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Information on EC 6.1.1.14 - glycine-tRNA ligase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q06817
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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: Saccharomyces cerevisiae
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
Glycine--tRNA ligase
Glycyl translase
Glycyl-transfer ribonucleate synthetase
Glycyl-transfer ribonucleic acid synthetase
Glycyl-transfer RNA synthetase
Glycyl-tRNA synthetase
GlyRS
GRS1
Synthetase, glycyl-transfer ribonucleate
Glycine--tRNA ligase
-
-
-
-
Glycyl translase
-
-
-
-
Glycyl-transfer ribonucleate synthetase
-
-
-
-
Glycyl-transfer ribonucleic acid synthetase
-
-
-
-
Glycyl-transfer RNA synthetase
-
-
-
-
Glycyl-tRNA synthetase
-
-
-
-
GlyRS
-
-
-
-
Synthetase, glycyl-transfer ribonucleate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
Aminoacylation
esterification
-
-
-
-
Aminoacylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
glycine:tRNAGly ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9037-62-1
-
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
-
-
-
?
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
-
?
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
-
?
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
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
?
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
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.145
glycine
wild type isoform GlyRS2, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C
0.00073
tRNAGly
wild type isoform GlyRS2, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C
0.13
glycine
wild type isoform GlyRS1(KMM1), in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C
0.135
glycine
wild type isoform GlyRS1, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C
0.14
glycine
wild type isoform GlyRS1 without K motif, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C
0.145
glycine
wild type isoform GlyRS1 without insertion peptide, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C
0.00028
tRNAGly
wild type isoform GlyRS1, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C
0.00137
tRNAGly
wild type isoform GlyRS1 without insertion peptide, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C
additional information
additional information
-
Km-values for mutant tRNAs
-
additional information
additional information
-
dissociation constants for complexes of wild-type or mutant enzyme with tRNA and mRNA
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.73
tRNAGly
wild type isoform GlyRS2, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C
0.19
tRNAGly
wild type isoform GlyRS1 without insertion peptide, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C
0.33
tRNAGly
wild type isoform GlyRS1, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
220
tRNAGly
wild type isoform GlyRS2, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C
140
tRNAGly
wild type isoform GlyRS1 without insertion peptide, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C
1230
tRNAGly
wild type isoform GlyRS1, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
gene product of GRS1 has enzymic activity both in cytoplasm and mitochondria
-
gene product of GRS1 has enzymic activity both in cytoplasm and mitochondria
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
135000 - 142000
-
sucrose density gradient centrifugation, dimeric enzyme form
158000 - 160000
-
PAGE under nondenaturing conditions, gel filtration, dimeric enzyme form
210000
-
sucrose density gradient centrifugation, tetrameric enzyme form
250000
-
PAGE under nondenaturing conditions, gel filtration, tetrameric enzyme form
57500
-
2 * 67600 (alpha) + 2 * 57500 (beta), enzyme form isolated in presence of minimal concentrations of dithioerythritol. A dimeric enzyme form is isolated in presence of high concentrations of protease inhibitors and dithioerythritol, SDS-PAGE
67600
-
2 * 67600 (alpha) + 2 * 57500 (beta), enzyme form isolated in presence of minimal concentrations of dithioerythritol. A dimeric enzyme form is isolated in presence of high concentrations of protease inhibitors and dithioerythritol, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
dimer
-
2 * 70000-80000 (alpha), SDS-PAGE, enzyme form isolated in presence of high concentrations of protease inhibitors and dithioerythritol. A tetrameric enzyme form is isolated in presence of minimal concentrations of dithioerythritol
tetramer
-
