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Information on EC 6.1.1.14 - glycine-tRNA ligase and Organism(s) Homo sapiens and UniProt Accession P41250
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6.1.1.14 glycine-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.14
- cord
-
glycinergic
-
postsynaptic
- strychnine
- alpha1
- synthetases
-
synapses
-
ligand-gated
- aminoacyl-trna
-
homomeric
-
gabaars
-
neurotransmission
-
electrophysiological
- aminoacylation
- charcot-marie-tooth
-
strychnine-sensitive
-
gephyrin
-
patch-clamp
- hyperekplexia
-
presynaptic
-
heteromeric
-
startle
-
pentameric
-
gabaergic
-
extrasynaptic
- picrotoxin
-
glycylation
-
glycine-induced
-
single-channel
-
glycine-activated
-
cys-loop
-
anticodon
-
mipscs
-
subunit-specific
- bicuculline
-
glycine-gated
-
outside-out
-
subunit-containing
- alars
-
two-electrode
-
alpha2beta
-
mesolimbic
-
pore-lining
- hisrs
-
glycine-mediated
-
accumbal
-
gabaar-mediated
- molecular biology
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
glyrs, glycyl-trna synthetase, glyrs2, glycyl trna synthetase, glyrs1, glycine-trna ligase, glycyl-trna synthetase 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Glycyl-tRNA synthetase
-
Glycine--tRNA ligase
-
-
-
-
Glycyl translase
-
-
-
-
Glycyl-transfer ribonucleate synthetase
-
-
-
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Glycyl-transfer ribonucleic acid synthetase
-
-
-
-
Glycyl-transfer RNA synthetase
-
-
-
-
Glycyl-tRNA synthetase
GlyRS
Synthetase, glycyl-transfer ribonucleate
-
-
-
-
Glycyl-tRNA synthetase
-
-
-
-
GlyRS
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
Aminoacylation
esterification
-
-
-
-
Aminoacylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
glycine:tRNAGly ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9037-62-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
two-step reaction
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
GlyRS allelic variants are causally associated with the Charcot-Marie-Tooth disease, the most common genetic disorder of the peripheral nervous system
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, the most common heritable disease of the peripheral nervous system, overview
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
mutations in the enzyme cause Charcot-Marie-Tooth disease type 2D, CMT2D, and distal spinal muscular atrophy type V, dSMA-V, axonal neuropathies characterized by a phenotype that is more severe in the upper extremities, in most cases, mutant GARS protein mislocalizes in neuronal cells
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
the fusion protein catalyzes the aminoacylation of bovine tRNA
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
enzyme mutations with reduced enzyme activity cause distal spinal muscular atrophy type V or Charcot-Marie-Tooth type 2D, i.e. dSMAV/CMT2D
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, at least 10 different mutant alleles, overview
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
tRNA binding site structure, and wild-type and S581L mutant active site structures, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
GlyRS allelic variants are causally associated with the Charcot-Marie-Tooth disease, the most common genetic disorder of the peripheral nervous system
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, the most common heritable disease of the peripheral nervous system, overview
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
mutations in the enzyme cause Charcot-Marie-Tooth disease type 2D, CMT2D, and distal spinal muscular atrophy type V, dSMA-V, axonal neuropathies characterized by a phenotype that is more severe in the upper extremities, in most cases, mutant GARS protein mislocalizes in neuronal cells
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
enzyme mutations with reduced enzyme activity cause distal spinal muscular atrophy type V or Charcot-Marie-Tooth type 2D, i.e. dSMAV/CMT2D
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, at least 10 different mutant alleles, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
enzyme knockdown decreases the global level of neddylation and causes cell cycle abnormality
metabolism
the essential enzyme for protein synthesis also plays a critical role in neddylation by specifically binding to NEDD8 and enhancing neddylation. The enzyme preferentially binds and protects Ubc12N8 and E, and regulates cell cycle progression
malfunction
physiological function
-
glycyl-tRNA synthetase specifically binds to the poliovirus internal ribosome entry site to activate translation initiation
malfunction
-
Charcot-Marie-Tooth disease, CMT, type 2D, a hereditary axonal neuropathy, is caused by mutations in glycyl-tRNA synthetase
malfunction
-
