,2,4-triazin-3(2H)-one
residual activity compared to wild-type enzyme is 70%
5-(2-hydroxyanilino)-1,2,4-triazin-3(2H)-one
residual activity compared to wild-type enzyme is 72%
5-(2-hydroxyanilino)-6-methyl-1,2,4-triazin-3(2H)-one
residual activity compared to wild-type enzyme is 67%
5-(4-hydroxy-2-methylanilino)-6-methyl-1,2,4-triazin-3(2H)-one
residual activity compared to wild-type enzyme is 72%
5-(4-hydroxyanilino)-1,2,4-triazin-3(2H)-one
residual activity compared to wild-type enzyme is 70%
5-(4-hydroxyanilino)-6-methyl-1,2,4-triazin-3(2H)-one
residual activity compared to wild-type enzyme is 55%
5-(5-chloro-2-hydroxy-phenylamino)-2H-[1,2,4]triazin-3-one
5-(5-chloro-2-hydroxy-phenylamino)-6-methyl-2H-[1,2,4]triazin-3-one
5-fluoro-1,3-dihydro-1-hydroxy-2,1-benzoxaborole
5-fluoro-2,1-benzoxaborol-1(3H)-ol
5-phenylamino-2H-[1,2,4]triazin-3-one
-
5-[(6-methyl-3-oxo-2,3-dihydro-1,2,4-triazin-5-yl)amino]benzene-1,3-dicarboxylic acid
residual activity compared to wild-type enzyme is 72%
6,8-dibenzyl-2-(4-methylphenyl)-4,7-dioxo-N-(prop-2-en-1-yl)hexahydro-2H-pyrazino[2,1-c][1,2,4]triazine-1(6H)-carboxamide
-
6-(2,2-dimethoxyethoxy)-2,1-benzoxaborol-1(3H)-ol
-
-
6-(2-methoxyethoxy)-2,1-benzoxaborol-1(3H)-ol
-
-
6-(3-hydroxypropyl)-2,1-benzoxaborol-1(3H)-ol
-
-
6-(benzyloxy)-2,1-benzoxaborol-1(3H)-ol
-
-
6-(cyclohexylmethoxy)-2,1-benzoxaborol-1(3H)-ol
-
-
6-(propan-2-yloxy)-2,1-benzoxaborol-1(3H)-ol
-
-
6-(pyridin-2-ylmethoxy)-2,1-benzoxaborol-1(3H)-ol
-
-
6-(quinolin-2-yloxy)-2,1-benzoxaborol-1(3H)-ol
-
-
6-butoxy-2,1-benzoxaborol-1(3H)-ol
-
-
6-dimethylaminopurine riboside 5'-triphosphate
-
-
6-ethoxy-2,1-benzoxaborol-1(3H)-ol
-
-
6-mercaptopurine riboside 5'-triphosphate
-
-
6-methylaminopurine riboside 5'-triphosphate
-
-
6-propoxy-2,1-benzoxaborol-1(3H)-ol
-
-
6-[(2-fluorobenzyl)oxy]-2,1-benzoxaborol-1(3H)-ol
-
-
6-[(3-hydroxypentan-2-yl)oxy]-2,1-benzoxaborol-1(3H)-ol
-
-
7-(3-hydroxypropyl)-2,1-benzoxaborol-1(3H)-ol
-
-
8-benzyl-6-[(4-chlorophenyl)methyl]-2-(4-methylphenyl)-4,7-dioxo-N-(prop-2-en-1-yl)hexahydro-2H-pyrazino[2,1-c][1,2,4]triazine-1(6H)-carboxamide
-
8-benzyl-N-([1,1'-biphenyl]-2-yl)-2-methyl-4,7-dioxo-6-(propan-2-yl)hexahydro-2H-pyrazino[2,1-c][1,2,4]triazine-1(6H)-carboxamide
-
adenine arabinoside 5'-triphosphate
-
-
adenyl(alpha,beta-methylene)triphosphonate
-
-
adenylyl(beta,gamma-imido)triphosphonate
-
-
adenylyl(beta,gamma-methylene)diphosphonate
-
-
Al3+
-
in vitro the enzyme is inhibited by 40% at 0.04 mM, Al3+ inhibits the enzyme in vivo and in vitro, quantitative analysis, in vivo acceptor activity of tRNALeu is decreased by 23% thereby the leucyl-tRNA synthetase activity is increased by 20%, overview
BC-LI-0186
-
the interaction between RagD and LRS is disrupted by compound BC-LI-0186 inhibitong the translocation of the enzyme to the lysosome
Cd2+
-
in presence of 0.1 mM Mg2+
ethyl (2E)-3-(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)prop-2-enoate
-
-
ethyl 2-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]-2-methylpropanoate
-
-
ethyl 2-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]butanoate
-
-
ethyl 2-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]propanoate
-
-
ethyl 3-(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)propanoate
-
-
ethyl 3-(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-7-yl)propanoate
-
-
ethyl [(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy](phenyl)acetate
-
-
ethyl [(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]acetate
-
-
methyl [(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]acetate
-
-
N,8-dibenzyl-6-[(4-hydroxyphenyl)methyl]-2-methyl-4,7-dioxohexahydro-2H-pyrazino[2,1-c][1,2,4]triazine-1(6H)-carboxamide
-
N-(4-fluorophenyl)-8-[(furan-2-yl)methyl]-2-methyl-4,7-dioxo-6-[3-[N'-(2,2,4,6,7-pentamethyl-2,3-dihydro-1-benzofuran-5-yl)carbamimidamido]propyl]hexahydro-2H-pyrazino[2,1-c][1,2,4]triazine-1(6H)-carboxamide
-
N-benzyl-8-butyl-2-(4-methylphenyl)-4,7-dioxo-6-(propan-2-yl)hexahydro-2H-pyrazino[2,1-c][1,2,4]triazine-1(6H)-carboxamide
-
N-benzyl-8-butyl-6-[(4-chlorophenyl)methyl]-2-(4-methylphenyl)-4,7-dioxohexahydro-2H-pyrazino[2,1-c][1,2,4]triazine-1(6H)-carboxamide
-
N-benzyl-8-[(furan-2-yl)methyl]-2-(4-methylphenyl)-4,7-dioxo-6-(propan-2-yl)hexahydro-2H-pyrazino[2,1-c][1,2,4]triazine-1(6H)-carboxamide
-
N-ethyl-2-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]acetamide
-
-
N-tert-butyl-2-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]acetamide
-
-
NaCl
-
no activity of isoform LeuRS1 is detected in NaCl solutions
O-[N-(L-norvalyl)sulfamoyl]adenosine
analogue to the reaction intermediate, non-hydrolyzable
Purine riboside 5'-triphosphate
-
-
tert-butyl [(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]acetate
-
-
tert-butyl [2-[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]ethyl]carbamate
-
-
Zn2+
-
in presence of 0.1 mM Mg2+
[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]acetaldehyde
-
-
[(1-hydroxy-1,3-dihydro-2,1-benzoxaborol-6-yl)oxy]acetic acid
-
-
[4-[(4-oxo-3,4-dihydroquinazolin-2-yl)amino]phenyl]acetic acid
residual activity compared to wild-type enzyme is 37%
[4-[(5-oxo-4,5-dihydro-1,2,4-triazin-3-yl)amino]phenyl]acetic acid
residual activity compared to wild-type enzyme is 72%
[4-[(6-methyl-5-oxo-4,5-dihydro-1,2,4-triazin-3-yl)amino]phenyl]acetic acid
residual activity compared to wild-type enzyme is 71%
5-(5-chloro-2-hydroxy-phenylamino)-2H-[1,2,4]triazin-3-one
binding mode, overview
5-(5-chloro-2-hydroxy-phenylamino)-2H-[1,2,4]triazin-3-one
residual activity compared to wild-type enzyme is 18%, binding mode, overview
5-(5-chloro-2-hydroxy-phenylamino)-6-methyl-2H-[1,2,4]triazin-3-one
binding mode, overview
5-(5-chloro-2-hydroxy-phenylamino)-6-methyl-2H-[1,2,4]triazin-3-one
residual activity compared to wild-type enzyme is 2.3%, binding mode, overview
5-fluoro-1,3-dihydro-1-hydroxy-2,1-benzoxaborole
-
i.e. AN2690, 0.1 mM, 5fold decrease in aminoacylation activity
5-fluoro-1,3-dihydro-1-hydroxy-2,1-benzoxaborole
-
i.e. AN2690, the editing active site is the proven target for the broad-spectrum drug. But the post-transfer editing by LeuRS is resistant to the broad-spectrum drug AN2690, AN2690 resistance and its possible mechanism, overview
5-fluoro-2,1-benzoxaborol-1(3H)-ol
-
AN-2690, antibiotic which specifically targets the editing active site of LeuRS
5-fluoro-2,1-benzoxaborol-1(3H)-ol
AN-2690, antibiotic which specifically targets the editing active site of LeuRS
AMP
-
-
ATP
-
at high concentration, the A293 mutants are ore sensitive
ATP
-
at high concentration, the mutants are more sensisitve than the wild-type enzyme
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
additional information
-
aminoacylation and editing reaction are resistant to inactivation by compound AN2690
-
additional information
-
development of a GlLeuRS-specific inhibitor for the treatment of giardiasis
-
additional information
inhibition by high levels of mono- and divalent cations
-
additional information
-
inhibition by high levels of mono- and divalent cations
-
additional information
design and synthesis of tetra-substituted hexahydro-4H-pyrazino[2,1-c][1,2,4]triazine-4,7(6H)-diones as beta-turn mimetics via tandem N-acyliminium cyclization using a parallel synthetic strategy involving both solid and solution-phase reactions. Construction of a 162-member library of tetra-substituted pyrazinotriazinediones with an average purity of 90% using a solid-phase parallel synthesis platform, and screening for the LRS-RagD interaction inhibition by the compounds, overview
-
additional information
derivatives of 5-phenylamino-2H-[1,2,4]triazin-3-one as leucyl-tRNA synthetase (LeuRS) inhibitors, docking study, overview. The inhibitory activity of some compounds against pathogenic LeuRS is 10fold higher compared to the human enzyme. Hydrogen bond-foming amino acids in active site of LeuRS are Phe97, Tyr99, Glu103, His109, Tyr113, Asp137, Ser631, Gly678, Glu680, His681, Gln714, Ile717, Lys759, and Ile760
-
additional information
-
derivatives of 5-phenylamino-2H-[1,2,4]triazin-3-one as leucyl-tRNA synthetase (LeuRS) inhibitors, docking study, overview. The inhibitory activity of some compounds against pathogenic LeuRS is 10fold higher compared to the human enzyme. Hydrogen bond-foming amino acids in active site of LeuRS are Phe97, Tyr99, Glu103, His109, Tyr113, Asp137, Ser631, Gly678, Glu680, His681, Gln714, Ile717, Lys759, and Ile760
-
additional information
derivatives of 5-phenylamino-2H-[1,2,4]triazin-3-one as leucyl-tRNA synthetase (LeuRS) inhibitors, docking study, overview. The inhibitory activity of some compounds against pathogenic LeuRS is 10fold higher compared to the human enzyme. Hydrogen bond-foming amino acids in active site of LeuRS are Phe97, Tyr99, Glu103, His109, Tyr113, Asp137, Ser631, Gly678, Glu680, His681, Gln714, Ile717, Lys759, and Ile760. No inhibition by 5-[(6-methyl-5-oxo-4,5-dihydro-1,2,4-triazin-3-yl)amino]cyclohexa-2,4-diene-1-carboxylic acid, 4-[(4-oxo-3,4,5,6,7,8-hexahydroquinazolin-2-yl)amino]benzoic acid, 2-(2-hydroxyanilino)-5,6,7,8-tetrahydroquinazolin-4(3H)-one, 4-[(6-oxo-4-propyl-1,6-dihydropyrimidin-2-yl)amino]benzoic acid, 2-(4-hydroxyanilino)-6-propylpyrimidin-4(3H)-one, 2-(2-hydroxyanilino)-6-propylpyrimidin-4(3H)-one, 2-(4-hydroxy-2-methylanilino)-6-propylpyrimidin-4(3H)-one, 2-(3-hydroxy-4-methylanilino)-6-propylpyrimidin-4(3H)-one, 3-(2-hydroxyanilino)-1,2,4-triazin-5(4H)-one, 3-(4-hydroxyanilino)-1,2,4-triazin-5(4H)-one, and 2-(2-hydroxyanilino)-3,5,6,7-tetrahydro-4H-cyclopenta[d]pyrimidin-4-one
-
additional information
-
derivatives of 5-phenylamino-2H-[1,2,4]triazin-3-one as leucyl-tRNA synthetase (LeuRS) inhibitors, docking study, overview. The inhibitory activity of some compounds against pathogenic LeuRS is 10fold higher compared to the human enzyme. Hydrogen bond-foming amino acids in active site of LeuRS are Phe97, Tyr99, Glu103, His109, Tyr113, Asp137, Ser631, Gly678, Glu680, His681, Gln714, Ile717, Lys759, and Ile760. No inhibition by 5-[(6-methyl-5-oxo-4,5-dihydro-1,2,4-triazin-3-yl)amino]cyclohexa-2,4-diene-1-carboxylic acid, 4-[(4-oxo-3,4,5,6,7,8-hexahydroquinazolin-2-yl)amino]benzoic acid, 2-(2-hydroxyanilino)-5,6,7,8-tetrahydroquinazolin-4(3H)-one, 4-[(6-oxo-4-propyl-1,6-dihydropyrimidin-2-yl)amino]benzoic acid, 2-(4-hydroxyanilino)-6-propylpyrimidin-4(3H)-one, 2-(2-hydroxyanilino)-6-propylpyrimidin-4(3H)-one, 2-(4-hydroxy-2-methylanilino)-6-propylpyrimidin-4(3H)-one, 2-(3-hydroxy-4-methylanilino)-6-propylpyrimidin-4(3H)-one, 3-(2-hydroxyanilino)-1,2,4-triazin-5(4H)-one, 3-(4-hydroxyanilino)-1,2,4-triazin-5(4H)-one, and 2-(2-hydroxyanilino)-3,5,6,7-tetrahydro-4H-cyclopenta[d]pyrimidin-4-one
-
additional information
-
enzyme drug inhibitor design and development based on the benzoxaborole structure, inhibitory potencies and effectiveness a anti-trypanosomal drugs, ligand, i.e. benzoxaborole-AMP, docking in the LeuRS homology model, overview
-
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Acidosis, Lactic
Correction for Li and Guan, "Human Mitochondrial Leucyl-tRNA Synthetase Corrects Mitochondrial Dysfunctions Due to the tRNA(Leu(UUR)) A3243G Mutation, Associated with Mitochondrial Encephalomyopathy, Lactic Acidosis, and Stroke-Like Symptoms and Diabetes".
Acidosis, Lactic
Human mitochondrial leucyl-tRNA synthetase corrects mitochondrial dysfunctions due to the tRNALeu(UUR) A3243G mutation, associated with mitochondrial encephalomyopathy, lactic acidosis, and stroke-like symptoms and diabetes.
Acidosis, Lactic
LARS2 Variants Associated with Hydrops, Lactic Acidosis, Sideroblastic Anemia, and Multisystem Failure.
Acidosis, Lactic
The expanding LARS2 phenotypic spectrum: HLASA, Perrault syndrome with leukodystrophy, and mitochondrial myopathy.
Anemia
Severe course with lethal hepatocellular injury and skeletal muscular dysgenesis in a neonate with infantile liver failure syndrome type 1 caused by novel LARS1 mutations.
Anemia, Sideroblastic
LARS2 Variants Associated with Hydrops, Lactic Acidosis, Sideroblastic Anemia, and Multisystem Failure.
Anemia, Sideroblastic
The expanding LARS2 phenotypic spectrum: HLASA, Perrault syndrome with leukodystrophy, and mitochondrial myopathy.
Carcinogenesis
Implication of leucyl-tRNA synthetase 1 (LARS1) over-expression in growth and migration of lung cancer cells detected by siRNA targeted knock-down analysis.
Carcinogenesis
Inactivation of LARS2, located at the commonly deleted region 3p21.3, by both epigenetic and genetic mechanisms in nasopharyngeal carcinoma.
Carcinoma, Non-Small-Cell Lung
Therapeutic effects of the novel Leucyl-tRNA synthetase inhibitor BC-LI-0186 in non-small cell lung cancer.
CHARGE Syndrome
Laser-capture micro dissection combined with next-generation sequencing analysis of cell type-specific deafness gene expression in the mouse cochlea.
Coma
Prognostic value of time-related Glasgow Coma Scale components in severe traumatic brain injury: a prospective evaluation with respect to 1-year survival and functional outcome.
Confusion
Homosexuality in ancient and modern Korea.
COVID-19
Instagram as a virtual art display for medical students.
Deafness
Biallelic variants in LARS2 and KARS cause deafness and (ovario)leukodystrophy.
Deafness
Characterization of a knock-in mouse model of the homozygous p.V37I variant in Gjb2.
Deafness
The expanding LARS2 phenotypic spectrum: HLASA, Perrault syndrome with leukodystrophy, and mitochondrial myopathy.
Diabetes Mellitus, Type 2
Evidence that the mitochondrial leucyl tRNA synthetase (LARS2) gene represents a novel type 2 diabetes susceptibility gene.
Diabetes Mellitus, Type 2
Genetic association analysis of LARS2 with type 2 diabetes.
Fetal Growth Retardation
Severe course with lethal hepatocellular injury and skeletal muscular dysgenesis in a neonate with infantile liver failure syndrome type 1 caused by novel LARS1 mutations.
Gram-Negative Bacterial Infections
An assessment of the genetic toxicology of novel boron-containing therapeutic agents.
Hearing Loss
LARS2 Variants Associated with Hydrops, Lactic Acidosis, Sideroblastic Anemia, and Multisystem Failure.
Hearing Loss
Laser-capture micro dissection combined with next-generation sequencing analysis of cell type-specific deafness gene expression in the mouse cochlea.
Hearing Loss
Mutations in LARS2, Encoding Mitochondrial Leucyl-tRNA Synthetase, Lead to Premature Ovarian Failure and Hearing Loss in Perrault Syndrome.
Hearing Loss
Novel Mutations in CLPP, LARS2, CDH23, and COL4A5 Identified in Familial Cases of Prelingual Hearing Loss.
Hearing Loss
The expanding LARS2 phenotypic spectrum: HLASA, Perrault syndrome with leukodystrophy, and mitochondrial myopathy.
Hearing Loss, Sensorineural
Marfanoid habitus is a nonspecific feature of Perrault syndrome.
Hypertension
Prevalence and perinatal outcomes of non-communicable diseases in pregnancy in a regional hospital in Haiti: A prospective cohort study.
Infections
Bacterial resistance to leucyl-tRNA synthetase inhibitor GSK2251052 develops during treatment of complicated urinary tract infections.
Infections
Directive clinique no 409 : Tests diagnostiques ftaux intra-utérins en cas d'infection virale chronique maternelle.
Infections
Discovery of a potent benzoxaborole-based anti-pneumococcal agent targeting leucyl-tRNA synthetase.
Infections
Recent development of leucyl-tRNA synthetase inhibitors as antimicrobial agents.
Kallmann Syndrome
Laser-capture micro dissection combined with next-generation sequencing analysis of cell type-specific deafness gene expression in the mouse cochlea.
leucine-trna ligase deficiency
Leucyl-tRNA synthetase deficiency systemically induces excessive autophagy in zebrafish.
Liver Failure
Deep phenotyping of MARS1 (interstitial lung and liver disease) and LARS1 (infantile liver failure syndrome 1) recessive multisystemic disease using Human Phenotype Ontology annotation: Overlap and differences. Case report and review of literature.
Liver Failure
Genotypic diversity and phenotypic spectrum of infantile liver failure syndrome type 1 due to variants in LARS1.
Liver Failure
Infantile Liver Failure Syndrome 1 associated with a novel variant of the LARS1 gene: Clinical, genetic, and functional characterization.
Liver Failure
Severe course with lethal hepatocellular injury and skeletal muscular dysgenesis in a neonate with infantile liver failure syndrome type 1 caused by novel LARS1 mutations.
Liver Failure
[Clinical feature and molecular diagnostic analysis of the first non-caucasian child with infantile liver failure syndrome type 1].
Liver Failure, Acute
Severe course with lethal hepatocellular injury and skeletal muscular dysgenesis in a neonate with infantile liver failure syndrome type 1 caused by novel LARS1 mutations.
Lung Diseases
A Leucyl-tRNA Synthetase Inhibitor with Broad-Spectrum Anti-Mycobacterial Activity.
Lung Neoplasms
Implication of leucyl-tRNA synthetase 1 (LARS1) over-expression in growth and migration of lung cancer cells detected by siRNA targeted knock-down analysis.
Lung Neoplasms
Therapeutic effects of the novel Leucyl-tRNA synthetase inhibitor BC-LI-0186 in non-small cell lung cancer.
Malaria
Recent development of leucyl-tRNA synthetase inhibitors as antimicrobial agents.
Mandibulofacial Dysostosis
Laser-capture micro dissection combined with next-generation sequencing analysis of cell type-specific deafness gene expression in the mouse cochlea.
MELAS Syndrome
Correction of the consequences of mitochondrial 3243A>G mutation in the MT-TL1 gene causing the MELAS syndrome by tRNA import into mitochondria.
MELAS Syndrome
Exploring the Ability of LARS2 Carboxy-Terminal Domain in Rescuing the MELAS Phenotype.
Migraine Disorders
Samuel Auguste Tissot (1728-1797). His research on migraine.
Mitochondrial Diseases
Biallelic variants in LARS2 and KARS cause deafness and (ovario)leukodystrophy.
Mitochondrial Encephalomyopathies
Correction for Li and Guan, "Human Mitochondrial Leucyl-tRNA Synthetase Corrects Mitochondrial Dysfunctions Due to the tRNA(Leu(UUR)) A3243G Mutation, Associated with Mitochondrial Encephalomyopathy, Lactic Acidosis, and Stroke-Like Symptoms and Diabetes".
Mitochondrial Encephalomyopathies
Human mitochondrial leucyl-tRNA synthetase corrects mitochondrial dysfunctions due to the tRNALeu(UUR) A3243G mutation, associated with mitochondrial encephalomyopathy, lactic acidosis, and stroke-like symptoms and diabetes.
Mitochondrial Myopathies
The expanding LARS2 phenotypic spectrum: HLASA, Perrault syndrome with leukodystrophy, and mitochondrial myopathy.
Muscular Diseases
The expanding LARS2 phenotypic spectrum: HLASA, Perrault syndrome with leukodystrophy, and mitochondrial myopathy.
Mycoses
Recent development of leucyl-tRNA synthetase inhibitors as antimicrobial agents.
Nasopharyngeal Carcinoma
Inactivation of LARS2, located at the commonly deleted region 3p21.3, by both epigenetic and genetic mechanisms in nasopharyngeal carcinoma.
Nasopharyngitis
Inactivation of LARS2, located at the commonly deleted region 3p21.3, by both epigenetic and genetic mechanisms in nasopharyngeal carcinoma.
