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Information on EC 6.1.1.14 - glycine-tRNA ligase
for references in articles please use BRENDA:EC6.1.1.14
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EC Tree 6 Ligases
6.1 Forming carbon-oxygen bonds
6.1.1 Ligases forming aminoacyl-tRNA and related compounds
6.1.1.14 glycine-tRNA ligase
The enzyme appears in viruses and cellular organisms
- 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
showSynonyms
glyrs, glycyl-trna synthetase, glyrs2, glycyl trna synthetase, glyrs1, glycine-trna ligase, glycyl-trna synthetase 1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GARS
Glycine--tRNA ligase
Glycyl translase
Glycyl-transfer ribonucleate synthetase
Glycyl-transfer ribonucleic acid synthetase
Glycyl-transfer RNA synthetase
Glycyl-tRNA synthetase
GlyRS
GlyRS1
GRS1
Synthetase, glycyl-transfer ribonucleate
additional information
-
the enzyme belongs to the class II of aminoacyl-tRNA synthetases
Glycine--tRNA ligase
-
-
-
-
Glycyl translase
-
-
-
-
Glycyl-transfer ribonucleate synthetase
-
-
-
-
Glycyl-transfer ribonucleic acid synthetase
-
-
-
-
Glycyl-transfer RNA synthetase
-
-
-
-
Glycyl-tRNA synthetase
-
-
-
-
Glycyl-tRNA synthetase
-
GlyRS
-
-
-
-
Synthetase, glycyl-transfer ribonucleate
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + glycine + tRNAGly = AMP + diphosphate + glycyl-tRNAGly
-
-
-
-
ATP + glycine + tRNAGly = AMP + diphosphate + glycyl-tRNAGly
`half-of-the-sites' mechanism in aminoacylation
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
esterification
Aminoacylation
-
-
-
-
esterification
-
-
-
-
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
AMP + ADP
P1,P3-bis(5'-adenosyl) triphosphate
-
Substrates: -
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AMP + ATP
P1,P4-bis(5'-adenosyl) tetraphosphate
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Substrates: -
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ATP + glycine + tRNAGly(C2*71-G2*C71)
AMP + diphosphate + glycyl-tRNAGly(C2*71-G2*C71)
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Substrates: -
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ATP + glycine + tRNAGly(C2*G71-C2*A71)
AMP + diphosphate + glycyl-tRNAGly(C2*G71-C2*A71)
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Substrates: -
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ATP + glycine + tRNAGly(G1*C72-A1*U72)
AMP + diphosphate + glycyl-tRNAGly(G1*C72-A1*U72)
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Substrates: -
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ATP + glycine + tRNAGly(G1*C72-G1*U72)
AMP + diphosphate + glycyl-tRNAGly(G1*C72-G1*U72)
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Substrates: -
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?
ATP + glycine + tRNAGly(U73-A73)
AMP + diphosphate + glycyl-tRNAGly(U73-A73)
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Substrates: -
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ATP + glycine + tRNAGly(U73-C73)
AMP + diphosphate + glycyl-tRNAGly(U73-C73)
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Substrates: -
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?
ATP + glycine + tRNAGly(U73-G73)
AMP + diphosphate + glycyl-tRNAGly(U73-G73)
-
Substrates: -
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
Substrates: 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
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
Substrates: 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
Products: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: 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
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
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Substrates: -
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
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Substrates: binds two molecules of glycyl-AMP per tetramer
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
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Substrates: activity with tRNAs with modified nucleotides
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
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Substrates: -
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: the fusion protein catalyzes the aminoacylation of bovine tRNA
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
Substrates: two-step reaction
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: enzyme mutations with reduced enzyme activity cause distal spinal muscular atrophy type V or Charcot-Marie-Tooth type 2D, i.e. dSMAV/CMT2D
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
Substrates: GlyRS allelic variants are causally associated with the Charcot-Marie-Tooth disease, the most common genetic disorder of the peripheral nervous system
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, at least 10 different mutant alleles, overview
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
Substrates: GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, the most common heritable disease of the peripheral nervous system, overview
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
Substrates: 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
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: tRNA binding site structure, and wild-type and S581L mutant active site structures, overview
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
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Substrates: -
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: enzyme mutation Nmf249 causes Charcot-Marie-Tooth peripheral neuropathy type 2D, overview
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: usage of calf liver tRNA
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: chloroplastic and mitochondrial tRNA substrate specificity of chloroplastic isozyme GlyRS2, isozyme GlyRS1 is much less efficient
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
Products: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
Substrates: -
Products: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: activity with tRNAs with modified nucleotides
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: wild-type and mutant tRNAGly substrates
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: 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
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: can also charge the tRNAs of certain other bacteria and yeast
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: 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
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: can also charge the tRNAs of certain other bacteria and yeast
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: -
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?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: activity with tRNAs with modified nucleotides
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ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
Substrates: substrate specificity with tRNAGly of diverse origins
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additional information
?