2 * 67600 (alpha) + 2 * 57500 (beta), enzyme form isolated in presence of minimal concentrations of dithioerythritol. A dimeric enzyme form is isolated in presence of high concentrations of protease inhibitors and dithioerythritol, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
cytoplasmic and mitochondrial isoforms have the same polypeptide sequence except for a 23 amino acid mitochondrial leader peptide
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P552F
-
temperature-sensitive mutant grs1-1 shows altered substrate specificities, the mutant strain can be complemented by expression of the wild-type enzyme
additional information
-
a defective mutant grs1-1 allel confers the temperature-sensitive growth defect by affection with the 3'-end formation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
in absence of protease inhibitors and/or dithioerythritol, the enzyme rapidly loses its activity
-
protectors of SH groups at concentrations of 20 mM are required to obtain an optimal aminoacylation rate
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-atgged wild-type enzyme and P552F mutant from Escherichia coli
-
recombinant His-tagged isozymes GlyRS1 and 2 from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 genes: grs1 encodes mitochondrial and cytoplasmic isozyme, grs2 encodes a mitochondrial dipensable isozyme, expression in Escherichia coli as HIs-tagged proteins, both cytoplasmic and mitochondrial phenotypes of a knockout allele of grs1 are complemented by the expression of the single gene of Schizosaccharomyces pombe, expression of gene grs2 in a grs1-deficient yeast mutant cannot complement the lethal phenotype
-
expression of His-tagged wild-type and p552F mutant enzyme in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
-
translation of mRNA for yeast glycyl-tRNA synthetase is alternatively initiated from UUG and a downstream AUG initiation codon. Unlike an AUG initiation codon, efficiency of this non-AUG initiation codon is significantly affected by its sequence context, in particular the nucleotides at positions -3 to -1 relative to the initiation codon. A/A/R (R: A or G) and C/G/C appear to be the most and least favorable sequences at these positions, respectively. Mutation of the native context sequence -3 to -1 from AAA to CGC reduce translation initiation from the UUG codon up to 32fold and resulted in loss of mitochondrial respiration
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
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
Nameki, N.; Tamura, K.; Asahara, H.; Hasegawa, T.
Recognition of tRNAGly by three widely diverged glycyl-tRNA synthetases
J. Mol. Biol.
268
640-647
1997
Escherichia coli, Saccharomyces cerevisiae, Thermus thermophilus
Kern, D.; Giege, R.; Ebel, J.P.
Glycyl-tRNA synthetase from baker's yeast. Interconversion between active and inactive forms of the enzyme
Biochemistry
20
122-131
1981
Saccharomyces cerevisiae
Wright, H.T.; Nurse, K.C.; Goldstein, D.J.
Naldixic acid, oxolinic acid, and novobiocin inhibit yeast glycyl- and leucyl-transfer RNA synthetases
Science
213
455-456
1981
Saccharomyces cerevisiae, Escherichia coli
Magrath, C.; Hyman, L.E.
A mutation in GRS1, a glycyl-tRNA synthetase, affects 3'-end formation in Saccharomyces cerevisiae
Genetics
152
129-141
1999
Saccharomyces cerevisiae
Turner, R.J.; Lovato, M.; Schimmel, P.
One of two genes encoding glycyl-tRNA synthetase in Saccharomyces cerevisiae provides mitochondrial and cytoplasmic functions
J. Biol. Chem.
275
27681-27688
2000
Saccharomyces cerevisiae
Johanson, K.; Hoang, T.; Sheth, M.; Hyman, L.E.
GRS1, a yeast tRNA synthetase with a role in mRNA 3' end formation
J. Biol. Chem.
278
35923-35930
2003
Saccharomyces cerevisiae
Chang, K.J.; Wang, C.C.
Translation initiation from a naturally occurring non-AUG codon in Saccharomyces cerevisiae
J. Biol. Chem.
279
13778-13785
2004
Saccharomyces cerevisiae
Chen, S.; Lin, G.; Chang, K.; Yeh, L.; Wang, C.
Translational efficiency of a non-AUG initiation codon is significantly affected by its sequence context in yeast
J. Biol. Chem.
283
3173-3180
2008
Saccharomyces cerevisiae
Wu, Y.H.; Chang, C.P.; Chien, C.I.; Tseng, Y.K.; Wang, C.C.
An insertion peptide in yeast glycyl-tRNA synthetase facilitates both productive docking and catalysis of cognate tRNAs
Mol. Cell. Biol.
33
3515-3523
2013
Saccharomyces cerevisiae (P38088), Saccharomyces cerevisiae (Q06817), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P38088)
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
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