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Information on EC 6.1.1.4 - leucine-tRNA ligase and Organism(s) Homo sapiens and UniProt Accession Q9P2J5

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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
leurs, leucyl-trna synthetase, lars2, lars1, cytoplasmic leurs, ecleurs, alphabeta-leurs, glleurs, hs mt leurs, leucyl-trna synthetase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cytoplasmic LeuRS
-
Leucyl-tRNA synthetase
-
HcleuRS
-
-
hs mt LeuRS
-
-
LARS1
-
-
LARS2
Leucine translase
Leucine--tRNA ligase
Leucyl-transfer ribonucleate synthetase
Leucyl-transfer ribonucleic acid synthetase
Leucyl-transfer RNA synthetase
leucyl-tRNA syntethase
-
Leucyl-tRNA synthetase
leucyl-tRNA synthetase 1
-
-
LeuRS
mt leucyl-tRNA synthetase
-
Synthetase, leucyl-transfer ribonucleate
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
Aminoacylation
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-leucine:tRNALeu ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9031-15-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
show the reaction diagram
-
-
-
?
ATP + L-leucine + tRNACAGLeu
AMP + diphosphate + L-leucyl-tRNACAGLeu
show the reaction diagram
human cytoplasmic tRNACAGLeu (hctRNACAG)
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
show the reaction diagram
L-isoleucyl-tRNALeu + H2O
t-RNALeu + L-isoleucine
show the reaction diagram
-
editing activity
-
?
ATP + L-isoleucine + tRNALeu
AMP + diphosphate + L-isoleucyl-tRNALeu
show the reaction diagram
ATP + L-leucine + tRNAIle
AMP + diphosphate + L-leucyl-tRNALeu
show the reaction diagram
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
show the reaction diagram
ATP + L-leucine + tRNALeu(UUR)
AMP + diphosphate + L-leucyl-tRNALeu(UUR)
show the reaction diagram
-
leucyl-tRNA synthetase contacts tRNALeu(UUR) in the amino acid acid acceptor stem, the anticodon stem, and the D-loop
-
-
?
ATP + L-leucine + tRNALeuCUN
AMP + diphosphate + L-leucyl-tRNALeuCUN
show the reaction diagram
-
-
-
-
?
ATP + L-leucine + tRNALeuUUR
AMP + diphosphate + L-leucyl-tRNALeuUUR
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
show the reaction diagram
ATP + L-leucine + tRNAIle
AMP + diphosphate + L-leucyl-tRNALeu
show the reaction diagram
-
-
-
?
ATP + L-leucine + tRNALeu
AMP + diphosphate + L-leucyl-tRNALeu
show the reaction diagram
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-(5-chloro-2-hydroxy-phenylamino)-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
binding mode, overview
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
-
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
-
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
-
5-fluoro-2,1-benzoxaborol-1(3H)-ol
-
AN-2690, antibiotic which specifically targets the editing active site of LeuRS
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
norvaline
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.04 - 3.3
L-isoleucine
0.024 - 0.9
L-leucine
0.00074 - 0.0017
tRNACAGLeu
-
0.09 - 1.349
ATP
14
L-isoleucine
-
pH 7.5, 37°C
0.0058 - 0.13
L-leucine
0.0014 - 0.014
tRNALeu
0.0179
tRNALeu(UUR)
-
-
-
0.0002 - 0.0022
tRNALeuCUN
-
0.0015 - 0.006
tRNALeuUUR
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.34 - 0.51
L-isoleucine
2.1 - 5.6
L-leucine
0.56 - 2.6
tRNACAGLeu
-
0.22 - 0.8
ATP
0.07
L-isoleucine
-
pH 7.5, 37°C
0.18 - 26.2
L-leucine
0.028 - 0.12
tRNALeu
0.35 - 3.2
tRNALeuCUN
-
0.003 - 0.14
tRNALeuUUR
-
additional information
additional information
-
turnover numbers for tRNALeu(UUR) variants
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16 - 0.17
L-isoleucine
5.6 - 94.3
L-leucine
330 - 3500
tRNACAGLeu
-
524 - 565
L-leucine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.011
-
recombinant mitochondrial isozyme mutant in cell lysate
0.128
-
purified recombinant mitochondrial isozyme mutant
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
assay at
7 - 7.5
-
assay at
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
LARS1 is over-expressed in lung cancer cell line A549
Manually annotated by BRENDA team
transmitochondrial, osteosarcoma-derived (143B.TK-) cybrid cell lines from patients
Manually annotated by BRENDA team