-
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
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additional information
?
-
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
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?
additional information
?
-
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Substrates: catalyzes glycine-dependent ATP-diphosphate exchange
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additional information
?
-
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Substrates: catalyzes alanine-dependent ATP-diphosphate exchange
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additional information
?
-
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Substrates: 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
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?
additional information
?
-
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
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?
additional information
?
-
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
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additional information
?
-
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Substrates: formation of glycine hydroxamate
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additional information
?
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Substrates: formation of glycine hydroxamate
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additional information
?
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Substrates: catalyzes glycine-dependent ATP-diphosphate exchange
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additional information
?
-
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
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?
additional information
?
-
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
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additional information
?
-
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Substrates: beta-subunit plays a major role in tRNA recognition
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additional information
?
-
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Substrates: 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
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?
additional information
?
-
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Substrates: the first base pair, G1*C72 is important for glycylation in E. coli and Thermus thermophilus
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additional information
?
-
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Substrates: catalyzes the synthesis of P1,P4-di(adenosine)tetraphosphate (Ap4A), P1,P3-di(adenosine)triphosphate (Ap3A) and ADP from the enzyme bound glycyl adenylate
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additional information
?
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Substrates: catalyzes the synthesis of P1,P4-di(adenosine)tetraphosphate (Ap4A), P1,P3-di(adenosine)triphosphate (Ap3A) and ADP from the enzyme bound glycyl adenylate
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additional information
?
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Substrates: catalyzes a glycine-independent transfer of the gamma-phosphate group from ATP to nucleoside 5'-diphosphate
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additional information
?
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
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?
additional information
?
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
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additional information
?
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Substrates: formation of glycine hydroxamate
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additional information
?
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
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?
additional information
?
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -
Products: -
?
additional information
?
-
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
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?
additional information
?
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Substrates: structure-function analysis
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additional information
?
-
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Substrates: structure-function analysis
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additional information
?
-
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -
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?
additional information
?
-
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -
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?
additional information
?
-
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
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additional information
?
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Substrates: the third base pair, G3*C70 is important for glycylation in yeast
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additional information
?
-
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Substrates: catalyzes glycine-dependent ATP-diphosphate exchange
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additional information
?
-
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Substrates: 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
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additional information
?
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Substrates: enzyme binds the 3'-ends of mRNA from yeast competing with the cognate tRNAGly substrate
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additional information
?
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
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additional information
?
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Substrates: enzyme plays an important role in transcription termination by affecting 3'-end formation
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additional information
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Substrates: phylogenetic analysis
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additional information
?
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
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additional information
?
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Substrates: catalyzes glycine-dependent ATP-diphosphate exchange
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additional information
?
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
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additional information
?
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Substrates: participates in peptidoglycan synthesis
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additional information
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Substrates: catalyzes glycine-dependent ATP-diphosphate exchange
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additional information
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Substrates: participates in peptidoglycan synthesis
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additional information
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Substrates: 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
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additional information
?
-
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Substrates: the first base pair, G1*C72 is important for glycylation in E. coli and Thermus thermophilus
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additional information
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Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + glycine + tRNAGly
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Substrates: insertion of glycine into proteins
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ATP + glycine + tRNAGly
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Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
Products: -
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?
ATP + glycine + tRNAGly
?
-
Substrates: insertion of glycine into proteins
Products: -
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?