Neoplasms
An In Vivo Gain-of-Function Screen Identifies the Williams-Beuren Syndrome Gene GTF2IRD1 as a Mammary Tumor Promoter.
Neoplasms
Avoir sa santé en main : le sentiment d'habilitation tel que perçu par les jeunes adultes souffrant d'un cancer avancé.
Neoplasms
Concept d'adaptation chez les conjoints de femmes iraniennes atteintes du cancer du sein: étude qualitative basée sur une approche phénoménologique.
Neoplasms
Connaissances, attitudes et croyances concernant le dépistage du cancer du col utérin dans le District d'Ajumako-Enyan-Essiam au Ghana.
Neoplasms
Degrés de collaboration perçus entre les patients atteints de cancer et leurs prestataires de soins pendant la radiothérapie.
Neoplasms
Élaboration d'un énoncé de position national sur la navigation des patients atteints de cancer au Canada.
Neoplasms
Implication of leucyl-tRNA synthetase 1 (LARS1) over-expression in growth and migration of lung cancer cells detected by siRNA targeted knock-down analysis.
Neoplasms
Leucyl-tRNA synthetase 1 is required for proliferation of TSC-null cells.
Neoplasms
Optimiser les soins des adultes âgés atteints de cancer et l'accompagnement de leurs proches: énoncé de position et contribution des infirmières canadiennes en oncologie.
Neoplasms
Plant tumour biocontrol agent employs a tRNA-dependent mechanism to inhibit leucyl-tRNA synthetase.
Neoplasms
Retour au travail de patients atteints de cancer.
Nephritis, Hereditary
Laser-capture micro dissection combined with next-generation sequencing analysis of cell type-specific deafness gene expression in the mouse cochlea.
Neurologic Manifestations
Biallelic mutations in LARS2 can cause Perrault syndrome type 2 with neurologic symptoms.
Onychomycosis
An antifungal agent inhibits an aminoacyl-tRNA synthetase by trapping tRNA in the editing site.
Pediatric Obesity
Prendre le virage des partenariats.
Primary Ovarian Insufficiency
Biallelic variants in LARS2 and KARS cause deafness and (ovario)leukodystrophy.
Primary Ovarian Insufficiency
LARS2 Variants Associated with Hydrops, Lactic Acidosis, Sideroblastic Anemia, and Multisystem Failure.
Primary Ovarian Insufficiency
Marfanoid habitus is a nonspecific feature of Perrault syndrome.
Primary Ovarian Insufficiency
Mutations in LARS2, Encoding Mitochondrial Leucyl-tRNA Synthetase, Lead to Premature Ovarian Failure and Hearing Loss in Perrault Syndrome.
Primary Ovarian Insufficiency
The expanding LARS2 phenotypic spectrum: HLASA, Perrault syndrome with leukodystrophy, and mitochondrial myopathy.
Squamous Cell Carcinoma of Head and Neck
Promoter methylation of cyclin A1 is associated with human papillomavirus 16 induced head and neck squamous cell carcinoma independently of p53 mutation.
Starvation
Glucose Starvation Blocks Translation at Multiple Levels.
Starvation
Glucose-dependent control of leucine metabolism by leucyl-tRNA synthetase 1.
Starvation
In vivo regulatory responses of four Escherichia coli operons which encode leucyl-tRNAs.
Starvation
Membrane association of leucyl-tRNA synthetase during leucine starvation in Escherichia coli.
Starvation
Mitochondrial leucine tRNA level and PTCD1 are regulated in response to leucine starvation.
Starvation
Regulation of the nuclear genes encoding the cytoplasmic and mitochondrial leucyl-tRNA synthetases of Neurospora crassa.
Starvation
Yeast proteinase yscB inactivates the leucyl tRNA synthetase in extracts of Saccharomyces cerevisiae.
Stroke
A video-game group intervention: Experiences and perceptions of adults with chronic stroke and their therapists: Intervention de groupe à l'aide de jeux vidéo : Expériences et perceptions d'adultes en phase chronique d'un accident vasculaire cérébral et de leurs ergothérapeutes.
Tuberculosis
A Leucyl-tRNA Synthetase Inhibitor with Broad-Spectrum Anti-Mycobacterial Activity.
Tuberculosis
A prokaryote and human tRNA synthetase provide an essential RNA splicing function in yeast mitochondria.
Tuberculosis
Crucial role of the C-terminal domain of Mycobacterium tuberculosis leucyl-tRNA synthetase in aminoacylation and editing.
Tuberculosis
Discovery of a Potent and Specific M. tuberculosis Leucyl-tRNA Synthetase Inhibitor: (S)-3-(Aminomethyl)-4-chloro-7-(2-hydroxyethoxy)benzo[c][1,2]oxaborol-1(3H)-ol (GSK656).
Tuberculosis
Discovery of novel antituberculosis agents among 3-phenyl-5-(1-phenyl-1H-[1,2,3]triazol-4-yl)-[1,2,4]oxadiazole derivatives targeting aminoacyl-tRNA synthetases.
Tuberculosis
Discovery of novel oral protein synthesis inhibitors of Mycobacterium tuberculosis that target leucyl-tRNA synthetase.
Tuberculosis
Discovery of potent anti-tuberculosis agents targeting leucyl-tRNA synthetase.
Tuberculosis
Dual-target inhibitors of mycobacterial aminoacyl-tRNA synthetases among N-benzylidene-N'-thiazol-2-yl-hydrazines.
Tuberculosis
Dual-targeted hit identification using pharmacophore screening.
Tuberculosis
First-Time-in-Human Study and Prediction of Early Bactericidal Activity for GSK3036656, a Potent Leucyl-tRNA Synthetase Inhibitor for Tuberculosis Treatment.
Tuberculosis
Identification of Mycobacterium tuberculosis leucyl-tRNA synthetase (LeuRS) inhibitors among the derivatives of 5-phenylamino-2H-[1,2,4]triazin-3-one.
Tuberculosis
In Vitro Susceptibility Testing of GSK656 against Mycobacterium Species.
Urinary Tract Infections
Bacterial resistance to leucyl-tRNA synthetase inhibitor GSK2251052 develops during treatment of complicated urinary tract infections.
Usher Syndromes
Laser-capture micro dissection combined with next-generation sequencing analysis of cell type-specific deafness gene expression in the mouse cochlea.
Waardenburg Syndrome
Laser-capture micro dissection combined with next-generation sequencing analysis of cell type-specific deafness gene expression in the mouse cochlea.
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0.16
8-azaadenosine 5'-triphosphate
-
-
1
8-bromoadenosine 5'-triphosphate
0.07
8-Methylaminoadenosine 5'-triphosphate
-
-
0.055
adenosine 5'-O-(3-thiotriphosphate)
-
-
0.002 - 0.0025
Ile-tRNALeu
-
1.034
L-didehydroleucine
-
mutant T252Y
0.0092 - 0.0173
L-isoleucyl-tRNALeu
0.01251 - 0.01643
L-leucyl-Pyrococcus horikoshii tRNALeu(GAG)
-
2.245
L-oxonorvaline
-
mutant T252Y
0.01101 - 0.01313
Natrialba magadii tRNALeu(CAA)
-
0.00335 - 0.00773
Natrialba magadii tRNALeu(GAG)
-
0.00074 - 0.0017
tRNACAGLeu
-
0.00012 - 0.0058
tRNAGAGLeu
-
0.0003 - 0.0014
tRNALeu from Aquifex aeolicus
-
0.00076 - 0.0015
tRNALeu from Escherichia coli
-
0.00032 - 0.0075
tRNALeu(GAG)
-
0.0013 - 0.0044
tRNALeu(UAA)
-
0.0076
tRNALeu(UAG)
Mesomycoplasma mobile
-
in 100 mM Tris-HCl (pH 7.8), 30 mM KCl, 12 mM MgCl2, 5 mM dithiothreitol, at 30°C
-
0.0179
tRNALeu(UUR)
-
-
-
0.0012
tRNALeuA35G
-
37°C, pH 7.8
-
0.00052
tRNALeuA73
-
wild-type tRNALeu, pH 7.5, 37°C
-
0.011
tRNALeuA73G
-
37°C, pH 7.8
-
0.0002 - 0.025
tRNALeuCUN
-
0.0003
tRNALeuGAG
-
pH 6.8, 65°C, recombinant wild-type enzyme
-
0.0047
tRNALeuU73
-
tRNALeu isoacceptor, pH 7.5, 37°C
-
0.000018 - 0.006
tRNALeuUUR
-
0.0014
tRNASer mutant
-
pH 7.5, 37°C
-
0.0015 - 0.0025
tRNAUAALeu
-
0.065
tubercidin 5'-triphosphate
-
-
additional information
additional information
-
1
8-bromoadenosine 5'-triphosphate
-
-
1
8-bromoadenosine 5'-triphosphate
-
3'-dATP, tubercidin triphosphate
0.08
ATP
-
mutant E292F, pH 7.8, 37°C
0.09
ATP
recombinant mitochondrial isozyme, pH 7.6, 37°C
0.1
ATP
-
mutants E292Q, E292D, and E292A, pH 7.8, 37°C
0.11
ATP
-
aminoacylation reaction, pH 7.8, 60°C
0.11
ATP
-
mutants E292D and E292K, pH 7.8, 37°C
0.112
ATP
-
65°C, wild-type enzyme
0.1123
ATP
-
pH 6.8, 65°C, recombinant wild-type enzyme
0.113
ATP
-
65°C, recombinant His6-tagged enzyme
0.22
ATP
-
37°C, pH 7.8, mutant enzyme T252E
0.228
ATP
-
recombinant enzyme complex, 65°C
0.23
ATP
-
37°C, pH 7.8, mutant enzyme T25D
0.24
ATP
-
37°C, pH 7.8, native enzyme
0.25
ATP
-
aminoacylation reaction, mutant enzyme, pH 7.8, 37°C
0.26
ATP
-
wild-type enzyme, pH 7.8, 37°C
0.28
ATP
-
recombinant enzyme
0.28
ATP
-
aminoacylation reaction, wild-type enzyme, pH 7.8, 37°C
0.296
ATP
-
pH 7.5, 65°C, mutant R106A
0.323
ATP
-
pH 7.5, 65°C, mutant R97A
0.33
ATP
-
mutant lacking residues Q281 to D294, 45°C
0.351
ATP
-
pH 7.5, 65°C, mutant V108A
0.36
ATP
-
ATP-diphosphate exchange reaction, pH 7.8, 37°C
0.362
ATP
-
pH 7.5, 65°C, mutant D98A
0.366
ATP
-
pH 7.5, 65°C, mutant K100A/Y109A
0.37
ATP
-
pH 7.5, 65°C, mutant N96A
0.373
ATP
-
pH 7.5, 65°C, mutant E114A
0.38
ATP
-
ATP-diphosphate exchange reaction, pH 7.8, 60°C
0.383
ATP
-
pH 7.5, 65°C, mutant T101A
0.472
ATP
-
pH 7.5, 65°C, mutant W103A
0.531
ATP
-
pH 7.5, 65°C, mutant K100A
0.537
ATP
-
pH 7.5, 65°C, mutant Y105A
0.547
ATP
-
pH 7.5, 65°C, mutant F119A
0.55
ATP
-
aminoacylation reaction, pH 7.8, 37°C
0.551
ATP
-
pH 7.5, 65°C, mutant D121A
0.578
ATP
-
pH 7.5, 65°C, wild-type enzyme
0.584
ATP
-
pH 7.5, 65°C, mutant K100A/Y105A
0.59 - 1
ATP
-
pH 7.5, 65°C, mutant Y109A
0.653
ATP
-
pH 8.2, 45°C, mutant W155A
0.675
ATP
-
pH 8.2, 45°C, mutant Q154A
0.683
ATP
-
pH 8.2, 45°C, mutant K170A
0.687
ATP
-
pH 8.2, 45°C, mutant K166A
0.688
ATP
-
wild-type, 45°C
0.698
ATP
-
pH 8.2, 45°C, mutant K148A
0.711
ATP
-
pH 8.2, 45°C, mutant S153A
0.725
ATP
-
37°C, pH 7.6, leucylation, DELTAChcLeuRS (a C-terminal 89-amino acid truncated enzyme form)
0.728
ATP
-
pH 8.2, 45°C, mutant K142A
0.772
ATP
-
pH 8.2, 45°C, mutant K141A
0.773
ATP
-
37°C, pH 7.6, leucylation, full-length enzyme
0.796
ATP
-
pH 7.5, 65°C, mutant I104A
0.812
ATP
-
pH 8.2, 45°C, mutant K139A
0.822
ATP
-
pH 8.2, 45°C, mutant K144A
0.834
ATP
-
pH 8.2, 45°C, mutant K152A
0.837
ATP
-
pH 7.5, 65°C, mutant E113A
0.99
ATP
-
recombinant mitochondrial isozyme mutant, 37°C
1.025
ATP
-
pH 8.2, 45°C, mutant D173A
1.157
ATP
-
pH 7.5, 65°C, mutant T118A
1.169
ATP
-
pH 8.2, 45°C, mutant E165A
1.308
ATP
-
37°C, pH 7.6, ATP-diphosphate exchange, full-length enzyme
1.349
ATP
-
37°C, pH 7.6, ATP-diphosphate exchange, DELTAChcLeuRS (a C-terminal 89-amino acid truncated enzyme form)
2.129
ATP
-
pH 8.2, 45°C, mutant E167A
2.177
ATP
-
pH 7.5, 65°C, mutant I115A
0.002
Ile-tRNALeu
mutant enzyme R185E, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C
-
0.0021
Ile-tRNALeu
wild type enzyme, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C
-
0.0024
Ile-tRNALeu
mutant enzyme R286E, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C
-
0.0025
Ile-tRNALeu
mutant enzyme E184R, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C
-
0.25
L-isoleucine
-
pH 7.5, 37°C
0.698
L-isoleucine
-
37°C
2.04
L-isoleucine
wild-type, pH 7.6, 30°C
2.8
L-isoleucine
-
ATP-diphosphate exchange reaction, mutant enzyme, pH 7.8, 37°C
3.3
L-isoleucine
mutant D399A, pH 7.6, 30°C
3.5
L-isoleucine
-
ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.8, 37°C
14
L-isoleucine
-
pH 7.5, 37°C
0.0092
L-isoleucyl-tRNALeu
-
wild-type, pH 7.5, 37°C
0.0122
L-isoleucyl-tRNALeu
-
mutant Y515A, pH 7.5, 37°C
0.0147
L-isoleucyl-tRNALeu
-
mutant Y520H, pH 7.5, 37°C
0.0173
L-isoleucyl-tRNALeu
-
mutant Y520A, pH 7.5, 37°C
0.008
L-Leu
-
-
0.05
L-Leu
-
adenylyl (beta,gamma-imido)diphosphonate
0.0011
L-leucine
-
-
0.0013
L-leucine
-
ATP-diphosphate exchange reaction, pH 7.8, 37°C
0.0015
L-leucine
-
wild-type enzyme, aminoacylation
0.0016
L-leucine
-
ATP-diphosphate exchange reaction, pH 7.8, 60°C
0.0016
L-leucine
-
mutant enzyme T252V, aminoacylation
0.002
L-leucine
-
mutant enzyme T252S, aminoacylation
0.0024
L-leucine
-
pH 8.2, 45°C, mutant K152A
0.0035
L-leucine
-
pH 8.2, 45°C, mutant Q154A
0.0036
L-leucine
-
mutant enzyme T252A, aminoacylation
0.00537
L-leucine
-
pH 7.5, 65°C, mutant N96A
0.0054
L-leucine
-
mutant Y515A, pH 8.2, 45°C
0.0054
L-leucine
-
mutant Y515E, pH 8.2, 45°C
0.0054
L-leucine
-
mutant Y520H, pH 8.2, 45°C
0.00555
L-leucine
-
pH 7.5, 65°C, mutant Y105A
0.00559
L-leucine
-
pH 7.5, 65°C, mutant I115A
0.00569
L-leucine
-
pH 7.5, 65°C, mutant I104A
0.0057
L-leucine
-
pH 7.5, 65°C, mutant K100A/Y109A
0.0058
L-leucine
-
37°C, pH 7.6, leucylation, DELTAChcLeuRS (a C-terminal 89-amino acid truncated enzyme form)
0.00581
L-leucine
-
pH 7.5, 65°C, mutant V108A
0.0059
L-leucine
-
mutant lacking residues Q281 to D294, 45°C
0.00592
L-leucine
-
pH 7.5, 65°C, wild-type enzyme
0.00592
L-leucine
-
pH 7.5, 65°C, mutant D98A
0.006
L-leucine
-
aminoacylation reaction, pH 7.8, 60°C
0.006
L-leucine
-
pH 6.8, 65°C, recombinant wild-type enzyme
0.006
L-leucine
-
mutant Y520A, pH 8.2, 45°C
0.0061
L-leucine
-
wild-type, pH 8.2, 45°C
0.00618
L-leucine
-
pH 7.5, 65°C, mutant E113A
0.00623
L-leucine
-
pH 7.5, 65°C, mutant E114A
0.0063
L-leucine
-
pH 7.5, 65°C, mutant K100A/Y105A
0.00636
L-leucine
-
pH 7.5, 65°C, mutant T118A
0.0064
L-leucine
-
aminoacylation reaction, pH 7.8, 37°C
0.0064
L-leucine
-
65°C, recombinant His6-tagged enzyme
0.0064
L-leucine
-
65°C, wild-type enzyme
0.00721
L-leucine
-
pH 7.5, 65°C, mutant D121A
0.0075
L-leucine
-
37°C, pH 7.6, leucylation, full-length enzyme
0.0077
L-leucine
-
mutant lacking residues S295 to L304, 45°C
0.0077
L-leucine
-
mutant Y520E, pH 8.2, 45°C
0.008
L-leucine
-
mutant Y515K, pH 8.2, 45°C
0.0083
L-leucine
-
recombinant enzyme complex, 65°C
0.00843
L-leucine
-
isoform LeuRS1, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
0.00854
L-leucine
-
pH 7.5, 65°C, mutant R106A
0.00871
L-leucine
-
pH 7.5, 65°C, mutant W103A
0.00891
L-leucine
-
pH 7.5, 65°C, mutant K100A
0.009
L-leucine
-
wild-type, 45°C
0.00902
L-leucine
-
pH 7.5, 65°C, mutant Y109A
0.00927
L-leucine
-
pH 7.5, 65°C, mutant R97A
0.00984
L-leucine
-
pH 7.5, 65°C, mutant T101A
0.01
L-leucine
-
recombinant mitochondrial isozyme mutant, 37°C
0.0118
L-leucine
-
pH 7.5, 65°C, mutant F119A
0.0119
L-leucine
-
pH 8.2, 45°C, mutant W155A
0.012
L-leucine
-
mutant E292K, pH 7.8, 37°C
0.0124
L-leucine
-
pH 8.2, 45°C, mutant K148A
0.013
L-leucine
-
mutant E292S, pH 7.8, 37°C
0.0132
L-leucine
-
pH 8.2, 45°C, mutant K141A
0.014
L-leucine
-
mutant E292D, E292A, and E292F pH 7.8, 37°C
0.0141
L-leucine
-
pH 8.2, 45°C, mutant K170A
0.0145
L-leucine
-
pH 8.2, 45°C, mutant K142A
0.0147
L-leucine
-
pH 8.2, 45°C, mutant K166A
0.015
L-leucine
-
pH 7.5, 37°C
0.015
L-leucine
-
aminoacylation reaction, wild-type and mutant enzyme, pH 7.8, 37°C
0.015
L-leucine
-
recombinant and native enzyme
0.015
L-leucine
-
wild-type enzyme and mutant E292Q, pH 7.8, 37°C
0.0151
L-leucine
-
pH 8.2, 45°C, mutant K139A
0.0153
L-leucine
-
pH 8.2, 45°C, mutant K144A
0.0157
L-leucine
-
pH 8.2, 45°C, mutant E165A
0.0159
L-leucine
-
pH 8.2, 45°C, mutant S153A
0.0162
L-leucine
-
pH 8.2, 45°C, mutant E167A
0.0165
L-leucine
-
pH 8.2, 45°C, mutant D173A
0.018
L-leucine
-
mutant T252Y
0.019
L-leucine
-
37°C, pH 7.8, mutant enzyme T252E
0.019
L-leucine
-
37°C, pH 7.8, mutant enzyme T25D
0.02
L-leucine
-
37°C, pH 7.8, native enzyme
0.021
L-leucine
-
recombinant mitochondrial isozyme mutant, 37°C
0.024
L-leucine
wild-type, pH 7.6, 30°C
0.039
L-leucine
wild type enzyme, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C
0.045
L-leucine
recombinant mitochondrial isozyme, pH 7.6, 37°C
0.0456
L-leucine
-
pH 7.6, 37°C, wild-type enzyme
0.05
L-leucine
-
pH 7.6, 37°C, mutant D399A
0.052
L-leucine
-
ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.8, 37°C
0.064
L-leucine
-
37°C, pH 7.6, ATP-diphosphate exchange, DELTAChcLeuRS (a C-terminal 89-amino acid truncated enzyme form)
0.069
L-leucine
-
ATP-diphosphate exchange reaction, mutant enzyme, pH 7.8, 37°C
0.075
L-leucine
-
37°C, pH 7.6, ATP-diphosphate exchange, full-length enzyme
0.13
L-leucine
-
pH 7.5, 37°C
0.891
L-leucine
-
isoform LeuRS2, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
0.9
L-leucine
mutant D399A, pH 7.6, 30°C
0.01251
L-leucyl-Pyrococcus horikoshii tRNALeu(GAG)
-
isoform LeuRS1, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
0.01643
L-leucyl-Pyrococcus horikoshii tRNALeu(GAG)
-
isoform LeuRS2, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
0.983
L-methionine
-
37°C
6.2
L-methionine
-
ATP-diphosphate exchange reaction, mutant enzyme, pH 7.8, 37°C
7.5
L-methionine
-
ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.8, 37°C
0.01
Leu
-
-
0.01101
Natrialba magadii tRNALeu(CAA)
-
isoform LeuRS1, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
0.01313
Natrialba magadii tRNALeu(CAA)
-
isoform LeuRS2, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
0.00335
Natrialba magadii tRNALeu(GAG)
-
isoform LeuRS2, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
0.00773
Natrialba magadii tRNALeu(GAG)
-
isoform LeuRS1, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
0.00074
tRNACAGLeu
pH 7.8, 37°C, recombinant wild-type enzyme
-
0.0017
tRNACAGLeu
pH 7.8, 37°C, recombinant mutant R668A
-
0.00012
tRNAGAGLeu
pH 7.8, 37°C, recombinant mutant R703A
-
0.0003
tRNAGAGLeu
pH 7.8, 65°C, recombinant wild-type enzyme
-
0.00031
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R98A
-
0.00039
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R98E
-
0.00044
tRNAGAGLeu
pH 7.8, 37°C, recombinant mutant K692A
-
0.00052
tRNAGAGLeu
pH 7.8, 37°C, recombinant mutant K698A
-
0.0006
tRNAGAGLeu
pH 7.8, 37°C, recombinant mutant K699A
-
0.00065
tRNAGAGLeu
pH 7.8, 37°C, recombinant mutant K696A
-
0.00075
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R94A
-
0.00081
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R94A/R98A
-
0.00081
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R94E
-
0.00088
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R94E/R98E
-
0.002
tRNAGAGLeu
pH 7.8, 37°C, recombinant wild-type enzyme
-
0.0022
tRNAGAGLeu
pH 7.5, 37°C, recombinant wild-type enzyme
-
0.0022
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R668A/R672A
-
0.0024
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant K671A
-
0.0024
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R672A
-
0.0028
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R668A
-
0.0028
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R672E
-
0.0054
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R668E
-
0.0058
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R668E/R672E
-
0.0001
tRNALeu
-
-
0.0001
tRNALeu
-
37°C, pH 7.8, mutant enzyme N163A
0.00011
tRNALeu
-
37°C, pH 7.8, mutant enzyme K238A
0.00014
tRNALeu
-
37°C, pH 7.8, mutant enzyme G237D
0.00018
tRNALeu
-
37°C, pH 7.8, mutant enzyme L283F
0.0002
tRNALeu
-
37°C, pH 7.8, wilde-type enzyme
0.0002
tRNALeu
-
mutant R449K
0.00024
tRNALeu
-
37°C, pH 7.8, mutant enzyme K160N
0.00025
tRNALeu
-
37°C, pH 7.8, mutant enzyme Q234H
0.00029
tRNALeu
-
37°C, pH 7.8, mutant enzyme N152A
0.00038
tRNALeu
-
37°C, pH 7.8, mutant enzyme M159A
0.0005
tRNALeu
-
37°C, pH 7.8, mutant enzyme R94A
0.0005
tRNALeu
-
mutant W445Y
0.00051
tRNALeu
-
37°C, pH 7.8, mutant enzyme A156V
0.0006
tRNALeu
-
wild-type enzyme
0.00061
tRNALeu
-
37°C, pH 7.8
0.0007
tRNALeu
-
wild-type enzyme
0.0007
tRNALeu
-
mutant R451K
0.00073
tRNALeu
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.00085
tRNALeu
-
substrate from E. coli
0.0009
tRNALeu
-
mutant V338A
0.0011
tRNALeu
-
mutant enzyme V910A, at pH 8.2 and 30°C
0.0011
tRNALeu
-
wild type enzyme, at pH 8.2 and 30°C
0.0012
tRNALeu
-
mutant E292K, pH 7.8, 37°C
0.0012
tRNALeu
-
mutant enzyme L964A, at pH 8.2 and 30°C
0.0013
tRNALeu
-
mutant enzyme Q915K, at pH 8.2 and 30°C
0.0014
tRNALeu
-
37°C, pH 7.6, tRNALeu from calf liver, leucylation, DELTAChcLeuRS (a C-terminal 89-amino acid truncated enzyme form)
0.0014
tRNALeu
-
mutant enzyme V910W, at pH 8.2 and 30°C
0.0015
tRNALeu
-
aminoacylation reaction, wild-type enzyme, pH 7.8, 37°C
0.0016
tRNALeu
-
of Euglena gracilis
0.0016
tRNALeu
-
recombinant and native enzyme
0.00167
tRNALeu
-
full-length enzyme, pH 7.5, 37°C
0.00179
tRNALeu
-
truncation mutant DELTA911-913, pH 7.5, 37°C
0.0018
tRNALeu
-
mutant enzyme R921K, at pH 8.2 and 30°C
0.0019
tRNALeu
-
37°C, pH 7.6, tRNALeu from calf liver, leucylation, full-length enzyme
0.0019
tRNALeu
-
mutant enzyme Q915A, at pH 8.2 and 30°C
0.002
tRNALeu
-
pH 7.5, 37°C, recombinant LS-domain deletion mutant
0.0021
tRNALeu
-
mutant E292A, pH 7.8, 37°C
0.0024
tRNALeu
-
aminoacylation reaction, mutant enzyme, pH 7.8, 37°C
0.0024
tRNALeu
-
mutant E292S, pH 7.8, 37°C
0.0025
tRNALeu
-
wild-type enzyme, pH 7.8, 37°C
0.0025
tRNALeu
-
37°C, pH 7.8, mutant enzyme T25D
0.0026
tRNALeu
-
unfractionated substrate of E. coli
0.0026
tRNALeu
-
37°C, pH 7.8, native enzyme
0.0031
tRNALeu
-
mutant E292Q, pH 7.8, 37°C
0.0033
tRNALeu
-
37°C, pH 7.8, mutant enzyme T252E
0.0035
tRNALeu
-
37°C, pH 7.8, mutant enzyme V286stop
0.0035
tRNALeu
-
pH 8.2, 45°C, mutant K142A
0.0038
tRNALeu
-
pH 8.2, 45°C, mutant Q154A
0.004
tRNALeu
-
mutants E292D and E292F, pH 7.8, 37°C
0.004
tRNALeu
-
pH 8.2, 45°C, mutant S153A
0.0049
tRNALeu
-
pH 8.2, 45°C, mutant E167A
0.005
tRNALeu
-
pH 8.2, 45°C, mutant K148A
0.0051
tRNALeu
-
pH 8.2, 45°C, mutant K141A
0.0051
tRNALeu
-
pH 8.2, 45°C, mutant K152A
0.0051
tRNALeu
-
pH 8.2, 45°C, mutant K170A
0.0052
tRNALeu
-
pH 8.2, 45°C, mutant K144A
0.0052
tRNALeu
-
mutant enzyme R921A, at pH 8.2 and 30°C
0.0056
tRNALeu
-
pH 8.2, 45°C, recombinant mutant T341A
0.0057
tRNALeu
-
pH 8.2, 45°C, recombinant mutant D444A
0.0059
tRNALeu
-
pH 8.2, 45°C, mutant D173A
0.0059
tRNALeu
-
pH 8.2, 45°C, recombinant mutant T341R
0.0061
tRNALeu
-
wild-type, 45°C
0.0071
tRNALeu
-
pH 8.2, 45°C, mutant W155A
0.008
tRNALeu
-
pH 8.2, 45°C, recombinant mutant R338A
0.0081
tRNALeu
-
pH 8.2, 45°C, mutant K166A
0.0082
tRNALeu
-
mutant lacking residues S295 to L304, 45°C
0.0083
tRNALeu
-
pH 8.2, 45°C, mutant E165A
0.0083
tRNALeu
-
mutant enzyme L949A, at pH 8.2 and 30°C
0.0092
tRNALeu
-
mutant enzyme V910P, at pH 8.2 and 30°C
0.0093
tRNALeu
-
pH 8.2, 45°C, recombinant mutant DELTAESI/DELTAHsESI
0.0095
tRNALeu
-
37°C, pH 7.8, mutant enzyme Q269stop
0.0101
tRNALeu
-
mutant lacking residues Q281 to D294, 45°C
0.0114
tRNALeu
-
pH 8.2, 45°C, mutant K139A
0.014
tRNALeu
recombinant mitochondrial isozyme, pH 7.6, 37°C
0.0174
tRNALeu
-
mutant enzyme L964K, at pH 8.2 and 30°C
0.0273
tRNALeu
-