GARS gene mutations are involved in autosomal dominant motor distal neuronopathy/axonopathy, CMT2D/dSMA-V, and sporadic juvenile muscular atrophy of the distal upper extremity or Hirayama's disease, phenotype and mechanism, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GARS_HUMAN
739
0
83166
Swiss-Prot
Mitochondrion (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer, crystal structure, overall structural organization of GlyRS, overview
additional information
additional information
structural alignment with the GlyRS from Thermus thermophilus
additional information
-
structural alignment with the GlyRS from Thermus thermophilus
additional information
-
sequence aligns well with a Bombyx mori sequence and a Saccharomyces cerevisiae sequence, but diverges widely from that of the Escherichia coli enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo form of full-length E71G mutant and tRNA-bound mutant complex E71G/C157R, vapor diffusion method, using 13-15% (w/v) PEG 6000, 0.1 M sodium citrate buffer (pH 5.5), and 0.1 M NaCl
purified recombinant soluble enzyme, hanging drop vapour diffusion method, 0.001 ml of 8 mg/ml protein in 10 mM HEPES, pH 7.0, with 20 mM NaCl is mixed with 0.001 ml of reservoir solution containing 10% PEG 6000, 0.1 HEPES pH 6.5, 0.01 Tris-HCl, pH 8.5, 0.5 NaCl and 0.1 magnesium acetate at room temperature, 2 days, X-ray diffraction structure determination and analysis at 3.0 A resolution
vapor diffusion method, using 0.2% (w/v) 4-diaminobutane, 0.2% (w/v) cystamine dihydrochloride, 0.2% (w/v) diloxanide furoate, 0.2% (w/v) sarcosine, 0.2% (w/v) spermine, and 0.02 M HEPES sodium (pH 6.8) at a 2:1:1 ratio
purified His-tagged wild-type and S581L mutant enzymes, sitting drop vapour diffusion nanocrystallization method, mutant S581L GlyRS from 20% PEG 3350, 0.2 M Na2SO4, 0.1 M Bis-Tris propane, pH 6.5, wild-type GlyRS from 20% PEG 3350, 0.2M sodium bromide, 0.1 M bis-Tris propane pH 8.5, X-ray diffraction structure determination and anaylsis at 2.8A and 3.1 A resolution, respectively
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E71G
G240R
the GARS mutation does not impair transcription or translation, modeled in yeast the mutation causes growth defects and impaired viability
G526R
H418R
modeled in yeast the mutation causes growth defects and impaired viability
L129P
modeled in yeast the mutation causes growth defects and impaired viability
Q82N
the mutant shows slightly increased activity compared to the wild type enzyme
R283A
the mutants retain 2% glycylation activity compared to the wild type enzyme
R283K
the mutants retain 20% glycylation activity compared to the wild type enzyme
R548A
the mutant shows strongly reduced activity compared to the wild type enzyme
Y604F
D500N
E71G
G240R
G526R
G598A
H418R
I280F
L129P
P234KY
-
naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
S581L
additional information
E71G
modeled in yeast the mutation causes growth defects and impaired viability
E71G
the mutant shows increased activity compared to the wild type enzyme
E71G
the mutant shows slightly elevated aminoacylation activity over wild type
G526R
modeled in yeast the mutation causes growth defects and impaired viability
G526R
naturally occuring mutation at the site for synthesis of glycyl-adenylate, G526 is a strictly conserved residue in the middle of motif 3, the mutant is inactive and shows tighter dimer interaction compared to the wild-type enzyme, long-range structural effects of the Charcot-Marie-Tooth disease-causing mutation in the human enzyme, overview
Y604F
the mutant shows strongly reduced activity compared to the wild type enzyme
D500N
-
naturally occuring mutation in the catalytic domain, the mutation lies in the disordered insertion III and causes Charcot-Marie-Tooth peripheral neuropathies
E71G
-
naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
G240R
-
naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
G526R
-
naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
G598A
-
naturally occuring mutation in the anticodon binding domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
H418R
-
naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
I280F
-
naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
L129P
-
naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
S581L
-
naturally occuring mutation in the anticodon binding domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
S581L
-
the naturally occuring dominant mutation to reduced aminoacylation activity and to motor nerve degeneration
additional information
mutations in the enzyme cause Charcot-Marie-Tooth disease type 2D, CMT2D, and distal spinal muscular atrophy type V, dSMA-V, axonal neuropathies characterized by a phenotype that is more severe in the upper extremities, in most cases, mutant GARS protein mislocalizes in neuronal cells, and four of the five mutations show loss-of-function, GARS-associated granules occur in the neurite projections of cultured neurons and in the peripheral nerve axons of normal human tissue
