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
-
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
- 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 (Substrates Products
Substrates Products on EC 6.1.1.14 - glycine-tRNA ligase
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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(C2*71-G2*C71)
AMP + diphosphate + glycyl-tRNAGly(C2*71-G2*C71)
-
-
-
-
?
ATP + glycine + tRNAGly(C2*G71-C2*A71)
AMP + diphosphate + glycyl-tRNAGly(C2*G71-C2*A71)
-
-
-
-
?
ATP + glycine + tRNAGly(G1*C72-A1*U72)
AMP + diphosphate + glycyl-tRNAGly(G1*C72-A1*U72)
-
-
-
-
?
ATP + glycine + tRNAGly(G1*C72-G1*U72)
AMP + diphosphate + glycyl-tRNAGly(G1*C72-G1*U72)
-
-
-
-
?
ATP + glycine + tRNAGly(U73-A73)
AMP + diphosphate + glycyl-tRNAGly(U73-A73)
-
-
-
-
?
ATP + glycine + tRNAGly(U73-C73)
AMP + diphosphate + glycyl-tRNAGly(U73-C73)
-
-
-
-
?
ATP + glycine + tRNAGly(U73-G73)
AMP + diphosphate + glycyl-tRNAGly(U73-G73)
-
-
-
-
?
ATP + glycine + tRNAGly
?
-
insertion of glycine into proteins
-
-
?
ATP + glycine + tRNAGly
?
-
insertion of glycine into proteins
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
examination pf glycylation activities using in vitro mutant glycine tRNA transcripts. The recognition nucleotides are determined to be C35 and C36 of anticodon, C2-G71 and G3-C70 base-pairs of acceptor stem. Discriminator base A73 is not recognized by glycyl-tRNA synthetase
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
examination pf glycylation activities using in vitro mutant glycine tRNA transcripts. The recognition nucleotides are determined to be C35 and C36 of anticodon, C2-G71 and G3-C70 base-pairs of acceptor stem. Discriminator base A73 is not recognized by glycyl-tRNA synthetase
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
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
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
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
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
binds two molecules of glycyl-AMP per tetramer
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
activity with tRNAs with modified nucleotides
-
?
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
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
?
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
two-step reaction
-
-
?
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 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, at least 10 different mutant alleles, overview
-
-
?
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
-
tRNA binding site structure, and wild-type and S581L mutant active site structures, overview
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
enzyme mutation Nmf249 causes Charcot-Marie-Tooth peripheral neuropathy type 2D, overview
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
usage of calf liver tRNA
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
chloroplastic and mitochondrial tRNA substrate specificity of chloroplastic isozyme GlyRS2, isozyme GlyRS1 is much less efficient
-
?
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
-
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
activity with tRNAs with modified nucleotides
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
wild-type and mutant tRNAGly substrates
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
replacement of ATP by CTP, UTP, ITP, GTP, or TTP results in a decrease in the reaction rate to less than 7% of that with ATP
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
can also charge the tRNAs of certain other bacteria and yeast
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
replacement of ATP by CTP, UTP, ITP, GTP, or TTP results in a decrease in the reaction rate to less than 7% of that with ATP
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
can also charge the tRNAs of certain other bacteria and yeast
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
activity with tRNAs with modified nucleotides
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
substrate specificity with tRNAGly of diverse origins
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
catalyzes glycine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
catalyzes alanine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
enzyme has two active sites for aminoacylation. tRNA2Gly binds with the enzyme in a molar ratio of 1:1. tRNA2Gly forms a 2:1 complex with the enzyme and is aminoacylated 2fold faster
-
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
catalyzes glycine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
beta-subunit plays a major role in tRNA recognition
-
-
?
additional information
?
-
-
the discriminator base at position 73, the second-base pair, C2*G71, in the acceptor stem, and the anticodon nucleotides, C35 and C36 contribute to the specific aminoacylation
-
-
?
additional information
?
-
-
the first base pair, G1*C72 is important for glycylation in E. coli and Thermus thermophilus
-
-
?
additional information
?
-
-
catalyzes the synthesis of P1,P4-di(adenosine)tetraphosphate (Ap4A), P1,P3-di(adenosine)triphosphate (Ap3A) and ADP from the enzyme bound glycyl adenylate
-
-
?
additional information
?
-
-
catalyzes the synthesis of P1,P4-di(adenosine)tetraphosphate (Ap4A), P1,P3-di(adenosine)triphosphate (Ap3A) and ADP from the enzyme bound glycyl adenylate
-
-
?
additional information
?
-
-
catalyzes a glycine-independent transfer of the gamma-phosphate group from ATP to nucleoside 5'-diphosphate
-
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
the third base pair, G3*C70 is important for glycylation in yeast
-
-
?
additional information
?
-
-
catalyzes glycine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
the discriminator base at position 73, the second-base pair, C2*G71, in the acceptor stem, and the anticodon nucleotides, C35 and C36 contribute to the specific aminoacylation
-
-
?
additional information
?
-
-
enzyme binds the 3'-ends of mRNA from yeast competing with the cognate tRNAGly substrate
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
enzyme plays an important role in transcription termination by affecting 3'-end formation
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
catalyzes glycine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
additional information
?
-
-
participates in peptidoglycan synthesis
-
-
?
additional information
?
-
-
catalyzes glycine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
participates in peptidoglycan synthesis
-
-
?
additional information
?
-
-
the discriminator base at position 73, the second-base pair, C2*G71, in the acceptor stem, and the anticodon nucleotides, C35 and C36 contribute to the specific aminoacylation
-
-
?
additional information
?
-
-
the first base pair, G1*C72 is important for glycylation in E. coli and Thermus thermophilus
-
-
?
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