-
LARS1 is over-expressed in lung cancer cells compared to control tissue
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
predominantly
Manually annotated by BRENDA team
-
co-localization of LRS and lysosome-associated membrane glycoprotein 2, LAMP2
Manually annotated by BRENDA team
additional information
-
location analysis of LRS with and without leucine, using stimulated emission depletion (STED) microscopy one of the super-resolution microscopy and transmission electron microscopy (TEM), reveals enzyme translocation to the lysosome from cytoplasm on addition of leucine. The translocation is inhibited by treatment with compound BC-LI-0186 disrupting the interaction between RagD and LRS
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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
metabolism
physiological function
malfunction
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SYLC_HUMAN
1176
0
134466
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
101000
recombinant enzyme, gel filtration
135000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 135000, SDS-PAGE
monomer
1 * 101000, recombinant enzyme, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
processing of the mitochondrial isozyme by removing of the mitochondrial targeting presequence in the mitochondria of insect cells
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of the selenomethionine-labeled CP1 domain to 3.25 A, comparison with the structure of Candida albicans enzyme
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
D399A
40fold increase in Km for leucine activation. Mutation eliminates Ile-tRNALeu deacylation activity
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
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
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
D399A
-
site-directed mutagenesis, tRNA selectivity compared to the wild-type enzyme
D399K
-
mutant is resitant to inhibitor 5-fluoro-2,1-benzoxaborol-1(3H)-ol but more sensitive to norvaline inhibition
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
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and dialysis, to homogeneity
recombinant wild-type and mutant enzymes
recombinant enzyme
-
recombinant His-tagged LeuRS from Escherichia coli strain RosettaTM 2 (DE3) by nickel affinity and anion exchange chromatography, and ethanol precipitation, to 90% purity
-
recombinant N-terminally mutated His-tagged mitochondrial isozyme
-
using Ni-NTA chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene LARS, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain Rosetta (DE3)
recombinant expression of wild-type and mutant enzymes
expressed in Escherichia coli as a His-tagged fusion protein
-
expression of hcLeuRS and DELTAChcLeuRS (a C-terminal 89-amino acid truncated enzyme form) in a baculovirus system
-
expression of His-tagged cytoplasmic LeuRS in Escherichia coli strain RosettaTM 2 (DE3), expression in Spodotera frugiperda cells via baculovirus transfection system
-
gene LARS1
-
gene LARS2, expression analysis, generation of the isolated C-terminal domain of human mt leucyl-tRNA synthetase
mitochondrial isozyme, DNA sequence determination and analysis, expression of the mature enzyme as His-tagged enzyme in Escherichia coli BL21(DE3)
the mitochondrial isozyme is cloned and expressed in Escherichia coli with the same N-terminus as that processed in the mitochondria of insect cells as His-tagged protein
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bullard, J.M.; Cai, Y.C.; Spremulli, L.L.
Expression and characterization of the human mitochondrial leucyl-tRNA synthetase
Biochim. Biophys. Acta
1490
245-258
2000
Homo sapiens (Q15031), Homo sapiens
Manually annotated by BRENDA team
Yao, Y.N.; Wang, L.; Wu, X.F.; Wang, E.D.
Human mitochondrial leucyl-tRNA synthetase with high activity produced from Escherichia coli
Protein Expr. Purif.
30
112-116
2003
Homo sapiens
Manually annotated by BRENDA team
Lue, S.W.; Kelley, S.O.
An aminoacyl-tRNA synthetase with a defunct editing site
Biochemistry
44
3010-3016
2005
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Ling, C.; Yao, Y.N.; Zheng, Y.G.; Wei, H.; Wang, L.; Wu, X.F.; Wang, E.D.