additional information
-
mutations in the enzyme cause Charcot-Marie-Tooth disease type 2D, CMT2D, and distal spinal muscular atrophy type V, dSMA-V, axonal neuropathies characterized by a phenotype that is more severe in the upper extremities, in most cases, mutant GARS protein mislocalizes in neuronal cells, and four of the five mutations show loss-of-function, GARS-associated granules occur in the neurite projections of cultured neurons and in the peripheral nerve axons of normal human tissue
additional information
-
expression in Escherichia coli as a fusion protein with 13 kDa biotinylated tag with an apparent MW of 90 kDa
additional information
-
GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, at least 10 different mutant alleles, most catalytic-domain mutations are at the dimer interface, overview, mapping mutations onto human GlyRS crystal structure show them within a band encompassing both sides of the dimer interface, with two CMT-causing mutations being at sites that are complementary partners of a kissing contact across the dimer interface, the CMT phenotype does not correlate with aminoacylation activity, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged cytosolic enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, chromosomal localization in region 7p15.1-p15.3, the gene contains only 1 transcriptional start point in 3 different cell lines, but 5 potential initiation codons, expression may be translationally regulated, N-terminal mitochondrial targeting sequence
gene GARS, allele-specific expression analysis, expression of wild-type enzyme in Escherichia coli strain BL21(DE3), expression of EGFP-tagged enzyme in COS-7 cells, wild-type GARS-EGFP associates with granules in both the cell body and neurite projections of 42% of EGFP-positive transfected MN-1 cells
gene GARS, lacking the mitochondrial-specific coding region, expression as C-terminally His6-tagged cytosolic enzyme in Escherichia coli strain BL21(DE3)
expression of CMT-causing mutant variants and wild-type enzymes in neuroblastoma cells that sprout primitive neurites
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
the distribution of mutations in the seven genes identified for hereditary motor neuropathy (HMN) is investigated in a cohort of 112 familial and isolated patients with a diagnosis of HMN. Nine different disease-causing mutations are found in small heat shock 22 kDa protein 8, small heat shock 27 kDa protein 1, Berardinelli-Seip congenital lipodystrophy and senataxin in 17 patients. No mutations are found in glycyl-tRNA synthetase, dynactin 1 and VAPB(VAMP)-associated protein B and C
medicine
-
Charcot-Marie-Tooth disease, CMT, type 2D, a hereditary axonal neuropathy, is caused by mutations in glycyl-tRNA synthetase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Freist, W.; Logan, D.T.; Gauss, D.H.
Glycyl-tRNA synthetase
Biol. Chem. Hoppe-Seyler
377
343-356
1996
Aliivibrio fischeri, Alcaligenes faecalis, Geobacillus stearothermophilus, Brevibacillus brevis, Bombyx mori, Bos taurus, Saccharomyces cerevisiae, Gallus gallus, Chlamydia trachomatis, Escherichia coli, eukaryota, Thermus thermophilus, Haemophilus influenzae, Homo sapiens, Staphylococcus aureus, Mus musculus, Mycoplasma genitalium, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium
Williams, J.; Osvath, S.; Khong, T.F.; Pearse.M.; Power, D.
Cloning, sequencing and bacterial expression of human glycine tRNA synthetase
Nucleic Acids Res.
23
1307-1310
1995
Homo sapiens
Ge, Q.; Trieu, E.P.; Targoff, I.N.
Primary structure and functional expression in human glycyl-tRNA synthetase, an autoantigen in myositis
J. Biol. Chem.
269
28790-28797
1994
Homo sapiens
Shiba, K.; Schimmel, P.; Motegi, H.; Noda, T.
Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation
J. Biol. Chem.
269
30049-30055
1994
Bombyx mori, Escherichia coli, Homo sapiens, Saccharomyces cerevisiae
Mudge, S.J.; Williams, J.H.; Eyre, H.J.; Sutherland, G.R.; Cowan, P.J.; Power, D.A.
Complex organisation of the 5'-end of the human glycine tRNA synthetase gene
Gene
209
45-50
1998
Homo sapiens (P41250), Homo sapiens
Xie, W.; Schimmel, P.; Yang, X.L.
Crystallization and preliminary X-ray analysis of a native human tRNA synthetase whose allelic variants are associated with Charcot-Marie-Tooth disease
Acta Crystallogr. Sect. F
62
1243-1246
2006
Homo sapiens (P41250), Homo sapiens
Cader, M.Z.; Ren, J.; James, P.A.; Bird, L.E.; Talbot, K.; Stammers, D.K.
Crystal structure of human wildtype and S581L-mutant glycyl-tRNA synthetase, an enzyme underlying distal spinal muscular atrophy
FEBS Lett.
581
2959-2964
2007
Homo sapiens
Antonellis, A.; Lee-Lin, S.Q.; Wasterlain, A.; Leo, P.; Quezado, M.; Goldfarb, L.G.; Myung, K.; Burgess, S.; Fischbeck, K.H.; Green, E.D.