mutant enzyme L949K, at pH 8.2 and 30°C
0.0003
tRNALeu from Aquifex aeolicus
-
aminoacylation reaction, pH 7.8, 60°C
-
0.00038
tRNALeu from Aquifex aeolicus
-
aminoacylation reaction, pH 7.8, 37°C
-
0.0014
tRNALeu from Aquifex aeolicus
-
recombinant enzyme complex, 55°C
-
0.00076
tRNALeu from Escherichia coli
-
aminoacylation reaction, pH 7.8, 37°C
-
0.0013
tRNALeu from Escherichia coli
-
recombinant enzyme complex, 55°C
-
0.0015
tRNALeu from Escherichia coli
-
aminoacylation reaction, pH 7.8, 60°C
-
0.00032
tRNALeu(GAG)
-
65°C, recombinant His6-tagged enzyme
-
0.00045
tRNALeu(GAG)
-
65°C, wild-type enzyme
-
0.0075
tRNALeu(GAG)
Mesomycoplasma mobile
-
in 100 mM Tris-HCl (pH 7.8), 30 mM KCl, 12 mM MgCl2, 5 mM dithiothreitol, at 30°C
-
0.0013
tRNALeu(UAA)
-
pH 7.5, 37°C, wild-type enzyme
-
0.0013
tRNALeu(UAA)
-
wild-type enzyme, aminoacylation
-
0.0015
tRNALeu(UAA)
-
mutant enzyme T252V, aminoacylation
-
0.0017
tRNALeu(UAA)
-
mutant enzyme T252S, aminoacylation
-
0.0022
tRNALeu(UAA)
-
pH 7.5, 37°C, mutant enzyme T248V
-
0.0024
tRNALeu(UAA)
-
pH 7.5, 37°C, mutant enzyme T247S/T248S
-
0.0026
tRNALeu(UAA)
-
pH 7.5, 37°C, mutant enzyme T247V
-
0.0028
tRNALeu(UAA)
-
mutant enzyme T252A, aminoacylation
-
0.0036
tRNALeu(UAA)
-
pH 7.5, 37°C, mutant enzyme T247A/T248A
-
0.0044
tRNALeu(UAA)
-
pH 7.5, 37°C, mutant enzyme T247V/T248V
-
0.0002
tRNALeuCUN
-
Escherichia coli derived substrate, pH 7.0, 37°C, recombinant wild-type enzyme
-
0.0004
tRNALeuCUN
-
Escherichia coli derived substrate, pH 7.0, 37°C, recombinant wild-type enzyme
-
0.0017
tRNALeuCUN
-
Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant L570F
-
0.0018
tRNALeuCUN
-
Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutants K600L and K600R
-
0.002
tRNALeuCUN
-
Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant L570R
-
0.0022
tRNALeuCUN
-
Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant K600F
-
0.025
tRNALeuCUN
-
Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant L570K
-
0.000018
tRNALeuUUR
-
human derived substrate, pH 7.0, 37°C, recombinant mutant L570K
-
0.00016
tRNALeuUUR
-
human derived substrate, pH 7.0, 37°C, recombinant wild-type enzyme
-
0.0015
tRNALeuUUR
-
human derived substrate, pH 7.0, 37°C, recombinant mutant K600L
-
0.0017
tRNALeuUUR
-
human derived substrate, pH 7.0, 37°C, recombinant mutant L570F
-
0.004
tRNALeuUUR
-
human derived substrate, pH 7.0, 37°C, recombinant mutant K600R
-
0.004
tRNALeuUUR
-
human derived substrate, pH 7.0, 37°C, recombinant wild-type enzyme
-
0.006
tRNALeuUUR
-
human derived substrate, pH 7.0, 37°C, recombinant mutant K600F
-
0.0015
tRNAUAALeu
Mesomycoplasma mobile
pH 7.8, 30°C, recombinant wild-type enzyme
-
0.0016
tRNAUAALeu
pH 7.5, 37°C, recombinant wild-type enzyme
-
0.0017
tRNAUAALeu
Mesomycoplasma mobile
pH 7.8, 30°C, recombinant mutant K452A
-
0.0019
tRNAUAALeu
Mesomycoplasma mobile
pH 7.8, 30°C, recombinant mutant K452E
-
0.0023
tRNAUAALeu
Mesomycoplasma mobile
pH 7.8, 30°C, recombinant mutant K456A
-
0.0025
tRNAUAALeu
Mesomycoplasma mobile
pH 7.8, 30°C, recombinant mutant K456E
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics, wild-type and mutant enzymes
-
additional information
additional information
-
kinetics, wild-type and mutant enzymes
-
additional information
additional information
-
substrate specificity with diverse tRNALeu isoacceptors and mutants
-
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes
-
additional information
additional information
-
KM-values for hydrolytic editing of mischarged Ile-tRNALeu(GAG)
-
additional information
additional information
-
turnover numbers for tRNALeu(UUR) variants
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of chimeric mutants
-
additional information
additional information
-
kinetics of mischarging and post-transfer editing activities, overview
-
additional information
additional information
-
kinetics of recombinant His-tagged wild-type and mutant enzymes
-
additional information
additional information
-
kinetics of recombinant trunacted mutants, overview
-
additional information
additional information
-
prolyl-tRNA synthetase, ProRS, and LeuRS interaction kinetics
-
additional information
additional information
-
kcat/Km: 1 (ATP, wild-type), 1 (Leu, wild-type), 0.43 (ATP, mutant K587A), 0.42 (Leu, mutant K587A), 0.57 (ATP, mutant K588A), 0.37 (Leu, mutant K588A), 0.91 (ATP, mutant D603A), 0.94 (Leu, mutant D603A), 0.98 (ATP, mutant K606R), 0.99 (Leu, mutant K606R), 0.9 (ATP, mutant K606E), 0.99 (Leu, mutant K606E), 0.85 (ATP, mutant K606L), 0.98 (Leu, mutant K606L), 0.86 (ATP, mutant K606D), 0.83 (Leu, mutant K606D)
-
additional information
additional information
-
equilibrium kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetic constants of wild-type and D399A mutant of LeuRS in amino acid activation reaction with different amino acids, overview. Cytoplasmic LeuRS overexpressed in Escherichia coli exhibits the same kcat values as the one overexpressed in insect cells using in vitro transcribed tRNA
-
additional information
additional information
-
steady-state leucine activation and aminoacylation kinetics of GlLeuRS and its mutants, overview
-
additional information
additional information
determination of dissociation constants of Zn2+ from LeuRS enzymes
-
additional information
additional information
-
determination of dissociation constants of Zn2+ from LeuRS enzymes
-
additional information
additional information
dissociation constants of LeuRS and mutants from Escherichia coli for their cognate tRNAs. Reaction kinetics of EcLeuRS for Mycoplasma mobile MmtRNAUAALeu and mutant variants, kinetic constants of EcLeuRS, chimeric LeuRS and their mutants for tRNALeu in aminoacylation reaction and for AMP formation in the presence of Nva and MmtRNACAA, detailed overview
-
additional information
additional information
-
dissociation constants of LeuRS and mutants from Escherichia coli for their cognate tRNAs. Reaction kinetics of EcLeuRS for Mycoplasma mobile MmtRNAUAALeu and mutant variants, kinetic constants of EcLeuRS, chimeric LeuRS and their mutants for tRNALeu in aminoacylation reaction and for AMP formation in the presence of Nva and MmtRNACAA, detailed overview
-
additional information
additional information
dissociation constants of LeuRS and mutants from human cytoplasm for their cognate tRNAs
-
additional information
additional information
kinetic origin of substrate specificity in post-transfer editing by leucyl-tRNA synthetase, single-turnover measurements, overview
-
additional information
additional information
-
kinetic origin of substrate specificity in post-transfer editing by leucyl-tRNA synthetase, single-turnover measurements, overview
-
additional information
additional information
kinetics of aminoacylation reaction of recombinant wild-type and mutant enzymes, and apparent kinetic parameters for hydrolytic editing of mischarged Met-tRNALeu, overview
-
additional information
additional information
-
kinetics of aminoacylation reaction of recombinant wild-type and mutant enzymes, and apparent kinetic parameters for hydrolytic editing of mischarged Met-tRNALeu, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.08
L-didehydroleucine
-
mutant T252Y
0.19 - 1.52
L-isoleucyl-tRNALeu
0.00119 - 0.0418
L-leucyl-Pyrococcus horikoshii tRNALeu(GAG)
-
0.06
L-oxonorvaline
-
mutant T252Y
0.000418 - 0.0464
Natrialba magadii tRNALeu(CAA)
-
0.000668 - 0.064
Natrialba magadii tRNALeu(GAG)
-
0.0055 - 4.9
tRNAGAGLeu
-
0.006 - 1.5
tRNALeu from Aquifex aeolicus
-
0.003 - 0.4
tRNALeu from Escherichia coli
-
1.48 - 1.8
tRNALeu(GAG)
-
0.02 - 6.5
tRNALeu(UAA)
-
2
tRNALeu(UAG)
Mesomycoplasma mobile
-
in 100 mM Tris-HCl (pH 7.8), 30 mM KCl, 12 mM MgCl2, 5 mM dithiothreitol, at 30°C
-
0.31
tRNALeuA35G
-
37°C, pH 7.8
-
0.11
tRNALeuA73G
-
37°C, pH 7.8
-
1.5
tRNALeuGAG
-
pH 6.8, 65°C, recombinant wild-type enzyme
-
0.000018 - 0.14
tRNALeuUUR
-
additional information
additional information
-
0.094
ATP
-
recombinant enzyme complex, 65°C
0.22
ATP
-
recombinant mitochondrial isozyme mutant, 37°C
0.27
ATP
-
37°C, pH 7.6, leucylation, full-length enzyme
0.55
ATP
-
37°C, pH 7.6, leucylation, DELTAChcLeuRS (a C-terminal 89-amino acid truncated enzyme form)
0.74
ATP
-
37°C, pH 7.6, ATP-diphosphate exchange, DELTAChcLeuRS (a C-terminal 89-amino acid truncated enzyme form)
0.79
ATP
-
37°C, pH 7.6, ATP-diphosphate exchange, full-length enzyme
0.8
ATP
-
mutant E292K, pH 7.8, 37°C
0.8
ATP
recombinant mitochondrial isozyme, pH 7.6, 37°C
1.48
ATP
-
65°C, wild-type enzyme
1.5
ATP
-
mutant E292S, pH 7.8, 37°C
1.6
ATP
-
mutant enzyme, pH 7.8, 37°C
1.8
ATP
-
aminoacylation reaction, pH 7.8, 60°C
1.8
ATP
-
mutant E292F, pH 7.8, 37°C
1.81
ATP
-
pH 6.8, 65°C, recombinant wild-type enzyme
2
ATP
-
mutants E292Q and E292A, pH 7.8, 37°C
2.2
ATP
-
mutant E292D, pH 7.8, 37°C
2.2
ATP
-
65°C, recombinant His6-tagged enzyme
3
ATP
-
pH 7.5, 65°C, mutant K100A/Y105A
3.1
ATP
-
mutant lacking residues Q281 to D294, 45°C
3.1
ATP
-
mutant lacking residues S295 to L304, 45°C
3.1
ATP
-
wild-type, 45°C
3.3
ATP
-
ATP-diphosphate exchange reaction, pH 7.8, 37°C
3.6
ATP
-
recombinant enzyme
3.6
ATP
-
wild-type enzyme, pH 7.8, 37°C
3.9
ATP
-
aminoacylation reaction, pH 7.8, 37°C
4
ATP
-
pH 7.5, 65°C, mutant F119A
4.2
ATP
-
pH 7.5, 65°C, mutant V108A
4.3
ATP
-
pH 7.5, 65°C, mutant D98A
4.3
ATP
-
pH 7.5, 65°C, mutant E114A
4.6
ATP
-
pH 7.5, 65°C, mutant K100A
4.7
ATP
-
pH 7.5, 65°C, mutant D121A
4.8
ATP
-
37°C, pH 7.8, mutant enzyme T25D
4.8
ATP
-
pH 7.5, 65°C, mutant Y109A
4.9
ATP
-
wild-type enzyme, pH 7.8, 37°C
4.9
ATP
-
37°C, pH 7.8, mutant enzyme T252E
4.9
ATP
-
pH 7.5, 65°C, mutant K100A/Y109A
5
ATP
-
wild-type enzyme, pH 7.8, 37°C
5
ATP
-
37°C, pH 7.8, native enzyme
5
ATP
-
pH 7.5, 65°C, mutant T101A
5.1
ATP
-
pH 7.5, 65°C, mutant N96A
5.4
ATP
-
pH 7.5, 65°C, mutant R106A
5.5
ATP
-
pH 7.5, 65°C, mutant R97A
5.8
ATP
-
pH 7.5, 65°C, mutant E113A
6.5
ATP
-
pH 7.5, 65°C, mutant Y105A
6.8
ATP
-
pH 7.5, 65°C, wild-type enzyme
7.4
ATP
-
pH 7.5, 65°C, mutant I104A
7.4
ATP
-
pH 7.5, 65°C, mutant W103A
7.5
ATP
-
pH 8.2, 45°C, mutant Q154A
7.7
ATP
-
pH 7.5, 65°C, mutant T118A
8.1
ATP
-
pH 8.2, 45°C, mutant K152A
13.8
ATP
-
pH 7.5, 65°C, mutant I115A
14.5
ATP
-
ATP-diphosphate exchange reaction, pH 7.8, 60°C
29.8
ATP
-
pH 8.2, 45°C, mutant W155A
30.1
ATP
-
pH 8.2, 45°C, mutant S153A
31
ATP
-
pH 8.2, 45°C, mutant K170A
31.3
ATP
-
pH 8.2, 45°C, mutant E165A
31.5
ATP
-
pH 8.2, 45°C, mutant K141A
31.8
ATP
-
pH 8.2, 45°C, mutant K144A
32.1
ATP
-
pH 8.2, 45°C, mutant K148A
32.3
ATP
-
pH 8.2, 45°C, mutant K166A
33.2
ATP
-
pH 8.2, 45°C, mutant K139A
34.4
ATP
-
pH 8.2, 45°C, mutant D173A
36.2
ATP
-
pH 8.2, 45°C, mutant K142A
60.2
ATP
-
pH 8.2, 45°C, mutant E167A
7
Ile-tRNALeu
wild type enzyme, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C
-
7.4
Ile-tRNALeu
mutant enzyme R286E, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C
-
7.6
Ile-tRNALeu
mutant enzyme R185E, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C
-
8.8
Ile-tRNALeu
mutant enzyme E184R, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C
-
0.07
L-isoleucine
-
pH 7.5, 37°C
0.1
L-isoleucine
-
pH 7.5, 37°C
0.34
L-isoleucine
wild-type, pH 7.6, 30°C
0.51
L-isoleucine
mutant D399A, pH 7.6, 30°C
6.9
L-isoleucine
-
ATP-diphosphate exchange reaction, mutant enzyme, pH 7.8, 37°C
18
L-isoleucine
-
ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.8, 37°C
0.19
L-isoleucyl-tRNALeu
-
mutant Y515A, pH 7.5, 37°C
0.48
L-isoleucyl-tRNALeu
-
mutant Y520A, pH 7.5, 37°C
0.93
L-isoleucyl-tRNALeu
-
mutant Y520H, pH 7.5, 37°C
1.52
L-isoleucyl-tRNALeu
-
wild-type, pH 7.5, 37°C
0.00961
L-leucine
-
isoform LeuRS2, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
0.134
L-leucine
-
recombinant enzyme complex, 65°C
0.18
L-leucine
-
recombinant mitochondrial isozyme mutant, 37°C
0.23
L-leucine
-
recombinant mitochondrial isozyme mutant, 37°C
0.3
L-leucine
-
37°C, pH 7.6, leucylation, full-length enzyme
0.39
L-leucine
-
aminoacylation reaction, pH 7.8, 37°C
0.56
L-leucine
-
37°C, pH 7.6, leucylation, DELTAChcLeuRS (a C-terminal 89-amino acid truncated enzyme form)
0.563
L-leucine
-
isoform LeuRS1, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
0.8
L-leucine
-
mutant E292K, pH 7.8, 37°C
0.8
L-leucine
-
mutant enzyme T252A, aminoacylation
0.81
L-leucine
-
37°C, pH 7.6, ATP-diphosphate exchange, DELTAChcLeuRS (a C-terminal 89-amino acid truncated enzyme form)
0.82
L-leucine
-
37°C, pH 7.6, ATP-diphosphate exchange, full-length enzyme
1
L-leucine
-
mutant Y515E, pH 8.2, 45°C
1.1
L-leucine
-
mutant Y520H, pH 8.2, 45°C
1.4
L-leucine
-
aminoacylation reaction, pH 7.8, 60°C
1.4
L-leucine
-
pH 6.8, 65°C, recombinant wild-type enzyme
1.4
L-leucine
-
mutant Y520E, pH 8.2, 45°C
1.5
L-leucine
-
mutant enzyme, pH 7.8, 37°C
1.57
L-leucine
-
65°C, wild-type enzyme
1.6
L-leucine
-
mutant E292S, pH 7.8, 37°C
1.79
L-leucine
-
65°C, recombinant His6-tagged enzyme
1.8
L-leucine
-
mutant E292F, pH 7.8, 37°C
1.8
L-leucine
-
mutant Y515K, pH 8.2, 45°C
1.8
L-leucine
-
mutant Y520A, pH 8.2, 45°C
1.9
L-leucine
-
mutant E292A, pH 7.8, 37°C
2
L-leucine
-
pH 7.5, 37°C
2.1
L-leucine
wild-type, pH 7.6, 30°C
2.2
L-leucine
-
mutant E292Q, pH 7.8, 37°C
2.2
L-leucine
-
mutant T252Y
2.4
L-leucine
-
mutant E292D, pH 7.8, 37°C
2.6
L-leucine
-
mutant Y515A, pH 8.2, 45°C
2.7
L-leucine
recombinant mitochondrial isozyme, pH 7.6, 37°C
2.7
L-leucine
-
wild-type, pH 8.2, 45°C
2.8
L-leucine
-
mutant lacking residues Q281 to D294, 45°C
2.8
L-leucine
-
mutant lacking residues S295 to L304, 45°C
2.8
L-leucine
-
wild-type, 45°C
3
L-leucine
-
recombinant enzyme
3
L-leucine
-
wild-type enzyme, pH 7.8, 37°C
3.1
L-leucine
-
pH 7.5, 65°C, mutant E114A
3.1
L-leucine
-
pH 7.5, 65°C, mutant K100A/Y105A
3.2
L-leucine
-
pH 7.5, 65°C, mutant D98A
3.4
L-leucine
-
native enzyme
3.4
L-leucine
-
pH 7.5, 65°C, mutant F119A
3.5
L-leucine
-
ATP-diphosphate exchange reaction, pH 7.8, 37°C
3.8
L-leucine
-
pH 7.5, 65°C, mutant T101A
3.9
L-leucine
-
pH 7.5, 65°C, mutant K100A
4.1
L-leucine
-
pH 7.5, 65°C, mutant V108A
4.3
L-leucine
-
pH 7.5, 65°C, mutant Y105A
4.4
L-leucine
-
pH 7.5, 65°C, mutant N96A
4.6
L-leucine
-
37°C, pH 7.8, mutant enzyme T25D
4.6
L-leucine
-
pH 7.5, 65°C, mutant K100A/Y109A
4.7
L-leucine
-
pH 7.5, 65°C, mutant R106A
4.7
L-leucine
-
pH 7.5, 65°C, mutant Y109A
4.9
L-leucine
-
37°C, pH 7.8, mutant enzyme T252E
5.1
L-leucine
-
wild-type enzyme, pH 7.8, 37°C
5.1
L-leucine
-
37°C, pH 7.8, native enzyme
5.1
L-leucine
-
mutant enzyme T252S, aminoacylation
5.1
L-leucine
-
pH 7.5, 65°C, mutant R97A
5.1
L-leucine
-
pH 7.5, 65°C, mutant W103A
5.2
L-leucine
-
wild-type enzyme, pH 7.8, 37°C
5.2
L-leucine
-
pH 7.5, 65°C, mutant E113A
5.6
L-leucine
mutant D399A, pH 7.6, 30°C
5.6
L-leucine
-
pH 7.5, 65°C, mutant I104A
5.9
L-leucine
-
pH 8.2, 45°C, mutant Q154A
6
L-leucine
-
pH 7.5, 65°C, wild-type enzyme
6
L-leucine
-
pH 7.5, 65°C, mutant D121A
6.1
L-leucine
-
wild-type enzyme, aminoacylation
6.2
L-leucine
-
mutant enzyme T252V, aminoacylation
6.2
L-leucine
-
pH 8.2, 45°C, mutant K152A
8.1
L-leucine
-
pH 7.5, 65°C, mutant T118A
10.7
L-leucine
-
pH 7.5, 65°C, mutant I115A
11
L-leucine
-
pH 7.5, 37°C
15.5
L-leucine
-
ATP-diphosphate exchange reaction, pH 7.8, 60°C
25.8
L-leucine
-
pH 7.6, 37°C, wild-type enzyme
26.2
L-leucine
-
pH 7.6, 37°C, mutant D399A
28.1
L-leucine
-
pH 8.2, 45°C, mutant K170A
28.4
L-leucine
-
pH 8.2, 45°C, mutant K148A
28.7
L-leucine
-
pH 8.2, 45°C, mutant K166A
28.9
L-leucine
-
pH 8.2, 45°C, mutant K144A
29.7
L-leucine
-
pH 8.2, 45°C, mutant E165A
29.9
L-leucine
-
pH 8.2, 45°C, mutant K139A
31.7
L-leucine
-
pH 8.2, 45°C, mutant K142A
31.9
L-leucine
-
pH 8.2, 45°C, mutant W155A
32.5
L-leucine
-
pH 8.2, 45°C, mutant S153A
33.1
L-leucine
-
pH 8.2, 45°C, mutant K141A
36.3
L-leucine
-
pH 8.2, 45°C, mutant D173A
54.6
L-leucine
-
pH 8.2, 45°C, mutant E167A
73.7
L-leucine
wild type enzyme, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C
101
L-leucine
-
ATP-diphosphate exchange reaction, mutant enzyme, pH 7.8, 37°C
171
L-leucine
-
ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.8, 37°C
0.00119
L-leucyl-Pyrococcus horikoshii tRNALeu(GAG)
-
isoform LeuRS2, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
0.0418
L-leucyl-Pyrococcus horikoshii tRNALeu(GAG)
-
isoform LeuRS1, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
3.2
L-methionine
-
37°C
7.6
L-methionine
-
ATP-diphosphate exchange reaction, mutant enzyme, pH 7.8, 37°C
19
L-methionine
-
ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.8, 37°C
2 - 3.7
Leu
-
aminoacylation
20 - 50
Leu
-
ATP-diphosphate exchange reaction
2.05
Leu-tRNALeu
-
-
0.000418
Natrialba magadii tRNALeu(CAA)
-
isoform LeuRS2, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
0.0464
Natrialba magadii tRNALeu(CAA)
-
isoform LeuRS1, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
0.000668
Natrialba magadii tRNALeu(GAG)
-
isoform LeuRS2, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
0.064
Natrialba magadii tRNALeu(GAG)
-
isoform LeuRS1, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
0.56
tRNACAGLeu
pH 7.8, 37°C, recombinant mutant R668A
-
2.6
tRNACAGLeu
pH 7.8, 37°C, recombinant wild-type enzyme
-
0.0055
tRNAGAGLeu
pH 7.8, 37°C, recombinant mutant R703A
-
0.017
tRNAGAGLeu
pH 7.8, 37°C, recombinant mutant K696A
-
0.02
tRNAGAGLeu
pH 7.8, 37°C, recombinant wild-type enzyme
-
0.041
tRNAGAGLeu
pH 7.8, 37°C, recombinant mutant K692A
-
0.05
tRNAGAGLeu
pH 7.8, 37°C, recombinant mutant K699A
-
0.067
tRNAGAGLeu
pH 7.8, 37°C, recombinant mutant K698A
-
0.18
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R668E/R672E
-
0.19
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R94E/R98E
-
0.31
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R668A/R672A
-
0.53
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R672E
-
0.59
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R668E
-
0.67
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R94A/R98A
-
0.89
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R94E
-
1
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R98E
-
1.3
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R94A
-
1.4
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R668A
-
1.5
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R98A
-
1.5
tRNAGAGLeu
pH 7.8, 65°C, recombinant wild-type enzyme
-
4.8
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant K671A
-
4.8
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R672A
-
4.9
tRNAGAGLeu
pH 7.5, 37°C, recombinant wild-type enzyme
-
0.003
tRNALeu
-
37°C, pH 7.8, mutant enzyme Q269stop
0.028
tRNALeu
-
37°C, pH 7.6, tRNALeu from calf liver, leucylation, full-length enzyme
0.05
tRNALeu
-
mutant R449K
0.059
tRNALeu
-
37°C, pH 7.6, tRNALeu from calf liver, leucylation, DELTAChcLeuRS (a C-terminal 89-amino acid truncated enzyme form)
0.072
tRNALeu
-
37°C, pH 7.8, mutant enzyme N152A
0.12
tRNALeu
-
wild-type enzyme
0.12
tRNALeu
recombinant mitochondrial isozyme, pH 7.6, 37°C
0.177
tRNALeu
-
truncation mutant DELTA911-913, pH 7.5, 37°C
0.2
tRNALeu
-
mutant W445Y
0.2
tRNALeu
-
pH 8.2, 45°C, mutant K142A
0.2
tRNALeu
-
pH 8.2, 45°C, mutant K144A
0.31
tRNALeu
-
37°C, pH 7.8, mutant enzyme R94A
0.32
tRNALeu
-
37°C, pH 7.8, mutant enzyme V286stop
0.32
tRNALeu
-
37°C, pH 7.8, wild-type enzyme
0.331
tRNALeu
-
full-length enzyme, pH 7.5, 37°C
0.39
tRNALeu
-
37°C, pH 7.8, mutant enzyme G237D
0.39
tRNALeu
-
37°C, pH 7.8, mutant enzyme N163A
0.4
tRNALeu
-
37°C, pH 7.8, mutant enzyme Q234H
0.4
tRNALeu
-
mutant V338A
0.4
tRNALeu
-
mutant V338D
0.4
tRNALeu
-
mutant V338E
0.4
tRNALeu
-
mutant V338F
0.4
tRNALeu
-
mutant V338L
0.42
tRNALeu
-
37°C, pH 7.8, mutant enzyme K238A
0.47
tRNALeu
-
37°C, pH 7.8, mutant enzyme M159A
0.5
tRNALeu
-
37°C, pH 7.8
0.59
tRNALeu
-
37°C, pH 7.8, mutant enzyme L283F
0.6
tRNALeu
-
mutant R451K
0.66
tRNALeu
-
37°C, pH 7.8, mutant enzyme K160N
0.7
tRNALeu
-
pH 8.2, 45°C, recombinant mutant DELTAESI/DELTAHsESI
0.8
tRNALeu
-
mutant E292K, pH 7.8, 37°C
0.8
tRNALeu
-
pH 8.2, 45°C, mutant D173A
0.8
tRNALeu
-
pH 8.2, 45°C, mutant K141A
0.8
tRNALeu
-
pH 8.2, 45°C, mutant Q154A
0.84
tRNALeu
-
37°C, pH 7.8, mutant enzyme A156V
0.9
tRNALeu
-
pH 7.5, 37°C, recombinant LS-domain deletion mutant
1
tRNALeu
-
pH 8.2, 45°C, recombinant mutant T341A
1.1
tRNALeu
-
pH 8.2, 45°C, mutant S153A
1.1
tRNALeu
-
pH 8.2, 45°C, recombinant mutant D444A
1.1
tRNALeu
-
pH 8.2, 45°C, recombinant mutant T341R
1.2
tRNALeu
-
pH 8.2, 45°C, mutant E167A
1.3
tRNALeu
-
mutant enzyme, pH 7.8, 37°C
1.3
tRNALeu
-
pH 8.2, 45°C, mutant K152A
1.3
tRNALeu
-
pH 8.2, 45°C, recombinant mutant R338A
1.4
tRNALeu
-
pH 8.2, 45°C, mutant K170A
1.5
tRNALeu
-
pH 8.2, 45°C, mutant K139A
1.6
tRNALeu
-
mutant E292S, pH 7.8, 37°C
1.8
tRNALeu
-
mutant E292A, pH 7.8, 37°C
1.9
tRNALeu
-
mutant E292Q, pH 7.8, 37°C
1.9
tRNALeu
-
pH 8.2, 45°C, mutant K148A
2
tRNALeu
-
mutant E292F, pH 7.8, 37°C
2.2
tRNALeu
-
mutant E292D, pH 7.8, 37°C
2.4
tRNALeu
-
mutant enzyme V910P, at pH 8.2 and 30°C
2.5
tRNALeu
-
pH 8.2, 45°C, mutant W155A
2.7
tRNALeu
-
mutant lacking residues Q281 to D294, 45°C
2.7
tRNALeu
-
mutant lacking residues S295 to L304, 45°C
2.7
tRNALeu
-
wild-type, 45°C
2.8
tRNALeu
-
pH 8.2, 45°C, mutant E165A
2.8
tRNALeu
-
pH 8.2, 45°C, mutant K166A
2.9
tRNALeu
-
wild-type enzyme, pH 7.8, 37°C
3.4
tRNALeu
-
recombinant enzyme
3.9
tRNALeu
-
native enzyme
4.7
tRNALeu
-
37°C, pH 7.8, mutant enzyme T25D
5
tRNALeu
-
wild-type enzyme
5
tRNALeu
-
wild-type enzyme, pH 7.8, 37°C
5
tRNALeu
-
mutant enzyme L949K, at pH 8.2 and 30°C
5
tRNALeu
-
mutant enzyme Q915K, at pH 8.2 and 30°C
5.1
tRNALeu
-
wild-type enzyme, pH 7.8, 37°C
5.1
tRNALeu
-
37°C, pH 7.8, mutant enzyme T252E
5.1
tRNALeu
-
37°C, pH 7.8, native enzyme
5.6
tRNALeu
-
mutant enzyme L949A, at pH 8.2 and 30°C
7
tRNALeu
-
mutant enzyme V910A, at pH 8.2 and 30°C
7.2
tRNALeu
-
mutant enzyme L964A, at pH 8.2 and 30°C
7.8
tRNALeu
-
wild type enzyme, at pH 8.2 and 30°C
9.2