The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex
J. Biol. Chem.
280
34755-34763
2005
Homo sapiens
Manually annotated by BRENDA team
Sohm, B.; Sissler, M.; Park, H.; King, M.P.; Florentz, C.
Recognition of human mitochondrial tRNALeu(UUR) by its cognate leucyl-tRNA synthetase
J. Mol. Biol.
339
17-29
2004
Homo sapiens
Manually annotated by BRENDA team
Lue, S.W.; Kelley, S.O.
A single residue in leucyl-tRNA synthetase affecting amino acid specificity and tRNA aminoacylation
Biochemistry
46
4466-4472
2007
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Shin, S.H.; Kim, H.S.; Jung, S.H.; Xu, H.D.; Jeong, Y.B.; Chung, Y.J.
Implication of leucyl-tRNA synthetase 1 (LARS1) over-expression in growth and migration of lung cancer cells detected by siRNA targeted knock-down analysis
Exp. Mol. Med.
40
229-236
2008
Homo sapiens
Manually annotated by BRENDA team
Yao, P.; Zhou, X.L.; He, R.; Xue, M.Q.; Zheng, Y.G.; Wang, Y.F.; Wang, E.D.
Unique residues crucial for optimal editing in yeast cytoplasmic Leucyl-tRNA synthetase are revealed by using a novel knockout yeast strain
J. Biol. Chem.
283
22591-22600
2008
Homo sapiens, Saccharomyces cerevisiae (P26637), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Park, H.; Davidson, E.; King, M.P.
Overexpressed mitochondrial leucyl-tRNA synthetase suppresses the A3243G mutation in the mitochondrial tRNA(Leu(UUR)) gene
RNA
14
2407-2416
2008
Homo sapiens
Manually annotated by BRENDA team
Pang, Y.L.; Martinis, S.A.
A paradigm shift for the amino acid editing mechanism of human cytoplasmic leucyl-tRNA synthetase
Biochemistry
48
8958-8964
2009
Homo sapiens (Q9P2J5), Homo sapiens
Manually annotated by BRENDA team
Seiradake, E.; Mao, W.; Hernandez, V.; Baker, S.J.; Plattner, J.J.; Alley, M.R.; Cusack, S.
Crystal structures of the human and fungal cytosolic Leucyl-tRNA synthetase editing domains: A structural basis for the rational design of antifungal benzoxaboroles
J. Mol. Biol.
390
196-207
2009
Candida albicans, Homo sapiens
Manually annotated by BRENDA team
Li, R.; Guan, M.X.
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
Mol. Cell. Biol.
30
2147-2154
2010
Homo sapiens
Manually annotated by BRENDA team
Montanari, A.; De Luca, C.; Frontali, L.; Francisci, S.
Aminoacyl-tRNA synthetases are multivalent suppressors of defects due to human equivalent mutations in yeast mt tRNA genes
Biochim. Biophys. Acta
1803
1050-1057
2010
Homo sapiens
Manually annotated by BRENDA team
Chen, X.; Ma, J.J.; Tan, M.; Yao, P.; Hu, Q.H.; Eriani, G.; Wang, E.D.
Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetase
Nucleic Acids Res.
39
235-247
2011
Homo sapiens
Manually annotated by BRENDA team
Duran, R.V.; Hall, M.N.
Leucyl-tRNA synthetase: double duty in amino acid sensing
Cell Res.
22
1207-1209
2012
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Han, J.M.; Jeong, S.J.; Park, M.C.; Kim, G.; Kwon, N.H.; Kim, H.K.; Ha, S.H.; Ryu, S.H.; Kim, S.
Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway
Cell
149
410-424
2012
Homo sapiens
Manually annotated by BRENDA team
Perli, E.; Giordano, C.; Pisano, A.; Montanari, A.; Campese, A.F.; Reyes, A.; Ghezzi, D.; Nasca, A.; Tuppen, H.A.; Orlandi, M.; Di Micco, P.; Poser, E.; Taylor, R.W.; Colotti, G.; Francisci, S.; Morea, V.; Frontali, L.; Zeviani, M.; dAmati, G.
The isolated carboxy-terminal domain of human mitochondrial leucyl-tRNA synthetase rescues the pathological phenotype of mitochondrial tRNA mutations in human cells
EMBO Mol. Med.