Functional analyses of glycyl-tRNA synthetase mutations suggest a key role for tRNA-charging enzymes in peripheral axons
J. Neurosci.
26
10397-10406
2006
Homo sapiens (P41250), Homo sapiens
Nangle, L.A.; Zhang, W.; Xie, W.; Yang, X.L.; Schimmel, P.
Charcot-Marie-Tooth disease-associated mutant tRNA synthetases linked to altered dimer interface and neurite distribution defect
Proc. Natl. Acad. Sci. USA
104
11239-11244
2007
Homo sapiens
Xie, W.; Nangle, L.A.; Zhang, W.; Schimmel, P.; Yang, X.L.
Long-range structural effects of a Charcot-Marie-Tooth disease-causing mutation in human glycyl-tRNA synthetase
Proc. Natl. Acad. Sci. USA
104
9976-9981
2007
Homo sapiens (P41250), Homo sapiens
Dierick, I.; Baets, J.; Irobi, J.; Jacobs, A.; De Vriendt, E.; Deconinck, T.; Merlini, L.; Van den Bergh, P.; Rasic, V.M.; Robberecht, W.; Fischer, D.; Morales, R.J.; Mitrovic, Z.; Seeman, P.; Mazanec, R.; Kochanski, A.; Jordanova, A.; Auer-Grumbach, M.; Helderman-van den Enden, A.T.; Wokke, J.H.
Relative contribution of mutations in genes for autosomal dominant distal hereditary motor neuropathies: a genotype-phenotype correlation study
Brain
131
1217-1227
2008
Homo sapiens
Motley, W.W.; Talbot, K.; Fischbeck, K.H.
GARS axonopathy: not every neurons cup of tRNA
Trends Neurosci.
33
59-66
2010
Homo sapiens, Mus musculus
Blumen, S.; Drory, V.; Sadeh, M.; El-Ad, B.; Soimu, U.; Groozman, G.; Bouchard, J.; Goldfarb, L.
Mutational analysis of glycyl-tRNA synthetase (GARS) gene in Hirayama disease
Amyotroph. Lateral Scler.
11
237-239
2010
Homo sapiens
Andreev, D.E.; Hirnet, J.; Terenin, I.M.; Dmitriev, S.E.; Niepmann, M.; Shatsky, I.N.
Glycyl-tRNA synthetase specifically binds to the poliovirus IRES to activate translation initiation
Nucleic Acids Res.
40
5602-5614
2012
Homo sapiens
McMillan, H.J.; Schwartzentruber, J.; Smith, A.; Lee, S.; Chakraborty, P.; Bulman, D.E.; Beaulieu, C.L.; Majewski, J.; Boycott, K.M.; Geraghty, M.T.
Compound heterozygous mutations in glycyl-tRNA synthetase are a proposed cause of systemic mitochondrial disease
BMC Med. Genet.
15
36
2014
Homo sapiens (P41250)
Qin, X.; Hao, Z.; Tian, Q.; Zhang, Z.; Zhou, C.; Xie, W.
Cocrystal structures of glycyl-tRNA synthetase in complex with tRNA suggest multiple conformational states in glycylation
J. Biol. Chem.
289
20359-20369
2014
Homo sapiens (P41250), Homo sapiens
Deng, X.; Qin, X.; Chen, L.; Jia, Q.; Zhang, Y.; Zhang, Z.; Lei, D.; Ren, G.; Zhou, Z.; Wang, Z.; Li, Q.; Xie, W.
Large conformational changes of insertion 3 in human glycyl-tRNA synthetase (hGlyRS) during catalysis
J. Biol. Chem.
291
5740-5752
2016
Homo sapiens (P41250), Homo sapiens
Mo, Z.; Zhang, Q.; Liu, Z.; Lauer, J.; Shi, Y.; Sun, L.; Griffin, P.R.; Yang, X.L.
Neddylation requires glycyl-tRNA synthetase to protect activated E2
Nat. Struct. Mol. Biol.
23
730-737
2016
Homo sapiens (P41250), Homo sapiens
Chien, C.I.; Chen, Y.W.; Wu, Y.H.; Chang, C.Y.; Wang, T.L.; Wang, C.C.
Functional substitution of a eukaryotic glycyl-tRNA synthetase with an evolutionarily unrelated bacterial cognate enzyme
PLoS ONE
9
e94659
2014
Arabidopsis thaliana, Homo sapiens, Saccharomyces cerevisiae, Thermus thermophilus
EXTERNAL LINKS (specific for EC-Number 6.1.1.14)
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