tRNALeu
-
mutant enzyme V910W, at pH 8.2 and 30°C
9.6
tRNALeu
-
pH 7.5, 37°C, recombinant wild-type enzyme
10.6
tRNALeu
-
mutant enzyme L964K, at pH 8.2 and 30°C
10.6
tRNALeu
-
mutant enzyme R921K, at pH 8.2 and 30°C
13.3
tRNALeu
-
mutant enzyme Q915A, at pH 8.2 and 30°C
13.6
tRNALeu
-
mutant enzyme R921A, at pH 8.2 and 30°C
0.006
tRNALeu from Aquifex aeolicus
-
recombinant enzyme complex, 55°C
-
0.39
tRNALeu from Aquifex aeolicus
-
aminoacylation reaction, pH 7.8, 37°C
-
1.5
tRNALeu from Aquifex aeolicus
-
aminoacylation reaction, pH 7.8, 60°C
-
0.003
tRNALeu from Escherichia coli
-
recombinant enzyme complex, 55°C
-
0.084
tRNALeu from Escherichia coli
-
aminoacylation reaction, pH 7.8, 37°C
-
0.4
tRNALeu from Escherichia coli
-
aminoacylation reaction, pH 7.8, 60°C
-
1.48
tRNALeu(GAG)
-
65°C, wild-type enzyme
-
1.59
tRNALeu(GAG)
-
65°C, recombinant His6-tagged enzyme
-
1.8
tRNALeu(GAG)
Mesomycoplasma mobile
-
in 100 mM Tris-HCl (pH 7.8), 30 mM KCl, 12 mM MgCl2, 5 mM dithiothreitol, at 30°C
-
0.02
tRNALeu(UAA)
-
pH 7.5, 37°C, mutant enzyme T247V/T248V
-
0.1
tRNALeu(UAA)
-
pH 7.5, 37°C, mutant enzyme T247A/T248A
-
0.8
tRNALeu(UAA)
-
pH 7.5, 37°C, mutant enzyme T247V
-
0.9
tRNALeu(UAA)
-
pH 7.5, 37°C, mutant enzyme T248V
-
1.6
tRNALeu(UAA)
-
mutant enzyme T252A, aminoacylation
-
3.2
tRNALeu(UAA)
-
pH 7.5, 37°C, wild-type enzyme
-
5.2
tRNALeu(UAA)
-
pH 7.5, 37°C, mutant enzyme T247S/T248S
-
6.1
tRNALeu(UAA)
-
wild-type enzyme, aminoacylation
-
6.3
tRNALeu(UAA)
-
mutant enzyme T252V, aminoacylation
-
6.5
tRNALeu(UAA)
-
mutant enzyme T252S, aminoacylation
-
0.35
tRNALeuCUN
-
Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant K600L
-
0.39
tRNALeuCUN
-
Escherichia coli derived substrate, pH 7.0, 37°C, recombinant wild-type enzyme
-
3
tRNALeuCUN
-
Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant K600F
-
3.2
tRNALeuCUN
-
Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant K600R
-
9.8
tRNALeuCUN
-
Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant L570K
-
14.5
tRNALeuCUN
-
Escherichia coli derived substrate, pH 7.0, 37°C, recombinant wild-type enzyme
-
21
tRNALeuCUN
-
Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant L570R
-
24
tRNALeuCUN
-
Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant L570F
-
0.000018
tRNALeuUUR
-
human derived substrate, pH 7.0, 37°C, recombinant mutant L570K
-
0.00016
tRNALeuUUR
-
human derived substrate, pH 7.0, 37°C, recombinant wild-type enzyme
-
0.0017
tRNALeuUUR
-
human derived substrate, pH 7.0, 37°C, recombinant mutant L570F
-
0.003
tRNALeuUUR
-
human derived substrate, pH 7.0, 37°C, recombinant mutant K600L
-
0.09
tRNALeuUUR
-
human derived substrate, pH 7.0, 37°C, recombinant wild-type enzyme
-
0.13
tRNALeuUUR
-
human derived substrate, pH 7.0, 37°C, recombinant mutant K600F
-
0.14
tRNALeuUUR
-
human derived substrate, pH 7.0, 37°C, recombinant mutant K600R
-
0.85
tRNAUAALeu
Mesomycoplasma mobile
pH 7.8, 30°C, recombinant mutant K456E
-
1.3
tRNAUAALeu
Mesomycoplasma mobile
pH 7.8, 30°C, recombinant mutant K456A
-
2.8
tRNAUAALeu
Mesomycoplasma mobile
pH 7.8, 30°C, recombinant mutant K452E
-
3.2
tRNAUAALeu
Mesomycoplasma mobile
pH 7.8, 30°C, recombinant mutant K452A
-
3.3
tRNAUAALeu
Mesomycoplasma mobile
pH 7.8, 30°C, recombinant wild-type enzyme
-
4.2
tRNAUAALeu
pH 7.5, 37°C, recombinant wild-type enzyme
-
additional information
additional information
-
kinetics, mutant enzymes
-
additional information
additional information
-
turnover number for hydrolytic editing of mischarged Ile-tRNALeu(GAG)
-
additional information
additional information
-
turnover numbers for tRNALeu(UUR) variants
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3100 - 3800
Ile-tRNALeu
-
0.016 - 0.165
L-isoleucyl-tRNALeu
0.0724 - 3.34
L-leucyl-Pyrococcus horikoshii tRNALeu(GAG)
-
0.0318 - 4.21
Natrialba magadii tRNALeu(CAA)
-
0.199 - 9.28
Natrialba magadii tRNALeu(GAG)
-
240
tRNALeu(GAG)
Mesomycoplasma mobile
-
in 100 mM Tris-HCl (pH 7.8), 30 mM KCl, 12 mM MgCl2, 5 mM dithiothreitol, at 30°C
-
260
tRNALeu(UAG)
Mesomycoplasma mobile
-
in 100 mM Tris-HCl (pH 7.8), 30 mM KCl, 12 mM MgCl2, 5 mM dithiothreitol, at 30°C
-
2.2
ATP
-
mutant lacking residues S295 to L304, 45°C
3.6
ATP
-
mutant lacking residues Q281 to D294, 45°C
4.5
ATP
-
wild-type, 45°C
5.2
ATP
-
pH 7.5, 65°C, mutant K100A/Y105A
6.4
ATP
-
pH 7.5, 65°C, mutant I115A
6.6
ATP
-
pH 7.5, 65°C, mutant T118A
6.9
ATP
-
pH 7.5, 65°C, mutant E113A
7.3
ATP
-
pH 7.5, 65°C, mutant F119A
8.1
ATP
-
pH 7.5, 65°C, mutant Y109A
8.5
ATP
-
pH 7.5, 65°C, mutant D121A
8.7
ATP
-
pH 7.5, 65°C, mutant K100A
9.3
ATP
-
pH 7.5, 65°C, mutant I104A
9.7
ATP
-
pH 8.2, 45°C, mutant K152A
11.1
ATP
-
pH 8.2, 45°C, mutant Q154A
11.5
ATP
-
pH 7.5, 65°C, mutant E114A
11.8
ATP
-
pH 7.5, 65°C, wild-type enzyme
11.9
ATP
-
pH 7.5, 65°C, mutant D98A
12
ATP
-
pH 7.5, 65°C, mutant V108A
12.1
ATP
-
pH 7.5, 65°C, mutant Y105A
13.1
ATP
-
pH 7.5, 65°C, mutant T101A
13.5
ATP
-
pH 7.5, 65°C, mutant K100A/Y109A
13.8
ATP
-
pH 7.5, 65°C, mutant N96A
15.7
ATP
-
pH 7.5, 65°C, mutant W103A
17
ATP
-
pH 7.5, 65°C, mutant R97A
18.2
ATP
-
pH 7.5, 65°C, mutant R106A
26.8
ATP
-
pH 8.2, 45°C, mutant E165A
28.3
ATP
-
pH 8.2, 45°C, mutant E167A
33.5
ATP
-
pH 8.2, 45°C, mutant D173A
38.7
ATP
-
pH 8.2, 45°C, mutant K144A
40.8
ATP
-
pH 8.2, 45°C, mutant K141A
40.9
ATP
-
pH 8.2, 45°C, mutant K139A
42.3
ATP
-
pH 8.2, 45°C, mutant S153A
45.4
ATP
-
pH 8.2, 45°C, mutant K170A
45.6
ATP
-
pH 8.2, 45°C, mutant W155A
46
ATP
-
pH 8.2, 45°C, mutant K148A
47
ATP
-
pH 8.2, 45°C, mutant K166A
49.7
ATP
-
pH 8.2, 45°C, mutant K142A
3100
Ile-tRNALeu
mutant enzyme R286E, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C
-
3300
Ile-tRNALeu
wild type enzyme, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C
-
3500
Ile-tRNALeu
mutant enzyme E184R, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C
-
3800
Ile-tRNALeu
mutant enzyme R185E, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C
-
0.16
L-isoleucine
wild-type, pH 7.6, 30°C
0.17
L-isoleucine
mutant D399A, pH 7.6, 30°C
0.016
L-isoleucyl-tRNALeu
-
mutant Y515A, pH 7.5, 37°C
0.028
L-isoleucyl-tRNALeu
-
mutant Y520A, pH 7.5, 37°C
0.063
L-isoleucyl-tRNALeu
-
mutant Y520H, pH 7.5, 37°C
0.165
L-isoleucyl-tRNALeu
-
wild-type, pH 7.5, 37°C
0.0108
L-leucine
-
isoform LeuRS2, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
0.181
L-leucine
-
mutant Y520E, pH 8.2, 45°C
0.185
L-leucine
-
mutant Y515E, pH 8.2, 45°C
0.203
L-leucine
-
mutant Y520H, pH 8.2, 45°C
0.225
L-leucine
-
mutant Y515K, pH 8.2, 45°C
0.3
L-leucine
-
mutant Y520A, pH 8.2, 45°C
0.442
L-leucine
-
wild-type, pH 8.2, 45°C
0.481
L-leucine
-
mutant Y515A, pH 8.2, 45°C
5.6
L-leucine
mutant D399A, pH 7.6, 30°C
66.8
L-leucine
-
isoform LeuRS1, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
77.9
L-leucine
-
mutant lacking residues S295 to L304, 45°C
94.3
L-leucine
wild-type, pH 7.6, 30°C
186
L-leucine
-
mutant lacking residues Q281 to D294, 45°C
286
L-leucine
-
pH 7.5, 65°C, mutant F119A
311
L-leucine
-
wild-type, 45°C
386
L-leucine
-
pH 7.5, 65°C, mutant T101A
438
L-leucine
-
pH 7.5, 65°C, mutant K100A
493
L-leucine
-
pH 7.5, 65°C, mutant K100A/Y105A
498
L-leucine
-
pH 7.5, 65°C, mutant E114A
521
L-leucine
-
pH 7.5, 65°C, mutant Y109A
524
L-leucine
-
pH 7.6, 37°C, mutant D399A
541
L-leucine
-
pH 7.5, 65°C, mutant D98A
550
L-leucine
-
pH 7.5, 65°C, mutant R106A
550
L-leucine
-
pH 7.5, 65°C, mutant R97A
565
L-leucine
-
pH 7.6, 37°C, wild-type enzyme
586
L-leucine
-
pH 7.5, 65°C, mutant W103A
706
L-leucine
-
pH 7.5, 65°C, mutant V108A
775
L-leucine
-
pH 7.5, 65°C, mutant Y105A
806
L-leucine
-
pH 7.5, 65°C, mutant K100A/Y109A
819
L-leucine
-
pH 7.5, 65°C, mutant N96A
839
L-leucine
-
pH 7.5, 65°C, mutant D121A
846
L-leucine
-
pH 7.5, 65°C, mutant E113A
984
L-leucine
-
pH 7.5, 65°C, mutant I104A
1013
L-leucine
-
pH 7.5, 65°C, wild-type enzyme
1277
L-leucine
-
pH 7.5, 65°C, mutant T118A
1686
L-leucine
-
pH 8.2, 45°C, mutant Q154A
1889
L-leucine
-
pH 8.2, 45°C, mutant K144A
1890
L-leucine
wild type enzyme, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C
1892
L-leucine
-
pH 8.2, 45°C, mutant E165A
1910
L-leucine
-
pH 7.5, 65°C, mutant I115A
1952
L-leucine
-
pH 8.2, 45°C, mutant K166A
1980
L-leucine
-
pH 8.2, 45°C, mutant K139A
1993
L-leucine
-
pH 8.2, 45°C, mutant K170A
2044
L-leucine
-
pH 8.2, 45°C, mutant S153A
2186
L-leucine
-
pH 8.2, 45°C, mutant K142A
2200
L-leucine
-
pH 8.2, 45°C, mutant D173A
2290
L-leucine
-
pH 8.2, 45°C, mutant K148A
2508
L-leucine
-
pH 8.2, 45°C, mutant K141A
2583
L-leucine
-
pH 8.2, 45°C, mutant K152A
2681
L-leucine
-
pH 8.2, 45°C, mutant W155A
3370
L-leucine
-
pH 8.2, 45°C, mutant E167A
0.0724
L-leucyl-Pyrococcus horikoshii tRNALeu(GAG)
-
isoform LeuRS2, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
3.34
L-leucyl-Pyrococcus horikoshii tRNALeu(GAG)
-
isoform LeuRS1, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
0.0318
Natrialba magadii tRNALeu(CAA)
-
isoform LeuRS2, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
4.21
Natrialba magadii tRNALeu(CAA)
-
isoform LeuRS1, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
0.199
Natrialba magadii tRNALeu(GAG)
-
isoform LeuRS2, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
9.28
Natrialba magadii tRNALeu(GAG)
-
isoform LeuRS1, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C
-
330
tRNACAGLeu
pH 7.8, 37°C, recombinant mutant R668A
-
3500
tRNACAGLeu
pH 7.8, 37°C, recombinant wild-type enzyme
-
30
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R668E/R672E
-
30
tRNAGAGLeu
pH 7.8, 37°C, recombinant mutant K696A
-
50
tRNAGAGLeu
pH 7.8, 37°C, recombinant mutant R703A
-
80
tRNAGAGLeu
pH 7.8, 37°C, recombinant mutant K699A
-
90
tRNAGAGLeu
pH 7.8, 37°C, recombinant mutant K692A
-
110
tRNAGAGLeu
pH 7.8, 37°C, recombinant wild-type enzyme
-
110
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R668E
-
130
tRNAGAGLeu
pH 7.8, 37°C, recombinant mutant K698A
-
140
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R668A/R672A
-
190
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R672E
-
220
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R94E/R98E
-
500
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R668A
-
830
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R94A/R98A
-
1100
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R94E
-
1700
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R94A
-
2000
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant K671A
-
2000
tRNAGAGLeu
pH 7.5, 37°C, recombinant mutant R672A
-
2230
tRNAGAGLeu
pH 7.5, 37°C, recombinant wild-type enzyme
-
2600
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R98E
-
4800
tRNAGAGLeu
pH 7.8, 65°C, recombinant mutant R98A
-
5000
tRNAGAGLeu
pH 7.8, 65°C, recombinant wild-type enzyme
-
38
tRNALeu
-
pH 8.2, 45°C, mutant K144A
57
tRNALeu
-
pH 8.2, 45°C, mutant K142A
73.2
tRNALeu
-
mutant lacking residues S295 to L304, 45°C
75.3
tRNALeu
-
pH 8.2, 45°C, recombinant mutant DELTAESI/DELTAHsESI
128.7
tRNALeu
-
mutant lacking residues Q281 to D294, 45°C
132
tRNALeu
-
pH 8.2, 45°C, mutant K139A
136
tRNALeu
-
pH 8.2, 45°C, mutant D173A
157
tRNALeu
-
pH 8.2, 45°C, mutant K141A
162.5
tRNALeu
-
pH 8.2, 45°C, recombinant mutant R338A
178.6
tRNALeu
-
pH 8.2, 45°C, recombinant mutant T341A
183.2
tRNALeu
-
mutant enzyme L949K, at pH 8.2 and 30°C
186.4
tRNALeu
-
pH 8.2, 45°C, recombinant mutant T341R
193
tRNALeu
-
pH 8.2, 45°C, recombinant mutant D444A
210
tRNALeu
-
pH 8.2, 45°C, mutant Q154A
245
tRNALeu
-
pH 8.2, 45°C, mutant E167A
255
tRNALeu
-
pH 8.2, 45°C, mutant K152A
260.9
tRNALeu
-
mutant enzyme V910P, at pH 8.2 and 30°C
275
tRNALeu
-
pH 8.2, 45°C, mutant K170A
275
tRNALeu
-
pH 8.2, 45°C, mutant S153A
337
tRNALeu
-
pH 8.2, 45°C, mutant E165A
346
tRNALeu
-
pH 8.2, 45°C, mutant K166A
352
tRNALeu
-
pH 8.2, 45°C, mutant W155A
380
tRNALeu
-
pH 8.2, 45°C, mutant K148A
442
tRNALeu
-
wild-type, 45°C
609.2
tRNALeu
-
mutant enzyme L964K, at pH 8.2 and 30°C
674.7
tRNALeu
-
mutant enzyme L949A, at pH 8.2 and 30°C
2615
tRNALeu
-
mutant enzyme R921A, at pH 8.2 and 30°C
3846
tRNALeu
-
mutant enzyme Q915K, at pH 8.2 and 30°C
5889
tRNALeu
-
mutant enzyme R921K, at pH 8.2 and 30°C
6000
tRNALeu
-
mutant enzyme L964A, at pH 8.2 and 30°C
6364
tRNALeu
-
mutant enzyme V910A, at pH 8.2 and 30°C
6571
tRNALeu
-
mutant enzyme V910W, at pH 8.2 and 30°C
7000
tRNALeu
-
mutant enzyme Q915A, at pH 8.2 and 30°C
7091
tRNALeu
-
wild type enzyme, at pH 8.2 and 30°C
340
tRNAUAALeu
Mesomycoplasma mobile
pH 7.8, 30°C, recombinant mutant K456E
-
600
tRNAUAALeu
Mesomycoplasma mobile
pH 7.8, 30°C, recombinant mutant K456A
-
1500
tRNAUAALeu
Mesomycoplasma mobile
pH 7.8, 30°C, recombinant mutant K452E
-
1900
tRNAUAALeu
Mesomycoplasma mobile
pH 7.8, 30°C, recombinant mutant K452A
-
2200
tRNAUAALeu
Mesomycoplasma mobile
pH 7.8, 30°C, recombinant wild-type enzyme
-
2600
tRNAUAALeu
pH 7.5, 37°C, recombinant wild-type enzyme
-
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evolution
-
the family of leucyl-tRNA synthetases is divided into prokaryotic and eukaryal/archaeal groups according to the presence and position of specific insertions and extensions. e.g. the LSD1, i.e. leucine-specific domain 1, which is naturally present in eukaryal/archaeal LeuRSs, but absent from prokaryotic LeuRSs. The LSD1s from organisms of both groups are dispensable for post-transfer editing
evolution
-
the family of leucyl-tRNA synthetases is divided into prokaryotic and eukaryal/archaeal groups according to the presence and position of specific insertions and extensions. e.g. the LSD1, i.e. leucine-specific domain 1, which is naturally present in eukaryal/archaeal LeuRSs, but absent from prokaryotic LeuRSs. The LSD1s from organisms of both groups are dispensable for post-transfer editing
evolution
based on sequence homology and the structures of the catalytic active sites, aaRSs are divided into two classes of 10 members each. Class I synthetases are further divided into three subclasses, a, b, and c, according to sequence homology. Leucyl-tRNA synthetase (LeuRS) belongs to class I aaRSs that include a typical Rossmann dinucleotide-binding fold active site architecture with the signature sequence modules HIGH and KMSKS. According to evolutionary models, the primitive catalytic core is extended by the insertion and/or fusion of additional domains (also called modules) in LeuRSs, most of which have inserted a large connective polypeptide 1 (CP1) domain that is responsible for amino acid editing. To ensure translation accuracy, LeuRSs have evolved a mechanism to remove aminoacyl AMP (aa-AMP, pre-transfer editing) and aa-tRNA (post-transfer editing). Sequence comparisons of the stem contact-fold domain (SC-fold) involved in editing, basic residues on helix alpha3 of the SC-fold are critical for catalytic efficiency, overview
evolution
based on sequence homology and the structures of the catalytic active sites, aaRSs are divided into two classes of 10 members each. Class I synthetases are further divided into three subclasses, a, b, and c, according to sequence homology. Leucyl-tRNA synthetase (LeuRS) belongs to class I aaRSs that include a typical Rossmann dinucleotide-binding fold active site architecture with the signature sequence modules HIGH and KMSKS. According to evolutionary models, the primitive catalytic core is extended by the insertion and/or fusion of additional domains (also called modules) in LeuRSs, most of which have inserted a large connective polypeptide 1 (CP1) domain that is responsible for amino acid editing. To ensure translation accuracy, LeuRSs have evolved a mechanism to remove aminoacyl AMP (aa-AMP, pre-transfer editing) and aa-tRNA (post-transfer editing). Sequence comparisons of the stem contact-fold domain (SC-fold) involved in editing, basic residues on helix alpha3 of the SC-fold are critical for catalytic efficiency, overview
evolution
Mesomycoplasma mobile
based on sequence homology and the structures of the catalytic active sites, aaRSs are divided into two classes of 10 members each. Class I synthetases are further divided into three subclasses, a, b, and c, according to sequence homology. Leucyl-tRNA synthetase (LeuRS) belongs to class I aaRSs that include a typical Rossmann dinucleotide-bindingfold active site architecture with the signature sequence modules HIGH and KMSKS. According to evolutionary models, the primitive catalytic core is extended by the insertion and/or fusion of additional domains (also called modules) in LeuRSs, most of which have inserted a large connective polypeptide 1 (CP1) domain that is responsible for amino acid editing. To ensure translation accuracy, LeuRSs have evolved a mechanism to remove aminoacyl AMP (aa-AMP, pre-transfer editing) and aa-tRNA (post-transfer editing). Although post-transfer editing is carried out by the CP1 domain in most LeuRSs, this domain has been naturally deleted in LeuRS from Mycoplasma mobile (MmLeuRS). Sequence comparisons of the stem contact-fold domain (SC-fold) involved in editing, basic residues on helix alpha3 of the SC-fold are critical for catalytic efficiency, overview
evolution
based on sequence homology and the structures of the catalytic active sites, aaRSs are divided into two classes of 10 members each. Class I synthetases are further divided into three subclasses, a, b, and c, according to sequence homology. Leucyl-tRNA synthetase (LeuRS) belongs to class I aaRSs that include a typical Rossmann dinucleotide-bindingfold active site architecture with the signature sequence modules HIGH and KMSKS. According to evolutionary models, the primitive catalytic core is extended by the insertion and/or fusion of additional domains (also called modules) in LeuRSs, most of which have inserted a large connective polypeptide 1 (CP1) domain that is responsible for amino acid editing. To ensure translation accuracy, LeuRSs have evolved a mechanism to remove aminoacyl AMP (aa-AMP, pre-transfer editing) and aa-tRNA (post-transfer editing). Sequence comparison of the EcLeuRS stem contact-fold domain (SC-fold) with editing-deficient enzymes suggests that key residues of this module have evolved an adaptive strategy to follow the editing functions of LeuRS, basic residues on helix alpha3 of the SC-fold are critical for catalytic efficiency, overview
evolution
based on sequence homology and the structures of the catalytic active sites, aaRSs are divided into two classes of 10 members each. Class I synthetases are further divided into three subclasses, a, b, and c, according to sequence homology. Leucyl-tRNA synthetase (LeuRS) belongs to class I aaRSs that include a typical Rossmann dinucleotide-bindingfold active site architecture with the signature sequence modules HIGH and KMSKS. According to evolutionary models, the primitive catalytic core is extended by the insertion and/or fusion of additional domains (also called modules) in LeuRSs, most of which have inserted a large connective polypeptide 1 (CP1) domain that is responsible for amino acid editing. To ensure translation accuracy, LeuRSs have evolved a mechanism to remove aminoacyl AMP (aa-AMP, pre-transfer editing) and aa-tRNA (post-transfer editing). Sequence comparisons of the stem contact-fold domain (SC-fold) involved in editing, basic residues on helix alpha3 of the SC-fold are critical for catalytic efficiency, overview
evolution
enzyme leucyl-tRNA synthetase is part of the aminoacyl-tRNA synthetase (aaRS) family
evolution
leucyl-tRNA synthetase (LeuRS) belongs to class Ia aminoacyl-tRNA synthetases (AaRSs). Based on their similar structures, LeuRS, IleRS, and ValRS are collectively known as LIVRS, all of which contain a representative catalytic core consisting of a Rossmann fold. Besides the conservative Rossmann fold, almost all LeuRSs contain a large insertion domain called connective peptide 1 (CP1) within the sequence of the catalytic core. CP1 folds independently in the tertiary structure and is defined as a classic editing domain, in which the aminoacyl bond of mischarged aatRNA is hydrolyzed (post-transfer editing) to ensure the fidelity of the catalytic process
evolution
Mesomycoplasma mobile ATCC 43663 / 163K / NCTC 11711
-
based on sequence homology and the structures of the catalytic active sites, aaRSs are divided into two classes of 10 members each. Class I synthetases are further divided into three subclasses, a, b, and c, according to sequence homology. Leucyl-tRNA synthetase (LeuRS) belongs to class I aaRSs that include a typical Rossmann dinucleotide-bindingfold active site architecture with the signature sequence modules HIGH and KMSKS. According to evolutionary models, the primitive catalytic core is extended by the insertion and/or fusion of additional domains (also called modules) in LeuRSs, most of which have inserted a large connective polypeptide 1 (CP1) domain that is responsible for amino acid editing. To ensure translation accuracy, LeuRSs have evolved a mechanism to remove aminoacyl AMP (aa-AMP, pre-transfer editing) and aa-tRNA (post-transfer editing). Although post-transfer editing is carried out by the CP1 domain in most LeuRSs, this domain has been naturally deleted in LeuRS from Mycoplasma mobile (MmLeuRS). Sequence comparisons of the stem contact-fold domain (SC-fold) involved in editing, basic residues on helix alpha3 of the SC-fold are critical for catalytic efficiency, overview
-
evolution
-