6
169-182
2014
Homo sapiens
Manually annotated by BRENDA team
Choi, H.; Son, J.B.; Kang, J.; Kwon, J.; Kim, J.H.; Jung, M.; Kim, S.K.; Kim, S.; Mun, J.Y.
Leucine-induced localization of Leucyl-tRNA synthetase in lysosome membrane
Biochem. Biophys. Res. Commun.
493
1129-1135
2017
Homo sapiens
Manually annotated by BRENDA team
Yoon, M.S.; Son, K.; Arauz, E.; Han, J.M.; Kim, S.; Chen, J.
Leucyl-tRNA synthetase activates Vps34 in amino acid-sensing mTORC1 signaling
Cell Rep.
16
1510-1517
2016
Homo sapiens (Q9P2J5)
Manually annotated by BRENDA team
Kim, C.; Jung, J.; Tung, T.T.; Park, S.B.
beta-Turn mimetic-based stabilizers of protein-protein interactions for the study of the non-canonical roles of leucyl-tRNA synthetase
Chem. Sci.
7
2753-2761
2016
Homo sapiens (Q9P2J5)
Manually annotated by BRENDA team
Perli, E.; Giordano, C.; Pisano, A.; Montanari, A.; Campese, A.F.; Reyes, A.; Ghezzi, D.; Nasca, A.; Tuppen, H.A.; Orlandi, M.; Di Micco, P.; Poser, E.; Taylor, R.W.; Colotti, G.; Francisci, S.; Morea, V.; Frontali, L.; Zeviani, M.; dAmati, G.
The isolated carboxy-terminal domain of human mitochondrial leucyl-tRNA synthetase rescues the pathological phenotype of mitochondrial tRNA mutations in human cells
EMBO Mol. Med.
6
169-182
2014
Homo sapiens (Q15031), Homo sapiens
Manually annotated by BRENDA team
Giordano, C.; Morea, V.; Perli, E.; dAmati, G.
The phenotypic expression of mitochondrial tRNA-mutations can be modulated by either mitochondrial leucyl-tRNA synthetase or the C-terminal domain thereof
Front. Genet.
6
113
2015
Homo sapiens (Q15031), Homo sapiens
Manually annotated by BRENDA team
Yan, W.; Ye, Q.; Tan, M.; Chen, X.; Eriani, G.; Wang, E.D.
Modulation of aminoacylation and editing properties of leucyl-tRNA synthetase by a conserved structural module
J. Biol. Chem.
290
12256-12267
2015
Pyrococcus horikoshii (O58698), Aquifex aeolicus (O66680 AND O67646), Escherichia coli (P07813), Escherichia coli, Mesomycoplasma mobile (Q6KHA5), Homo sapiens (Q9P2J5), Mesomycoplasma mobile ATCC 43663 / 163K / NCTC 11711 (Q6KHA5), Pyrococcus horikoshii ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3 (O58698)
Manually annotated by BRENDA team
Gudzera, O.I.; Golub, A.G.; Bdzhola, V.G.; Volynets, G.P.; Kovalenko, O.P.; Boyarshin, K.S.; Yaremchuk, A.D.; Protopopov, M.V.; Yarmoluk, S.M.; Tukalo, M.A.
Identification of Mycobacterium tuberculosis leucyl-tRNA synthetase (LeuRS) inhibitors among the derivatives of 5-phenylamino-2H-[1,2,4]triazin-3-one
J. Enzyme Inhib. Med. Chem.
31
201-207
2016
Mycobacterium tuberculosis (P9WFV1), Mycobacterium tuberculosis, Homo sapiens (Q9P2J5), Homo sapiens, Mycobacterium tuberculosis ATCC 25618 / H37Rv (P9WFV1)
Manually annotated by BRENDA team
Huang, Q.; Zhou, X.L.; Hu, Q.H.; Lei, H.Y.; Fang, Z.P.; Yao, P.; Wang, E.D.
A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity
RNA
20
1440-1450
2014
Homo sapiens (Q9P2J5), Homo sapiens
Manually annotated by BRENDA team