6.1.1.14: glycine-tRNA ligase
This is an abbreviated version!
For detailed information about glycine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.14
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6.1.1.14
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cord
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glycinergic
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postsynaptic
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strychnine
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alpha1
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synthetases
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synapses
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ligand-gated
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aminoacyl-trna
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homomeric
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gabaars
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neurotransmission
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electrophysiological
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aminoacylation
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charcot-marie-tooth
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strychnine-sensitive
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gephyrin
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patch-clamp
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hyperekplexia
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presynaptic
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heteromeric
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startle
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pentameric
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gabaergic
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extrasynaptic
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picrotoxin
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glycylation
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glycine-induced
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single-channel
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glycine-activated
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cys-loop
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anticodon
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mipscs
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subunit-specific
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bicuculline
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glycine-gated
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outside-out
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subunit-containing
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alars
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two-electrode
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alpha2beta
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mesolimbic
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pore-lining
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hisrs
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glycine-mediated
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accumbal
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gabaar-mediated
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molecular biology
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medicine
- 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
Reaction
Synonyms
GARS, Glycine--tRNA ligase, Glycyl translase, glycyl tRNA synthetase, Glycyl-transfer ribonucleate synthetase, Glycyl-transfer ribonucleic acid synthetase, Glycyl-transfer RNA synthetase, Glycyl-tRNA synthetase, glycyl-tRNA synthetase 1, GlyRS, GlyRS1, GlyRS2, GRS1, More, Synthetase, glycyl-transfer ribonucleate
ECTree
6.1.1.14 glycine-tRNA ligaseAdvanced search results
results (
results (Engineering
Engineering on EC 6.1.1.14 - glycine-tRNA ligase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
P61L
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mutant enzymes with an altered amino acid binding site. Pro61Leu substitution in the alpha chain confers an elevation of the Km value for Gly, 25fold, and for ATP, 45fold, in the aminoacylation reaction, but only a minor pertubation of the Km for tRNA
D500N
E71G
G240R
G526R
G598A
H418R
I280F
L129P
P234KY
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naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
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
S581L
Y604F
GarsC201R/+
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mouse model, decreased grip strength, poor skilled motor function, increased total GARS protein at p15, reduction in large diameter axon in sciatic nerve, normal lifespan
GarsC201R/C201R
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mouse model, reduced weight and viability, impaired limb movement, life expectancy 17 days
GarsNmf249/+
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mouse model, sensory and motor deficits, abnormal neuromuscular junction morphology, impaired nerve impule transmission, reduced nerve conduction velocities, loss of large diameter peripheral axons, life expectancy 6-8 weeks
GarsP278KY/+
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mouse model, sensory and motor deficits, abnormal neuromuscular junction morphology, impaired nerve impule transmission, reduced nerve conduction velocities, loss of large diameter peripheral axons, life expectancy 6-8 weeks
GarsXM256/+
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mouse model, reduced GARS RNA levels, normal neuromuscular junction morphology, normal nerve conduction velocities, normal lifespan
P552F
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temperature-sensitive mutant grs1-1 shows altered substrate specificities, the mutant strain can be complemented by expression of the wild-type enzyme
additional information
D500N
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naturally occuring mutation in the catalytic domain, the mutation lies in the disordered insertion III and causes Charcot-Marie-Tooth peripheral neuropathies
E71G
modeled in yeast the mutation causes growth defects and impaired viability
E71G
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naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
E71G
the mutant shows increased activity compared to the wild type enzyme
E71G
the mutant shows slightly elevated aminoacylation activity over wild type
G240R
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naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
G240R
the GARS mutation does not impair transcription or translation, modeled in yeast the mutation causes growth defects and impaired viability
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
G526R
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naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
G598A
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naturally occuring mutation in the anticodon binding domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
H418R
modeled in yeast the mutation causes growth defects and impaired viability
H418R
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naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
I280F
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naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
L129P
modeled in yeast the mutation causes growth defects and impaired viability
L129P
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naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
S581L
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naturally occuring mutation in the anticodon binding domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies
S581L
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the naturally occuring dominant mutation to reduced aminoacylation activity and to motor nerve degeneration
Y604F
the mutant shows strongly reduced activity compared to the wild type enzyme
additional information
direction of a marker protein into isolated pea chloroplasts by the N-terminal domain of the enzyme, construction of the embryo-defective development mutant edd1 by usage of transposons as insertional mutagens, the reversible mutation leads to arrest of embryo growth and is lethal, generation of transgenic plants
additional information
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truncated enzyme forms with deletions of 12, 27, 46, and 55 N-terminal residues reduce the kcat value of the wild-type enzyme by a factor 5-10 in diphosphate exchange and aminoacylation activity, but does not significantly change the Km of the three substrates. Deletions of 108 N-terminal residues or the internal segments 111-164 and 110-309 cause complete loss of activity. Deletions from the C-terminus of 24, 38, 60, 163, and 328 residues result in inactive enzyme forms. Whereas the wild-type enzyme binds both tRNAGly and noncognate tRNAAla, the mutant lacking 55 N-terminal residues shows altered binding of tRNAGly and does not bind tRNAAla
additional information
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truncated enzyme forms with deletions of 12, 27, 46, and 55 N-terminal residues reduce the kcat value of the wild-type enzyme by a factor 5-10 in diphosphate exchange and aminoacylation activity, but does not significantly change the Km of the three substrates. Deletions of 108 N-terminal residues or the internal segments 111-164 and 110-309 cause complete loss of activity. Deletions from the C-terminus of 24, 38, 60, 163, and 328 residues result in inactive enzyme forms. Whereas the wild-type enzyme binds both tRNAGly and noncognate tRNAAla, the mutant lacking 55 N-terminal residues shows altered binding of tRNAGly and does not bind tRNAAla
additional information
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fusion of carboxyl terminus of the alpha-chain to the amino-terminus of the beta-chain through a short peptide linker. The fusion protein is active to within 2fold to 3fold of the wild-type, unfused chains
additional information
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expression in Escherichia coli as a fusion protein with 13 kDa biotinylated tag with an apparent MW of 90 kDa
additional information
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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
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
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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
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a dominant mutation Nmf249 of gene GARS causes Charcot-Marie-Tooth peripheral neuropathy type 2D, phenotype analysis, the dominant phenotype is not caused by loss of GlyRS aminoacylation function, mutant mice have abnormal neuromuscular junction morphology and impaired transmission, reduced nerve conduction velocities, and a loss of large-diameter peripheral axons, without defects in myelination, overview, construction of a loss-of-function mutant by gene-trap insertion, which shows no dominant phenotype, overview
additional information
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a defective mutant grs1-1 allel confers the temperature-sensitive growth defect by affection with the 3'-end formation