based on sequence homology and the structures of the catalytic active sites, aaRSs are divided into two classes of 10 members each. Class I synthetases are further divided into three subclasses, a, b, and c, according to sequence homology. Leucyl-tRNA synthetase (LeuRS) belongs to class I aaRSs that include a typical Rossmann dinucleotide-bindingfold active site architecture with the signature sequence modules HIGH and KMSKS. According to evolutionary models, the primitive catalytic core is extended by the insertion and/or fusion of additional domains (also called modules) in LeuRSs, most of which have inserted a large connective polypeptide 1 (CP1) domain that is responsible for amino acid editing. To ensure translation accuracy, LeuRSs have evolved a mechanism to remove aminoacyl AMP (aa-AMP, pre-transfer editing) and aa-tRNA (post-transfer editing). Sequence comparisons of the stem contact-fold domain (SC-fold) involved in editing, basic residues on helix alpha3 of the SC-fold are critical for catalytic efficiency, overview
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malfunction
-
replacement of Giardia lamblia eukarya-specific insertion 1, GlESI, by human eukarya-specific insertion 1, HsESI, impairs leucine activation, aminoacylation and post-transfer editing functions without changing the editing specificity
malfunction
abrogation of the LeuRS specificity determinant threonine 252 does not improve the affinity of the editing site for the cognate leucine as expected, but instead substantially enhances the rate of leucyl-tRNALeu hydrolysis. Molecular dynamics simulations reveals that the wild-type enzyme, but not the T252A mutant, enforces leucine to adopt the side-chain conformation that promotes the steric exclusion of a putative catalytic water
malfunction
knockdown of LRS in HEK-293 cells results in impaired leucine-stimulated S6K1 phosphorylation, total amino acid stimulation of pS6K1 is also significantly reduced. Knockdown of LRS decreasesVps34 activity induced by leucine or total amino acids. Knockdown of LRS does not affect the protein levels of mTOR, raptor, Vps34, and Rag GTPases
malfunction
Lars knockdown does not decrease phosphorylated mTOR in differentiated myotubes, nor does it affect the hypertrophy of myotubes. Extracellular flux analysis shows that Lars knockdown does not affect the metabolism (glycolysis and mitochondrial respiration) of myotubes
malfunction
mutation of highly conserved basic residues on the third alpha-helix of the KMSKS catalytic loop domain impairs the affinity of LeuRS for the anticodon stem of tRNALeu, which decreases both aminoacylation and editing activities
malfunction
mutations in mitochondrial DNA determine important human diseases. The majority of the known pathogenic mutations are located in transfer RNA (tRNA) genes and are responsible for a wide range of currently untreatable disorders. The detrimental effects of mt-tRNA point mutations can be attenuated by increasing the expression of the cognate mt-aminoacyl-tRNA synthetases (aaRSs). The isolated C-terminal domain of human mt-leucyl-tRNA synthetase (LeuRS-Cterm) localizes to mitochondria and ameliorates the energetic defect in trans-mitochondrial cybrids carrying mutations either in the cognate mt-tRNALeu(UUR) or in the non-cognate mt-tRNAIle gene.Since the mt-LeuRS-Cterm does not possess catalytic activity, its rescuing ability is most likely mediated by a chaperon-like effect, consisting in the stabilization of the tRNA structure altered by the mutation
malfunction
siRNA-mediated knockdown of LeuRS leads to suppression of rapamycin (mTOR), p-mTOR, ribosomal protein S6 kinase 1 (S6K1), p-S6K1, beta-casein, sterol regulatory element binding-protein 1c (SREBP-1c), glucose transporter 1 (GLUT1), and cyclin D1 mRNA and protein expression. LeuRS knockdown reduces cell growth, the expression of lactation-associated proteins, and milk synthesis
malfunction
the C-terminal domain of human mt leucyl-tRNA synthetase is both necessary and sufficient to improve the pathologic phenotype associated either with these mild mutations or with the severe m.3243A>G mutation in the mt-tRNALeu(UUR) gene, overview. The 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. The carboxyterminal domain of human mt leucyl-tRNA synthetase can be used to correct mt dysfunctions caused by mt-tRNA mutations. The Cterm domain of human mt-LeuRS directly interacts with mt-tRNALeu(UUR) and mt-tRNAIle in vitro
metabolism
-
isoform LeuRS1 generates Leu-tRNALeu for protein biosynthesis and exhibits obvious post-transfer editing activity to prevent generation of mischarged tRNALeu
metabolism
LRS-RagD interaction plays a pivotal role in the nutrientdependent mTORC1 signalling pathway
metabolism
mTORC1 lysosomal translocation and activation in response to amino acids requires the GTP-bound form of RagA or B as well as the GDP-bound form of RagC or D. The Ragulator complex and the GATOR1 complex act as GEF (guanine nucleotide exchange factor) and GAP (GTPase activating protein) for RagA/B, respectively. Role of LRS as a leucine sensor upstream of TORC1. Two other tRNA synthetases, IRS (isoleucyl-tRNA synthetase) and EPRS (glutamyl-prolyl-tRNA synthetase), are both in the multi-tRNA synthetase complex together with enzyme LRS, but both have no effect on leucine-stimulated Vps34 activity. LRS directly regulates Vps34 activity
metabolism
-
isoform LeuRS1 generates Leu-tRNALeu for protein biosynthesis and exhibits obvious post-transfer editing activity to prevent generation of mischarged tRNALeu
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physiological function
-
existence of a tRNA-independent pretransfer editing pathway in leucyltRNA synthetases from Aquifex aeolicus. This editing pathway is distinct from the post-transfer editing site and may occur at the synthetic catalytic site
physiological function
-
leucyl-tRNA synthetase is an essential RNA splicing factor for yeast mitochondrial introns. RNA deletion mutants of the large bI4 intron are active in RNA splicing and the activity of the minimized bI4 intron is enhanced in vitro by the presence of the bI4 maturase or LeuRS
physiological function
-
the A3243G mutation of the tRNALeu gene causes mitochondrial encephalomyopathy, lactic acidosis, and stroke-like symptoms and 2% of cases of type 2 diabetes. The alteration of aminoacylation of tRNALeu(UUR) caused by the A3243G mutation leads to mitochondrial translational defects and thereby reduces the aminoacylating efficiencies of tRNALeu(UUR) as well as of tRNAAla and tRNAMet
physiological function
-
aminoacyl-tRNA synthetases are critical for the translational process, catalyzing the attachment of specific amino acids to their cognate tRNAs. To ensure formation of the correct aminoacyl-tRNA, and thereby enhance the reliability of translation, several aminoacyl-tRNA synthetases have an editing capability that hinders formation of misaminoacylated tRNAs, analysis of the mechanism of the editing reaction for class I enzyme leucyl-tRNA synthetase complexed with a misaminoacylated tRNALeu by initio hybrid quantum mechanical/molecular mechanical potentials in conjunction with molecular dynamics simulations, overview. Editing is a self-cleavage reaction of the tRNA and so it is the tRNA, and not the protein, that drives the reaction. The protein does, however, have an important stabilizing effect on some high-energy intermediates along the reaction path, which is more efficient than the ribozyme would be alone. This indicates that editing is achieved by a hybrid ribozyme/protein catalyst. The water molecule that acts as the nucleophile in the editing reaction is activated by a 3'-hydroxyl group at the 3'-end of tRNALeu and that the O2' atom of the leaving group of the substrate is capped by one of the water's hydrogen atoms
physiological function
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aminoacyl-tRNA synthetases have evolved editing mechanisms to hydrolyze misactivated amino acids (pre-transfer editing) or misacylated tRNAs (post-transfer editing). Class Ia leucyl-tRNA synthetase may misactivate various natural and non-protein amino acids and then mischarge tRNALeu. The fidelity of prokaryotic LeuRS depends on multiple editing pathways to clear the incorrect intermediates and products in every step of aminoacylation reaction. Post-transfer editing as a final checkpoint of the reaction is very important to prevent mis-incorporation in vitro
physiological function
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the carboxy-terminal domain of human mitochondrial leucyl-tRNA synthetase can be used to correct mitochondrial dysfunctions caused by mitochondrial tRNA mutations like the phenotype of m.3243A>G MTTL1 mutant cybrids
physiological function
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the enzyme is a leucine sensor for serine/threonine kinase TORC1 and interacts with Gtr1
physiological function
-
the enzyme is a leucine sensor for serine/threonine kinase TORC1 and interacts with Gtr2
physiological function
-
the enzyme naturally produces mischarged tRNALeu
physiological function
Mesomycoplasma mobile
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the enzyme naturally produces mischarged tRNALeu
physiological function
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the enzyme plays a critical role in amino acid-induced mammalian target of rapamycin C1 activation by sensing intracellular leucine concentration and initiating molecular events leading to mammalian target of rapamycin C1 activation. The enzyme directly binds to Rag GTPase, the mediator of amino acid signaling to mTORC1, in an amino acid-dependent manner and functions as a GTPase-activating protein for Rag GTPase to activate mammalian target of rapamycin C1
physiological function
aminoacyl-tRNA synthetases (aaRSs) are a large and diverse family of enzymes that catalyze the attachment of amino acids to their cognate tRNAs in a two-step aminoacylation reaction as follows: 1. amino acid activation by ATP hydrolysis to form an aminoacyl-adenylate intermediate, and 2. transfer of the aminoacyl moiety from the intermediate to the cognate tRNA isoacceptor to form aminoacyl-tRNA (aa-tRNA)
physiological function
aminoacyl-tRNA synthetases (aaRSs) are a large and diverse family of enzymes that catalyze the attachment of amino acids to their cognate tRNAs in a two-step aminoacylation reaction as follows: 1. amino acid activation by ATP hydrolysis to form an aminoacyl-adenylate intermediate, and 2. transfer of the aminoacyl moiety from the intermediate to the cognate tRNA isoacceptor to form aminoacyl-tRNA (aa-tRNA)
physiological function
Mesomycoplasma mobile
aminoacyl-tRNA synthetases (aaRSs) are a large and diverse family of enzymes that catalyze the attachment of amino acids to their cognate tRNAs in a two-step aminoacylation reaction as follows: 1. amino acid activation by ATP hydrolysis to form an aminoacyl-adenylate intermediate, and 2. transfer of the aminoacyl moiety from the intermediate to the cognate tRNA isoacceptor to form aminoacyl-tRNA (aa-tRNA)
physiological function
aminoacyl-tRNA synthetases (aaRSs) are a large and diverse family of enzymes that catalyze the attachment of amino acids to their cognate tRNAs in a two-step aminoacylation reaction as follows: 1. amino acid activation by ATP hydrolysis to form an aminoacyl-adenylate intermediate, and 2. transfer of the aminoacyl moiety from the intermediate to the cognate tRNA isoacceptor to form aminoacyl-tRNA (aa-tRNA)
physiological function
aminoacyl-tRNA synthetases (aaRSs) are a large and diverse family of enzymes that catalyze the attachment of amino acids to their cognate tRNAs in a two-step aminoacylation reaction as follows: 1. amino acid activation by ATP hydrolysis to form an aminoacyl-adenylate intermediate, and 2. transfer of the aminoacyl moiety from the intermediate to the cognate tRNA isoacceptor to form aminoacyl-tRNA (aa-tRNA)
physiological function
Escherichia coli leucyl-tRNA synthetase (LeuRS) is an essential multi-domain metalloenzyme that aminoacylates tRNALeu with leucine. Enzyme LeuRS is an essential enzyme that relies on specialized domains to facilitate the aminoacylation reaction. Structural changes within the ZN-1 domain play a central role in LeuRS's catalytic cycle. The enzyme performs a Zn2+ dependent translocation mechanism for charged tRNALeu, Zn2+ is an architectural cornerstone of the ZN-1 domain and that without its geometric coordination the domain collapses. Residues C159, C176 and C179 coordinate Zn2+ and that this interaction is essential for leucylation to occur, but is not essential for deacylation
physiological function
leucyl-tRNA synthetase (Lars) is an intracellular sensor of leucine involved in the activation of mTOR signaling with a physiological role in skeletal muscle cells, potential roles of Lars for the activation of mTOR signaling, skeletal muscle cell differentiation, hypertrophy, and metabolism. Enzyme Lars directly binds to Rag GTPase, a known mediator of amino acid signaling to mTORC1, in a leucine-dependent manner and acts as a GTPase-activating protein for Rag GTPase to activate mTOR signaling. Lars is required for skeletal muscle differentiation through the activation of mTOR signaling, but not for hypertrophy or metabolic alteration of myotubes, link between Lars and mTOR activation in muscle cells and the physiological role of myoblast differentiation. Lars is essential for the activation of mTOR signaling in skeletal muscle cells and myogenic differentiation thought the induction of Igf2 expression
physiological function
leucyl-tRNA synthetase (LRS) is a leucine sensor for the activation of Vps34-PLD1 upstream of mTORC1. LRS binds to RagD-GTP, and forms a LRS-RagD complex, which translocates mTORC1 from the cytosol to the lysosome surface for subsequent activation of the mTORC1 signalling pathway. LRS is necessary for amino acid-induced Vps34 activation, cellular phosphatidylinositol-3-phosphate level increase, PLD1 activation, and PLD1 lysosomal translocation. Leucine binding but not tRNA charging activity of LRS is required for this regulation. LRS directly interacts with Vps34 in a non-autophagic complex, and activates Vps34 kinase activity in a leucine-dependent manner. Vps34 and PLD1 are required to mediate LRS activation of mTORC1. Only non-autophagic Vps34 complexes are involved in amino acid signaling to mTOR. LRS is necessary for amino acid activation of PLD1. Overexpression of LRS enhanced amino acid activation of S6K1
physiological function
-
leucyl-tRNA synthetase (LRS) plays major roles in providing leucine-tRNA and activating mechanistic target of rapamycin complex 1 (mTORC1) through intracellular leucine sensing. mTORC1 activated by amino acids affects the influence on physiology functions including cell proliferation, protein synthesis and autophagy in various organisms. Crosstalk between leucine sensing, LRS translocation, RagD interaction, and mTORC1 activation, mTORC1 activation is related to LRS translocation dependent on leucine, analysis of relationship between mTORC1 activation and LRS translocation, overview
physiological function
leucyl-tRNA synthetase regulates lactation and cell proliferation via mTOR signaling in dairy cow mammary epithelial cells, role of LeuRS as an intracellular L-leucine sensor for the mTORC1 pathway. LeuRS up-regulates the mTOR pathway to promote proliferation and lactation of dairy cow mammary epithelial cells (DCMECs) in response to changes in the intracellular leucine concentration. Treatment with L-leucine increases DCMECs viability and proliferation, as well as mammalian target of rapamycin (mTOR), p-mTOR, ribosomal protein S6 kinase 1 (S6K1), p-S6K1, beta-casein, sterol regulatory element binding-protein 1c (SREBP-1c), glucose transporter 1 (GLUT1), and cyclin D1 mRNA and protein expression via activity of enzyme LeuRS. Secretion of lactose and triglyceride are also increased. Effect of leucine on LeuRS to regulate cell growth and expression of proteins involved in mTOR signaling in DCMECs
physiological function
leucyl-tRNA synthetases (LeuRSs) catalyze the linkage of leucine with tRNALeu
physiological function
the direct interaction between enzyme LRS and RagD activates mTORC1 in live cells under leucine-deprived conditions. The nutrient sensing mechanism of mTORC1, particularly for Leu, an essential biomarker for nutrient status in cellular systems, is regulated by protein-protein interactions between LRS and RagD and directly mediate mTORC1 activation
physiological function
the ligation of amino acid to tRNA for purposes of protein synthesis proceeds in two steps, bothcatalyzed by a corresponding aminoacyl-tRNA synthetase(aaRS). The amino acid is first activated to anaminoacyl-adenylate (aa-AMP) intermediate at theexpense of ATP, followed by the transfer of aminoacylmoiety to the 2'- or 3'-OH groups at the terminal ribose of the cognate tRNA. Both steps occurwithin the same synthetic/aminoacylation active site located in thecatalytic aaRS domain. Based on the topology of the catalytic domains, the conserved recognition peptides and interaction with the tRNA, aaRSs can be divided into two classes, I and II. The mechanisms of aminoacylation and editing are basically conserved among the classes, although some class-specific features have been recognized. Editing aaRSs exercise specificity through a double-selection mechanism that uses structural/chemical differences between the cognate and non-cognate amino acids twice but in different ways. Leu-tRNALeu is excluded from proofreading basically at the level of catalysis, not binding. This is accomplished by the side chain of the cognate leucine, which adopts a conformation that sterically precludes the positioning of a water nucleophile near the tRNA-assisted hydrolytic machinery. The A76 3'-OH group is a crucial residue in the positioning and activation of the catalytic water. Deacylation mechanism of the enzyme, simulation and modeling, overview
physiological function
Mesomycoplasma mobile ATCC 43663 / 163K / NCTC 11711
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aminoacyl-tRNA synthetases (aaRSs) are a large and diverse family of enzymes that catalyze the attachment of amino acids to their cognate tRNAs in a two-step aminoacylation reaction as follows: 1. amino acid activation by ATP hydrolysis to form an aminoacyl-adenylate intermediate, and 2. transfer of the aminoacyl moiety from the intermediate to the cognate tRNA isoacceptor to form aminoacyl-tRNA (aa-tRNA)
-
physiological function
-
aminoacyl-tRNA synthetases (aaRSs) are a large and diverse family of enzymes that catalyze the attachment of amino acids to their cognate tRNAs in a two-step aminoacylation reaction as follows: 1. amino acid activation by ATP hydrolysis to form an aminoacyl-adenylate intermediate, and 2. transfer of the aminoacyl moiety from the intermediate to the cognate tRNA isoacceptor to form aminoacyl-tRNA (aa-tRNA)
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additional information
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activating role of C-terminal domain in the reactions of aminoacylation and editing, and its contribution to interaction with tRNALeu, overview. The C-terminal domain does is not critical for the manifestation of specificity of the enzyme of homologous RNAs, but is required for to enhance the rate of catalysis in aminoacylation and editing reaction
additional information
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human leucyl-tRNA synthetase and mitochondrial protein elongation factor EF-Tu show suppressing cross-activity on different tRNA mutants in humans and Saccharomyces cerevisiae, mechanism and specificity of suppression, overview. Suppressive activities of wild-type and mutant enzymes, overview
additional information
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leucine-specific domain 1, LSD1, is dispensable for post-transfer editing
additional information
-
leucine-specific domain 1, LSD1, is dispensable for post-transfer editing
additional information
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the CP1, i.e. connective peptide 1, domain of LeuRS contains the editing active site ESI, eukarya-specific insertion 1, Thr341 serves as a specificity discriminator. Arg338 is crucial for tRNALeu charging and the Asp440 is crucial for leucine activation and aminoacylation. The post-transfer editing required the C-terminal domain, Arg338 and Asp440 of GlLeuRS
additional information
analysis of the bacterial LeuRS structures (PDB IDs 2BTE and 4AS1) reveals that the isolated C-terminal domain of human mt-leucyl-tRNA synthetase (LeuRS-Cterm) interacts with the elbow region of the cognate tRNA and establishes a higher number of contacts with the sugar-phosphate backbone than with nucleotide-specific chemical groups, preferred interaction of human mt-LeuRS-Cterm with ribose and phosphate oxygen atoms
additional information
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analysis of the bacterial LeuRS structures (PDB IDs 2BTE and 4AS1) reveals that the isolated C-terminal domain of human mt-leucyl-tRNA synthetase (LeuRS-Cterm) interacts with the elbow region of the cognate tRNA and establishes a higher number of contacts with the sugar-phosphate backbone than with nucleotide-specific chemical groups, preferred interaction of human mt-LeuRS-Cterm with ribose and phosphate oxygen atoms
additional information
enzyme structure homology modeling using the structure of Thermus thermophilus LeuRS, PDB ID 2V0C, as template
additional information
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enzyme structure homology modeling using the structure of Thermus thermophilus LeuRS, PDB ID 2V0C, as template
additional information
in silico models of the wild-type and mutated LeuRS CP1 editing domain bound to the analogues with an ester linkage between the amino acid and adenosine as in real substrates [2'-L-leucyladenosine (Leu2A) and 2?-L-norvalyladenosine (Nva2A)] are constructed based on the structure of T252A LeuRS in a complex with tRNALeu and leucyl-adenylate sulphamoyl analogue (Leu-AMS), both positioned in the synthetic active site, and Leu2AA located in the editing domain. The tRNA body dominates the binding energetics of aa-tRNA:LeuRS complex formation
