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Information on EC 6.1.1.14 - glycine-tRNA ligase and Organism(s) Thermus thermophilus and UniProt Accession P56206
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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: Thermus thermophilus
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
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
-
-
-
-
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
-
activity with tRNAs with modified nucleotides
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
substrate specificity with tRNAGly of diverse origins
-
?
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
-
-
?
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
additional information
?
-
-
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
-
-
?
ATP + glycine + tRNAGly
AMP + diphosphate + glycyl-tRNAGly
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km-values for mutant tRNAs
-
additional information
additional information
-
kinetics for tRNAGly substrates of diverse prokaryotic and eukaryotic origins
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kcat for tRNAGly substrates of diverse prokaryotic and eukaryotic origins
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
comparison of structures of enzymes of diverse origins
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene glyS, GlyRS phylogenetic analysis, deduction of ancestral sequence of GlyRS, and introduction of individual or pairs of ancestral residues into Thermus thermophilus GlyRS resulting in ancestral mutants, which are expressed in Escherichia coli strain BL21(DE3), overview
gene glyS, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli BL21(DE3)
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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
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
Logan, D.T.; Mazauric, M.H.; Kern, D.; Moras, D.
Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus
EMBO J.
14
4156-4167
1995
Thermus thermophilus
Mazauric, M.H.; Keith, G.; Logan, D.; Kreutzer, R.; Giege, R.; Kern, D.
Glycyl-tRNA synthetase from Thermus thermophilus--wide structural divergence with other prokaryotic glycyl-tRNA synthetases and functional inter-relation with prokaryotic and eukaryotic glycylation systems
Eur. J. Biochem.
251
744-757
1998
Thermus thermophilus
Shimizu, H.; Yokobori, S.; Ohkuri, T.; Yokogawa, T.; Nishikawa, K.; Yamagishi, A.
Extremely thermophilic translation system in the common ancestor commonote: ancestral mutants of Glycyl-tRNA synthetase from the extreme thermophile Thermus thermophilus
J. Mol. Biol.
369
1060-1069
2007
Thermus thermophilus (P56206), Thermus thermophilus
Oberthuer, D.; Eichert, A.; Erdmann, V.A.; Fuerste, J.P.; Betzel, C.h.; Foerster, C.
The crystal structure of a Thermus thermophilus tRNAGly acceptor stem microhelix at 1.6 A resolution
Biochem. Biophys. Res. Commun.
404
245-249
2011
Thermus thermophilus
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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