additional information
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in silico models of the wild-type and mutated LeuRS CP1 editing domain bound to the analogues with an ester linkage between the amino acid and adenosine as in real substrates [2'-L-leucyladenosine (Leu2A) and 2?-L-norvalyladenosine (Nva2A)] are constructed based on the structure of T252A LeuRS in a complex with tRNALeu and leucyl-adenylate sulphamoyl analogue (Leu-AMS), both positioned in the synthetic active site, and Leu2AA located in the editing domain. The tRNA body dominates the binding energetics of aa-tRNA:LeuRS complex formation
additional information
small-molecule protein-protein interactions modulators between LRS and RagD can be used as powerful research tools for studying the nutrient-dependent activation of mTORC1 and the subsequent biological outcome
additional information
the CP1 hairpin editing structure, residue R236 to G256, and the flexibility of small residues and the charge of polar residues in the CP1 hairpin are crucial for the function of LeuRS. The CP1 hairpin domain is crucial for activities of leucine, leucylation of tRNALeu, and tRNA binding of hcLeuRS
additional information
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the CP1 hairpin editing structure, residue R236 to G256, and the flexibility of small residues and the charge of polar residues in the CP1 hairpin are crucial for the function of LeuRS. The CP1 hairpin domain is crucial for activities of leucine, leucylation of tRNALeu, and tRNA binding of hcLeuRS
additional information
the KMSKS catalytic loop exhibits alpha-alpha-beta-alpha topology in class Ia and Ib aminoacyl-tRNA synthetases, two glycine residues on the third alpha-helix contribute to flexibility, leucine activation, and editing of LeuRS from Escherichia coli (EcLeuRS), acidic residues on the beta-strand enhance the editing activity of EcLeuRS and sense the size of the tRNALeu D-loop. Incorporation of acidic residues on the beta-strand stimulates the tRNA-dependent editing activity of the chimeric minimalist enzyme Mycoplasma mobile LeuRS fused to the connective polypeptide 1 editing domain and leucine-specific domain from EcLeuRS. Sequence comparison of the EcLeuRS stem contact-fold domain with editing-deficient enzymes suggests that key residues of this module have evolved an adaptive strategy to follow the editing functions of LeuRS. Amino acid residues Arg668 or Arg672 are not involved in the amino acid activation step but rather the second tRNA transfer step
additional information
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the KMSKS catalytic loop exhibits alpha-alpha-beta-alpha topology in class Ia and Ib aminoacyl-tRNA synthetases, two glycine residues on the third alpha-helix contribute to flexibility, leucine activation, and editing of LeuRS from Escherichia coli (EcLeuRS), acidic residues on the beta-strand enhance the editing activity of EcLeuRS and sense the size of the tRNALeu D-loop. Incorporation of acidic residues on the beta-strand stimulates the tRNA-dependent editing activity of the chimeric minimalist enzyme Mycoplasma mobile LeuRS fused to the connective polypeptide 1 editing domain and leucine-specific domain from EcLeuRS. Sequence comparison of the EcLeuRS stem contact-fold domain with editing-deficient enzymes suggests that key residues of this module have evolved an adaptive strategy to follow the editing functions of LeuRS. Amino acid residues Arg668 or Arg672 are not involved in the amino acid activation step but rather the second tRNA transfer step
additional information
Mesomycoplasma mobile
the KMSKS catalytic loop exhibits alpha-alpha-beta-alpha topology in class Ia and Ib aminoacyl-tRNA synthetases. Incorporation of acidic residues on the beta-strand stimulates the tRNA-dependent editing activity of the chimeric minimalist enzyme Mycoplasma mobile LeuRS fused to the connective polypeptide 1 editing domain and leucine-specific domain from EcLeuRS, acidic residues on the beta-strand enhance the editing activity of EcLeuRS and sense the size of the tRNALeu D-loop
additional information
there are two catalytic sites, the leucylation site housed within the aminoacylation domain and the hydrolytic deacylation site housed within the CP1 editing domain, the ZN-1 domain is known to play an essential structural role in stabilizing the Leu-Amp adenylate. Structural analysis of LeuRS enzymes using Fourier transform infrared spectroscopy (FTIR), and homology modeling of LeuRS in the editing conformation, visualizing the ZN-1 domain, by using the structure in editing conformation of the LeuRS enzyme from Thermus thermophilus, PDB ID 1OBH as template, overview
additional information
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there are two catalytic sites, the leucylation site housed within the aminoacylation domain and the hydrolytic deacylation site housed within the CP1 editing domain, the ZN-1 domain is known to play an essential structural role in stabilizing the Leu-Amp adenylate. Structural analysis of LeuRS enzymes using Fourier transform infrared spectroscopy (FTIR), and homology modeling of LeuRS in the editing conformation, visualizing the ZN-1 domain, by using the structure in editing conformation of the LeuRS enzyme from Thermus thermophilus, PDB ID 1OBH as template, overview
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
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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
Mesomycoplasma mobile ATCC 43663 / 163K / NCTC 11711
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the KMSKS catalytic loop exhibits alpha-alpha-beta-alpha topology in class Ia and Ib aminoacyl-tRNA synthetases. Incorporation of acidic residues on the beta-strand stimulates the tRNA-dependent editing activity of the chimeric minimalist enzyme Mycoplasma mobile LeuRS fused to the connective polypeptide 1 editing domain and leucine-specific domain from EcLeuRS, acidic residues on the beta-strand enhance the editing activity of EcLeuRS and sense the size of the tRNALeu D-loop
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additional information
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enzyme structure homology modeling using the structure of Thermus thermophilus LeuRS, PDB ID 2V0C, as template
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A156V
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mutation in beta-subunit, the ratio of turnover-number to Km-value is identical to the wild-type ratio
D373A
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mutant defective in post-transfer editing function
G237D
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mutation in beta-subunit, the ratio of turnover-number to Km-value is 1.7fold higher than the wild-type ratio
K238A
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mutation in beta-subunit, the ratio of turnover-number to Km-value is 2.4fold higher than the wild-type ratio
K599A
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site-directed mutagenesis, the mutation of the residue in the alpha-subunit involved in catalysis only slightly affects the enzyme activity
K599A/K600A
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site-directed mutagenesis, the mutation of the residue in the alpha-subunit involved in catalysis only slightly affects the enzyme activity
K599A/K600A/K605A/K606A
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site-directed mutagenesis, the mutation of the residue in the alpha-subunit involved in catalysis only slightly affects the enzyme activity
K600A
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site-directed mutagenesis, the mutation of the residue in the alpha-subunit involved in catalysis only slightly affects the enzyme activity
K605A
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site-directed mutagenesis, the mutation of the residue in the alpha-subunit involved in catalysis only slightly affects the enzyme activity
K605A/K606A
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site-directed mutagenesis, the mutation of the residue in the alpha-subunit involved in catalysis only slightly affects the enzyme activity
K606A
-
site-directed mutagenesis, the mutation of the residue in the alpha-subunit involved in catalysis only slightly affects the enzyme activity
L283F
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mutation in beta-subunit, the ratio of turnover-number to Km-value is 2fold higher than the wild-type ratio
M159A
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mutation in beta-subunit, the ratio of turnover-number to Km-value is 80% of the wild-type value
M160N
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mutation in beta-subunit, the ratio of turnover-number to Km-value is 2.4fold higher than the wild-type ratio
N152A
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mutation in beta-subunit, the ratio of turnover-number to Km-value is 16% of the wild-type ratio
N163A
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mutation in beta-subunit, the ratio of turnover-number to Km-value is 2.4fold higher than the wild-type ratio
Q234H
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mutation in beta-subunit, the ratio of turnover-number to Km-value is identical to the wild-type ratio
Q260stop
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mutation in beta-subunit, the ratio of turnover-number to Km-value is 0.02% of the wild-type ratio
R94A/R98A
site-directed mutagenesis, 83% reduced catalytic efficiency compared to wild-type
R94E
site-directed mutagenesis, mutating Arg94 to Glu decreases kcat/Km values to 22% of that of wild-type AaLeuRS
R94E/R98E
site-directed mutagenesis, the rate of AMP formation is decreased compared to the wild-type
R98A
site-directed mutagenesis, the mutation does not alter the catalytic efficiency
R98E
site-directed mutagenesis, the rate of AMP formation is decreased compared to the wild-type
T273R
-
no change in aminoacylation activity, but the deacylation of Ile-tRNALeu is strongly impaired. Mutant still exhibits 70% of wild-type AMP formation
V286stop
-
mutation in beta-subunit, the ratio of turnover-number to Km-value is 0.6% of the wild-type ratio
ts025C1
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temperature sensitive mutant ts025C1
tsH1
-
temperature sensitive mutant tsH1
A293E
-
site-directed mutagenesis, the mutant activity is similar to the wild-type enzyme
A293F
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54% decreased activity compared to the wild-type, more sensitive too inhibition by ATP
A293G
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50% decreased activity, decreased editing function, stronger binding of ATP, decrease in Km for the substrates, more sensitive too inhibition by ATP
A293I
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51% decreased activity, decreased editing function, stronger binding of ATP, decrease in Km for the substrates, more sensitive too inhibition by ATP
A293K
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site-directed mutagenesis, the post-transfer editing activity of the isolated CP1-domain is enhanced compared to the wild-type enzyme's domain
A293Y
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50% decreased activity, decreased editing function, stronger binding of ATP, decrease in Km for the substrates, more sensitive too inhibition by ATP
C159A
site-directed mutagenesis, structure comparison with the wild-type
C176A
site-directed mutagenesis, structure comparison with the wild-type
C179A
site-directed mutagenesis, structure comparison with the wild-type
D251W
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site-directed mutagenesis, editing site mutant, the substrate specificity and charging fidelity is retained
D342A
site-directed mutagenesis, the mutant shows altered deacylation activity with amino acids norvaline, isoleucine, and leucine compared to the wild-type enzyme, overview
DELTA788-798
-
partial deletion of the C-terminal domain peptide linker shows that as the length of the peptide linker decreases, aminoacylation activity decreases. This mutant shows almost no aminoacylation activity. Mutant shows reduced deacylation activity against mischarged Ile-tRNALeu
DELTA790-798
-
partial deletion of the C-terminal domain peptide linker shows that as the length of the peptide linker decreases, aminoacylation activity decreases. Mutant shows reduced deacylation activity against mischarged Ile-tRNALeu
DELTA792-798
-
partial deletion of the C-terminal domain peptide linker shows that as the length of the peptide linker decreases, aminoacylation activity decreases. Mutant retains significant deacylation activity against mischarged Ile-tRNALeu
DELTA793
-
single-site deletion at the more flexible end of the peptide linker: no significant change in aminoacylation activity
DELTA794
-
single-site deletion at the more flexible end of the peptide linker: no significant change in aminoacylation activity
DELTA794-798
-
partial deletion of the C-terminal domain peptide linker shows that as the length of the peptide linker decreases, aminoacylation activity decreases. Mutant retains significant deacylation activity against mischarged Ile-tRNALeu
DELTA795
-
single-site deletion at the more flexible end of the peptide linker: no significant change in aminoacylation activity
DELTA795-796
-
two-site deletion at the more flexible end of the peptide linker: no significant change in aminoacylation activity
DELTA795-798
-
partial deletion of the C-terminal domain peptide linker shows that as the length of the peptide linker decreases, aminoacylation activity decreases. Mutant retains significant deacylation activity against mischarged Ile-tRNALeu
DELTA796
-
single-site deletion at the more flexible end of the peptide linker: no significant change in aminoacylation activity
DELTA797
-
single-site deletion at the more flexible end of the peptide linker: no significant change in aminoacylation activity
DELTA797-798
-
two-site deletion at the more flexible end of the peptide linker: mutant exhibits lower aminoacylation activity compared to wild-type
E184A
the mutant performs the activities of amino acid activation, aminoacylation and deacylation of mischarged tRNAs as well as the native enzyme
E184R
the mutant performs the activities of amino acid activation, aminoacylation and deacylation of mischarged tRNAs as well as the native enzyme. The substitution specifically inhibits tRNA-dependent pre-transfer editing
E184R/T252R
the mutant performs the activities of amino acid activation, aminoacylation and deacylation of mischarged tRNAs as well as the native enzyme
E292A
-
unaltered specific activity in amino acid activation reaction, 61% reduced aminoacylation activity compared to the wild-type
E292D
-
unaltered specific activity in amino acid activation reaction, 53% reduced aminoacylation activity compared to the wild-type
E292F
-
unaltered specific activity in amino acid activation reaction, 60% reduced aminoacylation activity compared to the wild-type
E292K
-
unaltered specific activity in amino acid activation reaction, 85% reduced aminoacylation activity compared to the wild-type
E292Q
-
unaltered specific activity in amino acid activation reaction, 54% reduced aminoacylation activity compared to the wild-type
E292S
-
unaltered specific activity in amino acid activation reaction, 66% reduced aminoacylation activity compared to the wild-type
E797GGG
-
mutant shows no altered aminoacylation activity compared to wild-type
E797PPP
-
mutant shows no altered aminoacylation activity compared to wild-type
G225P
-
abolishes tRNA leucylation due to a defect in leucine activation, decrease in deacylation of Ile-tRNALeu
G229P
-
increased aminoacylation activity compared to the wild-type, mutant deacylates Ile-tRNALeu similar to wild-type
G229P/T252A
-
double mutant rescues leucylation activity to levels comparable to wild-type and retains deacylation activity of LeutRNALeu that is characteristic of the T252A mutation
G407P
-
aminoacylates tRNALeu and decylates Ile-tRNALeu as well as wild-type
G409P
-
increased aminoacylation activity compared to the wild-type, mutant deacylates Ile-tRNALeu similar to wild-type
G409P/T252A
-
double mutant fails to rescue the T252A mutation in LeuRS
K671A
site-directed mutagenesis, the mutation does no affect the catalytic efificiency
K809A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme
K846A
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-typ enzyme
K846A/K853A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme
K846E
-
site-directed mutagenesis, the mutant shows similar activity compared to the wild-typ enzyme
K846E/K853E
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme
K853A
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-typ enzyme
K853E
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-typ enzyme
L570F
-
the mutation leads to altered catalytic efficiency and perturbations to the discrimination of leucine and isoleucine and affects tRNA recognition and aminoacylation, it shows a catalytic turnover for isoleucine decreased by a factor of 2, L570F has an 11fold higher Km for leucine compared to the wild-type enzyme, the activity is reduceDdcompared to the wild-type enzyme
L570K
-
the mutation leads to altered catalytic efficiency and perturbations to the discrimination of leucine and isoleucine and affects tRNA recognition and aminoacylation, it shows a catalytic turnover for isoleucine decreased by a factor of 2, L570F has an 11fold higher Km for leucine compared to the wild-type enzyme, the activity is reduced compared to the wild-type enzyme
L570R
-
the mutation leads to altered catalytic efficiency and perturbations to the discrimination of leucine and isoleucine and affects tRNA recognition and aminoacylation, it shows a catalytic turnover for isoleucine decreased by a factor of 2, L570R has a 4fold stronger binding affinity for leucine compared to the wild-type enzyme, the activity is reduce compared to the wild-type enzyme
L854A
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-typ enzyme
L855A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme
M328K
-
7% increased activity compared to the wild-type
M336A
-
site-directed mutagenesis, editing site mutant, the mutant shows a small increase in leucine editing activity
M336F/T252A
-
site-directed mutagenesis, editing site mutant, the T252A mutation uncouples specificity, M336F/T252A double LeuRS mutant exhibited only slightly increased leucylation activity relative to the T252A single mutation
N807A
-
site-directed mutagenesis, the mutant shows similar activity compared to the wild-typ enzyme
N807A/N856A
-
site-directed mutagenesis, the mutant shows similar activity compared to the wild-typ enzyme
N856A
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-typ enzyme
Q805A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme
Q805A/N807A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme
Q805A/N807A/N856A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme
R185E
the mutation significantly enhances tRNA-dependent pre-transfer editing activity
R249F
-
site-directed mutagenesis, editing site mutant, editing activity of Leu-tRNALeu is decreased
R249F/T252A
-
site-directed mutagenesis, editing site mutant, the T252A mutation uncouples specificity
R249T
-
site-directed mutagenesis, editing site mutant, the mutant shows increased activity with tRNALeu, but even higher activity with tRNAIle compared to the wild-type enzyme
R249T/D251W
-
site-directed mutagenesis, editing site mutant, the mutant shows decreased hydrolysis of mischarged Ile-tRNALeu compared to the wild type enzyme
R286E
the mutation significantly enhances tRNA-dependent pre-transfer editing activity
R344A
site-directed mutagenesis, the mutant shows altered deacylation activity with amino acids norvaline, isoleucine, and leucine compared to the wild-type enzyme, overview
R668A
site-directed mutagenesis, the mutant shows 77% reduced catalytic efficiency compared to wild-type, the rate of AMP formation is decreased compared to the wild-type
R668A/R672A
site-directed mutagenesis, the mutant shows 93.6% reduced catalytic efficiency compared to wild-type, the rate of AMP formation is decreased compared to the wild-type
R668E
site-directed mutagenesis, the mutant shows 95% reduced catalytic efficiency compared to wild-type, the rate of AMP formation is decreased compared to the wild-type
R668E/R672E
site-directed mutagenesis, the mutant shows 98.6% reduced catalytic efficiency compared to wild-type. But the almost inactive mutant exhibits intact Leu activation activity comparable with the wild-type enzyme
R672A
site-directed mutagenesis, the rate of AMP formation is decreased compared to the wild-type
R672E
site-directed mutagenesis, the rate of AMP formation is decreased compared to the wild-type
R811A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme
T247A/T248A
-
533fold decrease in the ratio of turnover number to Km-value compared to wild-type ratio
T247S/T248S
-
77fold decrease in the ratio of turnover number to Km-value compared to wild-type ratio
T248A
site-directed mutagenesis, the mutant shows altered deacylation activity with amino acids norvaline, isoleucine, and leucine compared to the wild-type enzyme, overview
T252D
-
mutation results in isoleucylation of tRNALeu, editing activity is impaired, ATP hydrolysis in presence of norvaline is 27% of the wild-type value, ATP hydrolysis in presence of leucine is 98% of the wild-type value
T252E/M328K
-
activity is similar to the wild-type
T252F
-
impaired proofreading mechanism, increase rate of misaminoacylation with isoleucine and valine
T252G
-
the mutant enzyme, like the native enzyme, does not mischarge tRNALeu with isoleucine, ATP hydrolysis in presence of norvaline is 2.1fold higher than wild-type value, ATP hydrolysis in presence of leucine is 60% of the wild-type value
T252L
-
impaired proofreading mechanism, increase rate of misaminoacylation with isoleucine and valine
T252R
the mutant performs the activities of amino acid activation, aminoacylation and deacylation of mischarged tRNAs as well as the native enzyme
T252S
-
the ratio of turnover-number to KM-value for L-leucine in aminoacylation is 60% of the wild-type ratio, the ratio of turnover-number to KM-value for tRNALeu in aminoacylation is 80% of the wild-type ratio. The ratio of turnover-number to Km value for Leu-tRNALeu(UAA) is 7.5fold higher than the wild-type value, the ratio of turnover-number to Km value for Ile-tRNALeu(UAA) is 1.6fold lower than the wild-type value
T252V
-
the ratio of turnover-number to KM-value for L-leucine in aminoacylation is identical to wild-type ratio, the ratio of turnover-number to KM-value for tRNALeu in aminoacylation is 90% of the wild-type ratio. The ratio of turnover-number to Km value for Leu-tRNALeu(UAA) is 1.75fold higher than the wild-type value, the ratio of turnover-number to Km value for Ile-tRNALeu(UAA) is 13.3fold higher than the wild-type value
T272R
-
no change in aminoacylation activity, but the deacylation of Ile-tRNALeu is strongly impaired. Mutant still exhibits 45% of wild-type AMP formation
V338A
-
site-directed mutagenesis, editing site mutant, it shows increased post-transfer editing activity of Leu-tRNALeu compared to the wild-type enzyme
V338D
-
site-directed mutagenesis, editing site mutant, the mutant shows reduced post-transfer editing activity compared to the wild-type enzyme
V338E
-
site-directed mutagenesis, editing site mutant, the mutant shows reduced post-transfer editing activity compared to the wild-type enzyme
V338F
-
site-directed mutagenesis, editing site mutant, single introduction of the bulky phenylalanine residue nearly abolished post-transfer editing activity and facilitated mischarging of both isoleucine and valine to tRNALeu, 3000fold reduced activity
V338F/T252A
-
site-directed mutagenesis, editing site mutant, the T252A mutation uncouples specificity
V338L
-
site-directed mutagenesis, editing site mutant, the mutant shows reduced post-transfer editing activity compared to the wild-type enzyme
D173A
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, overview
D444E
-
site-directed mutagenesis
D588A
-
kcat/Km: 0.57 (ATP), 0.37 (Leu), mutant displays lower amino acid activation and aminoacylation activities than wild-type
D603A
-
kcat/Km: 0.91 (ATP), 0.94 (Leu), similar activity compared to wild-type
DELTA581-617
-
deletion of the CP2 domain, an insertion domain called connective peptide 2, of Giardia lamblia LeuRS shows that the CP2 domain is indispensable for amino acid activation, post-transfer editing and contributes to LeuRS-tRNALeu binding affinity. CP2 domain of Pyrococcus horikoshii LeuRS but not that of Escherichia coli LeuRS can partially restore amino acid activation and post-transfer editing functions suggesting that the functions of the CP2 domain are dependent on its location in the primary sequence of LeuRS
E165A
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, overview
E167A
-
site-directed mutagenesis, the mutant shows defects in leucine activation, mutant kinetics compared to the wild-type enzyme, overview
E298A
-
activity similar to wild-type
F171A
-
site-directed mutagenesis, inactive mutant
K139A
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, overview
K141A
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, overview
K142A
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, overview
K144A
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, overview
K148A
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, overview
K152A
-
site-directed mutagenesis, the mutant shows defects in leucine activation, mutant kinetics compared to the wild-type enzyme, overview
K166A
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, overview
K170A
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, overview
K299A
-
activity similar to wild-type
K303A
-
activity similar to wild-type
K587A
-
kcat/Km: 0.43 (ATP), 0.42 (Leu), mutant displays lower amino acid activation and aminoacylation activities than wild-type
K606A
-
mutant shows a complete loss of amino acid activation, aminoacylation and post-transfer editing activities
K606D
-
kcat/Km: 0.86 (ATP), 0.83 (Leu), similar leucine activation and post-transfer editing activities compared to wild-type
K606E
-
kcat/Km: 0.90 (ATP), 0.99 (Leu), no difference in leucine activation and post-transfer editing activities compared to wild-type
K606L
-
kcat/Km: 0.85 (ATP), 0.98 (Leu), similar leucine activation and post-transfer editing activities compared to wild-type
K606R
-
kcat/Km: 0.98 (ATP), 0.99 (Leu), no difference in leucine activation and post-transfer editing activities compared to wild-type
N301A
-
activity similar to wild-type
Q154A
-
site-directed mutagenesis, the mutant shows defects in leucine activation, mutant kinetics compared to the wild-type enzyme, overview
R338A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S153A
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, overview
S295A
-
activity similar to wild-type
T341A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T341R
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W155A
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, overview
W586A
-
mutant shows a complete loss of amino acid activation, aminoacylation and post-transfer editing activities
Y515A
-
109% of wild-type activity
Y515E
-
42% of wild-type activity
Y515K
-
51% of wild-type activity
Y520A
-
68% of wild-type activity
Y520E
-
41% of wild-type activity
Y520H
-
46% of wild-type activity
Y581A
-
mutant shows a complete loss of amino acid activation, aminoacylation and post-transfer editing activities
Y581E
-
mutant is unable to activate leucine by the ATP-diphosphate exchange assay, and mutant has no post-transfer editing activity
Y581F
-
mutant shows some but significantly reduced leucine activation activity its post-transfer editing activity is similar to wild-type
Y581K
-
mutant is unable to activate leucine by the ATP-diphosphate exchange assay, and mutant has no post-transfer editing activity
Y581S
-
mutant is unable to activate leucine by the ATP-diphosphate exchange assay, and mutant has no post-transfer editing activity
A3243G
-
respiratory chain defects in A3243G mutant cells is suppressed by overexpressing human mitochondrial leucyl-tRNA synthetase. The rates of oxygen consumption in suppressed cells are directly proportional to the levels of leucyl-tRNA synthetase. 15fold higher levels of leucyl-tRNA synthetase results in wild-type respiratory chain function. The suppressed cells have increased steady-state levels of tRNA(Leu(UUR)) and up to 3fold higher steady-state levels of mitochondrial translation products, but do not have rates of protein synthesis above those in parental mutant cells
A525S
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency in the aminoacylation reaction compared to the wild-type enzyme
C527E
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency in the aminoacylation reaction compared to the wild-type enzyme
D250A
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency in the aminoacylation reaction compared to the wild-type enzyme
D250E
site-directed mutagenesis, the mutant shows slightly altered kinetics and slightly reduced catalytic efficiency in the aminoacylation reaction compared to the wild-type enzyme
D250N
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency in the aminoacylation reaction compared to the wild-type enzyme
D250R
site-directed mutagenesis, inactive mutant
D252R
site-directed mutagenesis, inactive mutant
D399K
-
mutant is resitant to inhibitor 5-fluoro-2,1-benzoxaborol-1(3H)-ol but more sensitive to norvaline inhibition
D528R
site-directed mutagenesis, the mutant shows altered kinetics, reduced catalytic efficiency in the aminoacylation reaction, and 85% reduced amino acid activation activity compared to the wild-type enzyme
F50A/Y52A
site-directed mutagenesis, the leucine-binding deficient LRS mutant also activates Vps34, but to a lesser degree and in a leucine-independent manner
G245A
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency in the aminoacylation reaction compared to the wild-type enzyme
G245D
site-directed mutagenesis, the mutant shows altered kinetics and 50% reduced catalytic efficiency in the aminoacylation reaction compared to the wild-type enzyme
G245P
site-directed mutagenesis, inactive mutant
G245R
site-directed mutagenesis, the mutant shows altered kinetics and 50% reduced catalytic efficiency in the aminoacylation reaction compared to the wild-type enzyme
H251D
site-directed mutagenesis, inactive mutant
K600F
-
the mutation leads to altered catalytic efficiency and perturbations to the discrimination of leucine and isoleucine and affects tRNA recognition and aminoacylation, the mutant demonstrates a 9fold decrease in its ability to distinguish between leucine and isoleucine effectively, the activity is reduced compared to the wild-type enzyme
K600L
-
the mutation leads to altered catalytic efficiency and perturbations to the discrimination of leucine and isoleucine and affects tRNA recognition and aminoacylation, the mutant demonstrates an 11fold increase in its ability to distinguish between leucine and isoleucine effectively, the activity is reduced compared to the wild-type enzyme
K600R
-
the mutation leads to altered catalytic efficiency and perturbations to the discrimination of leucine and isoleucine and affects tRNA recognition and aminoacylation, the mutant shows a slight decrease in activity compared to the wild-type enzyme
P242E
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency in the aminoacylation reaction compared to the wild-type enzyme
P247A
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency in the aminoacylation reaction compared to the wild-type enzyme
Q529A
site-directed mutagenesis, the mutant shows altered kinetics, reduced catalytic efficiency in the aminoacylation reaction, and 70% reduced amino acid activation activity compared to the wild-type enzyme
R236D
site-directed mutagenesis, the mutant shows altered kinetics, reduced catalytic efficiency in the aminoacylation reaction, and 30% reduced amino acid activation activity compared to the wild-type enzyme
R517D
site-directed mutagenesis, the mutant shows altered kinetics, reduced catalytic efficiency in the aminoacylation reaction, and 90% reduced amino acid activation activity compared to the wild-type enzyme
R766A
site-directed mutagenesis, the mutation decreases the kcat/Km value to less than 10% that of the wild-type enzyme hcLeuRS
S519G
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency in the aminoacylation reaction compared to the wild-type enzyme
T298A
activity similar to wild-type, mutation maintains Ile-tRNALeu deacylation activity
T298Y
mutation uncouples specificity in the editing active site and mutant hydrolyzes Leu-tRNALeu
V523I
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency in the aminoacylation reaction compared to the wild-type enzyme
W530A
site-directed mutagenesis, the mutant shows altered kinetics, reduced catalytic efficiency in the aminoacylation reaction, and 50% reduced amino acid activation activity compared to the wild-type enzyme
Y240A
site-directed mutagenesis, the mutant shows altered kinetics, reduced catalytic efficiency in the aminoacylation reaction, and 50% reduced amino acid activation activity compared to the wild-type enzyme
Y531A
site-directed mutagenesis, the mutant shows altered kinetics, reduced catalytic efficiency in the aminoacylation reaction, and 50% reduced amino acid activation activity compared to the wild-type enzyme
Y534A
site-directed mutagenesis, the mutant shows altered kinetics, reduced catalytic efficiency in the aminoacylation reaction, and 60% reduced amino acid activation activity compared to the wild-type enzyme
K452A
Mesomycoplasma mobile
site-directed mutagenesis, the mutation has only a minimal effect on aminoacylation activity, the Km values is not significantly altered compared to wild-type
K452E
Mesomycoplasma mobile
site-directed mutagenesis, the mutation has only a minimal effect on aminoacylation activity, the Km values is not significantly altered compared to wild-type
K598A
Mesomycoplasma mobile
-
the mutation simultaneously reduces the tRNA-binding strength and aminoacylation and editing capacities of the enzyme's leucine-specific domain
R456A
Mesomycoplasma mobile
site-directed mutagenesis, 75% reduced catalytic efficiency compared to wild-type, the Km values is not significantly altered
R456E
Mesomycoplasma mobile
site-directed mutagenesis, 79% reduced catalytic efficiency compared to wild-type, the Km values is not significantly altered
K452A
Mesomycoplasma mobile ATCC 43663 / 163K / NCTC 11711
-
site-directed mutagenesis, the mutation has only a minimal effect on aminoacylation activity, the Km values is not significantly altered compared to wild-type
-
K452E
Mesomycoplasma mobile ATCC 43663 / 163K / NCTC 11711
-
site-directed mutagenesis, the mutation has only a minimal effect on aminoacylation activity, the Km values is not significantly altered compared to wild-type
-
R456A
Mesomycoplasma mobile ATCC 43663 / 163K / NCTC 11711
-
site-directed mutagenesis, 75% reduced catalytic efficiency compared to wild-type, the Km values is not significantly altered
-
R456E
Mesomycoplasma mobile ATCC 43663 / 163K / NCTC 11711
-
site-directed mutagenesis, 79% reduced catalytic efficiency compared to wild-type, the Km values is not significantly altered
-
L949A
-
the mutant shows 9.5% activity compared to the wild type enzyme
L949K
-
the mutant shows 2.6% activity compared to the wild type enzyme
L964A
-
the mutant shows 85% activity compared to the wild type enzyme
L964K
-
the mutant shows 8.6% activity compared to the wild type enzyme
Q915A
-
the mutant shows 99% activity compared to the wild type enzyme
Q915K
-
the mutant shows 54% activity compared to the wild type enzyme
R921A
-
the mutant shows 37% activity compared to the wild type enzyme
R921K
-
the mutant shows 83% activity compared to the wild type enzyme
V910A
-
the mutant shows 90% activity compared to the wild type enzyme
V910P
-
the mutant shows 3.7% activity compared to the wild type enzyme
V910W
-
the mutant shows 93% activity compared to the wild type enzyme
Q915A
-
the mutant shows 99% activity compared to the wild type enzyme
-
Q915K
-
the mutant shows 54% activity compared to the wild type enzyme
-
V910A
-
the mutant shows 90% activity compared to the wild type enzyme
-
V910P
-
the mutant shows 3.7% activity compared to the wild type enzyme
-
V910W
-
the mutant shows 93% activity compared to the wild type enzyme
-
D121A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
D98A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
E113A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
E114A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
F119A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
I104A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
I115A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
K100A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
K100A/Y105A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
K100A/Y109A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
K692A
site-directed mutagenesis, the mutation has no effect on tRNA charging activity
K696A
site-directed mutagenesis, the mutant shows a highly reduced kcat value compared to wild-type, while the Km value is 3fold increased
K699A
site-directed mutagenesis, the mutation has no effect on tRNA charging activity
N96A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
R106A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
R698A
site-directed mutagenesis, the mutation has no effect on tRNA charging activity
R703A
site-directed mutagenesis, kcat of mutant PhLeuRSR703A is much lower than that of wild-type PhLeuRS
R97A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
T101A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
T118A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
V108A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
W103A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
Y105A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
Y109A
-
site-directed mutagenesis, mutant steady-state leucine activation kinetics compared to the wild-type enzyme, overview
K692A
-
site-directed mutagenesis, the mutation has no effect on tRNA charging activity
-
K696A
-
site-directed mutagenesis, the mutant shows a highly reduced kcat value compared to wild-type, while the Km value is 3fold increased
-
K699A
-
site-directed mutagenesis, the mutation has no effect on tRNA charging activity
-
R698A
-
site-directed mutagenesis, the mutation has no effect on tRNA charging activity
-
R703A
-
site-directed mutagenesis, kcat of mutant PhLeuRSR703A is much lower than that of wild-type PhLeuRS
-
D357A
-
site-directed mutagenesis, the mutant shows reduced activity and abolished editing activity and misaminoacylated isoleucine to tRNALeu compared to the wild-type enzyme
D418R
mutant is significantly resistant to inhibitor AN-2690. Mutant aminoacylation of yctRNALeu is not different from wild-type ycLeuRS. Growth rate is similar to wild-type. Growth rate is moderately inhibited in medium containing a large excess of norvaline and reduced leucine
DELTA270-530
deletion of the CP1 domain shows that the mutant is not able to rescue LeuRS knock-out strain
DELTA314-319
deletion of the T-rich region shows that the mutant is able to rescue LeuRS knock-out strain with a grwoth rate similar to wild-type
DELTA819-828
-
deletion of the C-terminal domain peptide linker stimulates aminoacylation and editing activity shows that as the length of the peptide linker decreases, aminoacylation activity decreases. Mutant retains significant deacylation activity against mischarged Ile-tRNALeu
K404Y
mutant is significantly resistant to inhibitor AN-2690. Mutant aminoacylation of yctRNALeu is not different from wild-type ycLeuRS. Growth rate is similar to wild-type. Growth rate is moderately inhibited in medium containing a large excess of norvaline and reduced leucine
R265A
-
site-directed mutagenesis, the mutant shows reduced activity and abolished post-transfer editing activity compared to the wild-type enzyme
R449A
-
site-directed mutagenesis, nearly inactive mutant
R449E
-
site-directed mutagenesis, mutation within the RDW peptide, no complementation of the null mutant strain QBY320
R449K
-
site-directed mutagenesis, mutation within the RDW peptide, no complementation of the null mutant strain QBY320, 30fold reduced activity compared to the wild-type enzyme
R451A
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site-directed mutagenesis, nearly inactive mutant
R451E
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site-directed mutagenesis, mutation within the RDW peptide, no complementation of the null mutant strain QBY320
R451K
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site-directed mutagenesis, mutation within the RDW peptide, complementation of the null mutant strain QBY320, 11fold reduced activity compared to the wild-type enzyme
S416D
mutant is significantly resistant to inhibitor AN-2690. Mutant aminoacylation of yctRNALeu is not different from wild-type ycLeuRS. Growth rate is similar to wild-type. Growth rate is moderately inhibited in medium containing a large excess of norvaline and reduced leucine
T263V/T264V
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site-directed mutagenesis, the mutant shows reduced activity and decreased post-transfer editing activity compared to the wild-type enzyme
T31E
mutant is significantly resistant to inhibitor AN-2690. Mutant aminoacylation of yctRNALeu is not different from wild-type ycLeuRS. Growth rate is similar to wild-type. Mutant T319A shows mischarging capacity with Ile. Growth rate is severly inhibited in medium containing a large excess of norvaline and reduced leucine
T347A
mutant is inhibited by AN-2690. Mutant aminoacylation of yctRNALeu is not different from wild-type ycLeuRS. Growth rate is similar to wild-type. Growth rate is moderately inhibited in medium containing a large excess of norvaline and reduced leucine
T410A
mutant is inhibited by AN-2690. Mutant aminoacylation of yctRNALeu is not different from wild-type ycLeuRS. Growth rate is similar to wild-type. Growth rate is moderately inhibited in medium containing a large excess of norvaline and reduced leucine
W445A
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site-directed mutagenesis, nearly inactive mutant
W445F
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site-directed mutagenesis, mutation within the RDW peptide, no complementation of the null mutant strain QBY320
W445H
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site-directed mutagenesis, mutation within the RDW peptide, no complementation of the null mutant strain QBY320
W445K
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site-directed mutagenesis, mutation within the RDW peptide, no complementation of the null mutant strain QBY320
W445Y
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site-directed mutagenesis, mutation within the RDW peptide, weak complementation of the null mutant strain QBY320, 30fold reduced activity compared to the wild-type enzyme
D347A
mutation of the highly conserved Asp residue, located in the CP1 domain, is responsible for editing mechanism, slightly reduced activity with L-leucine, mutant mischarges tRNALeu with isoleucine
R94A
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mutation in beta-subunit, the ratio of turnover-number to Km-value is 40% of the wild-type ratio
R94A
site-directed mutagenesis, mutating Arg94 to Ala decreases kcat/Km values to 34% of that of wild-type AaLeuRS
A293D
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81% decreased activity, highly decreased editing function, very strong binding of ATP, high decrease in Km for the substrates, more sensitive too inhibition by ATP, increased heat lability compared to the wild-type
A293D
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site-directed mutagenesis, the mutant activity is similar to the wild-type enzyme
A293R
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30% decreased activity, decreased editing function, stronger binding of ATP, decrease in Km for the substrates
A293R
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site-directed mutagenesis, the post-transfer editing activity of the isolated CP1-domain is enhanced compared to the wild-type enzyme's domain
D345A
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mutation of the highly conserved Asp residue, located in the CP1 domain, is responsible for editing mechanism, slightly reduced activity with L-leucine, mutant mischarges tRNALeu with isoleucine
D345A
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site-directed mutagenesis, the mutation in the isolated CP1-domain abolishes hydrolytic post-transfer editing activity
D345A
site-directed mutagenesis, the mutant shows altered deacylation activity with amino acids norvaline, isoleucine, and leucine compared to the wild-type enzyme, overview
DELTA796-798
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partial deletion of the C-terminal domain peptide linker shows that as the length of the peptide linker decreases, aminoacylation activity decreases. Mutant retains significant deacylation activity against mischarged Ile-tRNALeu
DELTA796-798
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two-site deletion at the more flexible end of the peptide linker: mutant exhibits lower aminoacylation activity compared to wild-type
T247V
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8fold decrease in the ratio of turnover number to Km-value compared to wild-type ratio
T247V
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site-directed mutagenesis, hydrolysis of Ile-tRNALeu is completely abolished
T247V/T248V
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fold decrease in the ratio of turnover number to Km-value compared to wild-type ratio
T247V/T248V
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site-directed mutagenesis, the double mutation abolishes post-transfer editing activity
T248V
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6fold decrease in the ratio of turnover number to Km-value compared to wild-type ratio
T248V
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site-directed mutagenesis, hydrolysis of Ile-tRNALeu is completely abolished
T252A
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decreased activity with L-leucine, mutant shows altered editing specificity, it edits correctly formed leucyl-tRNALeu
T252A
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the ratio of turnover-number to KM-value for L-leucine in aminoacylation is 5% of the wild-type ratio, the ratio of turnover-number to KM-value for tRNALeu in aminoacylation is 10% of the wild-type ratio. The ratio of turnover-number to Km value for Leu-tRNALeu(UAA) is 25fold higher than the wild-type value, the ratio of turnover-number to Km value for Ile-tRNALeu(UAA) is 1.25fold higher than the wild-type value
T252A
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site-directed mutagenesis, the mutation in the full-length LeuRS uncouples specificity and hydrolyzes correctly charged LeutRNALeu
T252A
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site-directed mutagenesis, the mutation uncouples specificity and shows a 24-fold increase in hydrolytic activity compared to the wild-type enzyme, introduction of the large aromatic residue at Arg249 or Val338 rescued leucylation activity of the T252A mutation
T252A
site-directed mutagenesis, the mutant shows altered deacylation activity with amino acids norvaline, isoleucine, and leucine compared to the wild-type enzyme, conformational changes associated with the binding of post-transfer editing analogues in the editing site of T252A LeuRS, overview
T252E
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activity is similar to the wild-type
T252E
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mutation results in isoleucylation of tRNALeu, editing activity is impaired, ATP hydrolysis in presence of norvaline is 18% of the wild-type value, ATP hydrolysis in presence of leucine is 86% of the wild-type value
T252Y
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impaired proofreading mechanism, increase rate of misaminoacylation with isoleucine and valine, effective aminoacylation of tRNALeu with allylglycine, homopropargylglycine, 2-butynylalanine, norvaline, and norisoleucine
T252Y
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site-directed mutagenesis, the mutation occupies the amino acid binding pocket and blocks the binding of substrate to abolish editing activity
T252Y
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mutant is unable to proofread amino acids with unbranched side chains, and enables insertion of a variety of noncanonical amino acids into recombinant proteins in place of leucine
T252Y
site-directed mutagenesis, an editing defective mutant
D444A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D444A
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site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, overview
D399A
40fold increase in Km for leucine activation. Mutation eliminates Ile-tRNALeu deacylation activity
D399A
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site-directed mutagenesis, tRNA selectivity compared to the wild-type enzyme
D332A
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site-directed mutagenesis
D332A
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unlike the wild-type enzyme the mutant enzyme synthesizes the incorrect product Ile-tRNALeu, unlike the wild-type enzyme, the mutant enzyme cannot deacylate Ile-tRNALeu
D419A
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mutation of the highly conserved Asp residue, located in the CP1 domain, is responsible for editing mechanism, slightly reduced activity with L-leucine, mutant mischarges tRNALeu with isoleucine
D419A
mutant is significantly resistant to inhibitor AN-2690. Mutant aminoacylation of yctRNALeu is not different from wild-type ycLeuRS. Growth rate is similar to wild-type. Mutant D419A shows mischarging capacity with Ile. Growth rate is severly inhibited in medium containing a large excess of norvaline and reduced leucine
additional information
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deletion of the last 36 residues of the alpha-subunit is deleterious for tRNA charging, resulting in an inactive mutant, the monomeric mutants containing the alpha-subunit have activities comparable to the wild-type enzyme, while the heterodimeric enzymes show very low activity
additional information
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construction of diverse truncation mutants, ATP-diphosphate-exchange and aminoacylation activities, and ability to charge minihelixLeu of alpha and beta subunit mutants, overview
additional information
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the freestanding LeuRS editing domain can edit this precursor in contrast to IleRS and ValRS editing domains, overview, design and preparation of minihelixLIV, overview
additional information
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a mutation in the gene, leuS1, increases the transcription and expression of the ilv-leu operon, permitting monitoring of leuS alleles
additional information
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using a Chinese hamster ovary cell line containing a temperature-sensitive mutation in leucyl-tRNA synthetase which is active at 34 °C but defective at 39.5 °C, it is shown that shifting the cells to the latter temperature mimics the effects of amino acid starvation on protein synthesis. Leucine deprivation markedly inhibits mTORC1 signaling in these cells, but shifting the cells to the nonpermissive temperature for the synthetase does not. These data indicate that uncharged tRNALeu does not switch off mTORC1 signaling and suggest that mTORC1 is controlled by a distinct pathway that senses the availability of amino acids
additional information
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-
additional information
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leucine-auxotrophic strain
additional information
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construction of an enzyme mutant with a duplication of the peptide fragment from Met238 to Pro368 within the CP1 domain which shows an activity reduced by 59% compared to the wild-type enzyme, and catalyzes the mischarging of tRNALeu by methionine or isoleucine due to impaired ability to edit incorrect products
additional information
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construction of several CP1 domain mutants by introduction of restriction endonuclease sites into gene leuS
additional information
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overexpression of the alpha and beta subunits of the Aquifex aeolicus enzyme and the C- and N-terminal parts of the Escherichia coli enzyme in Escherichia coli as monomeric and dimeric mutants, also mixed between the species, the heterodimeric mutants and the monomeric mutants containing the N-terminal-subpart of the enzyme show very low activity
additional information
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deletion of the unique inserted leucine-specific domain of LeuRS primarily impacts kcat, chimeric LeuRS and ValRS mutants restore limited aminoacylation actiVity, overview
additional information
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deletions of the C terminus differentially impact the two functions of the enzyme in splicing and aminoacylation in vivo, overview, a five-amino acid C-terminal deletion of LeuRS, which does not complement a null strain, can form a ternary complex with the bI4 intron and its maturase splicing partner, however, the complex fails to stimulate splicing activity, deletion of the C-terminal domain of LeuRS abolishes aminoacylation of tRNALeu and also amino acid editing of mischarged tRNA molecules, overview
additional information
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isolated LeuRS CP1 domain requires idiosyncratic adaptations to confer editing activity independent of the full-length enzyme, the beta-strands, which link the CP1 domain to the aminoacylation core of LeuRS, are required for editing of mischarged tRNALeu, hydrolytic activity is also enhanced by inclusion of short flexible peptides, called hinges, at the end of both LeuRS beta-strands, overview
additional information
a helix alpha3-deletion mutant is inactive
additional information
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a helix alpha3-deletion mutant is inactive
additional information
C159A, C176A and C179A disassociate from Zn2+ much more readily than wild-type LeuRS, the wild-type LeuRS binds more tightly to Zn2+ than do C159A, C176A or C179A
additional information
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C159A, C176A and C179A disassociate from Zn2+ much more readily than wild-type LeuRS, the wild-type LeuRS binds more tightly to Zn2+ than do C159A, C176A or C179A
additional information
in silico models of the wild-type and mutated LeuRS CP1 editing domain bound to the analogues with an ester linkage between the amino acid and adenosine as in real substrates [2'-L-leucyladenosine (Leu2A) and 2?-L-norvalyladenosine (Nva2A)] are constructed based on the structure of T252A LeuRS in a complex with tRNALeu and leucyl-adenylate sulphamoyl analogue (Leu-AMS), both positioned in the synthetic active site, and Leu2AA located in the editing domain. The tRNA body dominates the binding energetics of aa-tRNA:LeuRS complex formation
additional information
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in silico models of the wild-type and mutated LeuRS CP1 editing domain bound to the analogues with an ester linkage between the amino acid and adenosine as in real substrates [2'-L-leucyladenosine (Leu2A) and 2?-L-norvalyladenosine (Nva2A)] are constructed based on the structure of T252A LeuRS in a complex with tRNALeu and leucyl-adenylate sulphamoyl analogue (Leu-AMS), both positioned in the synthetic active site, and Leu2AA located in the editing domain. The tRNA body dominates the binding energetics of aa-tRNA:LeuRS complex formation
additional information
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construction of deletion mutant LeuRS-A lacking residues Q281 to D294, and of deletion mutant LeuRS-B, lacking residues S295 to L304. The Km values of the two mutants for leucine and ATP decrease slightly and for tRNA increase slightly. The kcat values for the three substrates decrease
additional information
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deletion of the entire LSD1 abolishes synthetic activity of LeuRS
additional information
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replacement of Giardia lamblia eukarya-specific insertion 1, GlESI, by human eukarya-specific insertion 1, HsESI, results in mutant DELTAESI/DELTAHsESI. The mutation impairs leucine activation, aminoacylation and post-transfer editing functions without changing the editing specificity
additional information
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to explore the oncogenic potential of LARS1 over-expression in lung cancer, LARS1 is knocked-down using siRNA. LARS1 knock-down cells show reduced ability to migrate through transwell membrane and to form colonies in both soft agar and culture plate
additional information
enzyme knockout by shRNA and iRNA
additional information
generation of the isolated C-terminal domain of human mt leucyl-tRNA synthetase, and of DELTACterm mutant
additional information
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generation of the isolated C-terminal domain of human mt leucyl-tRNA synthetase, and of DELTACterm mutant
additional information
the CP1 hairpin of Homo sapiens cytoplasmic LeuRS (hcLeuRS) is deleted or substituted by those from other representative species. Lack of a CP1 hairpin leads to complete loss of aminoacylation, amino acid activation, and tRNA binding, butthe mutants retain post-transfer editing activity. Only the CP1 hairpin from Saccharomyces cerevisiae LeuRS (ScLeuRS) can partly rescue the hcLeuRS functions. Construction of chimeric mutants with the CP1 hairpin of hcLeuRS substituted for that of hcIleRS or hcValRS. The deacylating activity toward mischarged tRNALeu of hcLeuRS-ScCH1 and -ScCH2 decreases by 15% compared to that of hcLeuRS, kinetics comparisons, overview. Further site-directed mutagenesis indicates that the flexibility of small residues and the charge of polar residues in the CP1 hairpin are crucial for the function of LeuRS
additional information
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the CP1 hairpin of Homo sapiens cytoplasmic LeuRS (hcLeuRS) is deleted or substituted by those from other representative species. Lack of a CP1 hairpin leads to complete loss of aminoacylation, amino acid activation, and tRNA binding, butthe mutants retain post-transfer editing activity. Only the CP1 hairpin from Saccharomyces cerevisiae LeuRS (ScLeuRS) can partly rescue the hcLeuRS functions. Construction of chimeric mutants with the CP1 hairpin of hcLeuRS substituted for that of hcIleRS or hcValRS. The deacylating activity toward mischarged tRNALeu of hcLeuRS-ScCH1 and -ScCH2 decreases by 15% compared to that of hcLeuRS, kinetics comparisons, overview. Further site-directed mutagenesis indicates that the flexibility of small residues and the charge of polar residues in the CP1 hairpin are crucial for the function of LeuRS
additional information
siRNA-mediated knockdown of Lars decreases phosphorylated p70 S6 kinase and inhibits the differentiation of C2C12 mouse myoblasts into myotubes, as evidenced by a decreased fusion index and decreased mRNA and protein expression levels of myogenic markers. si-Lars decreases the level of insulin-like growth factor 2 (Igf2) mRNA expression from the early stages of differentiation, indicating the possibility of an association between the mTORIGF2 axis and Lars. But Lars knockdown does not decrease phosphorylated mTOR in differentiated myotubes, nor does it affect the hypertrophy of myotubes as evidenced by measuring their diameters and detecting the mRNA and protein expression of hypertrophy markers
additional information
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siRNA-mediated knockdown of Lars decreases phosphorylated p70 S6 kinase and inhibits the differentiation of C2C12 mouse myoblasts into myotubes, as evidenced by a decreased fusion index and decreased mRNA and protein expression levels of myogenic markers. si-Lars decreases the level of insulin-like growth factor 2 (Igf2) mRNA expression from the early stages of differentiation, indicating the possibility of an association between the mTORIGF2 axis and Lars. But Lars knockdown does not decrease phosphorylated mTOR in differentiated myotubes, nor does it affect the hypertrophy of myotubes as evidenced by measuring their diameters and detecting the mRNA and protein expression of hypertrophy markers
additional information
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temperature-sensitive and leucine-auxotroph mutant leu-5
additional information
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temperature-sensitive and leucine-auxotroph mutant leu-5
additional information
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the deletion mutant lacking the C-terminal domain, LeuRSDELTA811-967, retains normal editing activity, but has severely reduced aminoacylation activity, deletion of amino acid residues 911-913 of LeuRS enhances the Ile-tRNAIle deacylation activity, without affecting the Ile-tRNALeu deacylation activity, a C-terminally truncated LeuRS can catalyze the first step of the aminoacylation reaction, Leu-AMP formation, but cannot catalyze the second step, transfer of Leu from Leu-AMP to tRNALeu, overview
additional information
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deletion of the entire LSD1 abolishes synthetic activity of LeuRS
additional information
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respiratory deficient mutants. The phenotype is a consequence of a mutation in a nuclear gene coding for mitochondrial leucyl-tRNA synthetase
additional information
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deletions of the C terminus differentially impact the two functions of the enzyme in splicing and aminoacylation in vivo, overview, a five-amino acid C-terminal deletion of LeuRS, which does not complement a null strain, can form a ternary complex with the bI4 intron and its maturase splicing partner, however, the complex fails to stimulate splicing activity, deletion of the entire yeast mitochondrial LeuRS C-terminal domain enhances its aminoacylation and amino acid editing activities
additional information
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a series of deletions and chimeric variations in the peptide linker of the yeast mitochondrial LeuRS chimeric mutant that is fused to the Escherichia coli LeuRS C-terminal domain extension are created: a four residue deletion mutant of the yeast mitochondrial LeuRS chimera (Ym EcCTD Delta4) stimulates aminoacylation activity significantly compared to that of the chimera enzyme with no deletion within the linker peptide
additional information
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an eight residue peptide linker deletion mutant that contains three (Ym EcCTD DELTA8/+3), six (Ym EcCTD DELTA8/+6), or nine (Ym EcCTD DELTA8/+9) residues from the Escherichia coli LeuRS linker peptide restors protein stability and activity. Within these three chimeric peptide linker swaps, successive increases in the length of the Escherichia coli chimeric peptide linker decreases aminoacylation activity progressively
additional information
deletion of the leuS gene is lethal. Human cytoplasmic LeuRS can rescue the knock-out strain but not Escherichia coli LeuRS. LeuRS mutant strains T319, D419A, K404Y, S416D, D418R, T347A or T410A are also able to rescue the null mutant
additional information
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deletion of the leuS gene is lethal. Human cytoplasmic LeuRS can rescue the knock-out strain but not Escherichia coli LeuRS. LeuRS mutant strains T319, D419A, K404Y, S416D, D418R, T347A or T410A are also able to rescue the null mutant
additional information
growth rate of wild-type strain in media containing a large excess of noncognate amino acid norvaline and reduced leucine is reduced to 35%
additional information
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growth rate of wild-type strain in media containing a large excess of noncognate amino acid norvaline and reduced leucine is reduced to 35%
additional information
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deletion of the C-terminal domain lowering the kcat by 152fold
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