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Information on EC 6.1.1.18 - glutamine-tRNA ligase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P13188
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EC Tree
6.1.1.18 glutamine-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.18
- synthetases
- aminoacyl-trna
- aminoacylation
-
anticodon
- glutamyl-trna
-
glutaminylation
- gln-trnagln
-
noncognate
-
aarss
-
trna-dependent
-
mischarging
-
transamidation
- asnrs
- aspartyl-trna
- trna2gln
-
nondiscriminating
- trnatyr
-
misaminoacylation
- glurss
-
misacylated
- ilers
- cysrs
-
anticodon-binding
- valrs
- gatcab
-
gln-trna
- drug development
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
glnrs, glutaminyl trna synthetase, glutaminyl-transfer rna synthetase, cytosolic glutaminyl-trna synthetase, class i glutaminyl-trna synthetase, glutamyl/glutaminyl-trna synthetase, l-glutamine:trnagln ligase (amp-forming), 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GlnRS
-
-
-
-
Glutamine translase
-
-
-
-
Glutamine--tRNA ligase
-
-
-
-
Glutamine-tRNA synthetase
-
-
-
-
Glutaminyl-transfer ribonucleate synthetase
-
-
-
-
Glutaminyl-transfer RNA synthetase
-
-
-
-
Glutaminyl-tRNA synthetase
-
-
-
-
Synthetase, glutaminyl-transfer ribonucleate
-
-
-
-
Vegetative specific protein H4
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
-
-
-
-
Aminoacylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamine:tRNAGln ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9075-59-6
-
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 + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
a two-step aminoacylation reaction
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
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 + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.7
L-glutamine
pH and temperature not specified in the publication
0.00019
tRNAGln
pH and temperature not specified in the publication
additional information
additional information
steady-state and transient kinetic analysis
-
additional information
additional information
-
steady-state and transient kinetic analysis
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
L-glutamine
pH and temperature not specified in the publication
1.4
tRNAGln
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.824
L-glutamine
pH and temperature not specified in the publication
7368.4
tRNAGln
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
localization of cytoplasmic GlnRS in mitochondrial Gln-tRNA synthesis
-
localization of cytoplasmic GlnRS in mitochondrial Gln-tRNA synthesis. Saccharomyces cerevisiae imports the cytosolic pathway for Gln-tRNA synthesis into the mitochondrion
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme evolved by gene duplication in early eukaryotes from a nondiscriminating glutamyl-tRNAsynthetase (GluRSND, EC 6.1.1.24) that aminoacylates both tRNAGln and tRNAGlu with glutamate. This ancient GluRS also separately differentiated to exclude tRNAGln as a substrate, and the resulting discriminating GluRS and GlnRS further acquired additional protein domains assisting function in cis (the GlnRS N-terminal Yqey domain) or in trans (the Arc1p protein associating with GluRS), evolutionary modeling, detailed overview. These added domains are absent in contemporary bacterial GlnRS and GluRS. The eukaryote-specific protein domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA. Eukaryotic tRNAGln and tRNAGlu recognition determinants are found in equivalent positions and aremutually exclusive to a significant degree, with key nucleotides located adjacent to portions of the protein structure that differentiated during the evolution of archaeal nondiscriminating GluRS to GlnRS. The added eukaryotic domains arose in response to distinctive selective pressures associated with the greater complexity of the eukaryotic translational apparatus. GluRS and GlnRS are among just four aaRS families (the others are arginyl-tRNA synthetase and class I LysRS) that require the presence of tRNA for synthesis of the aminoacyl adenylate reaction intermediate. Each cytoplasmic GlxRS-tRNA pair has fully lost the ancestral nondiscriminating activity in the course of coevolution, and the more stringent specificities of Saccharomyces cerevisiae GlnRS and GluRS arise from the conserved catalytic portions of each enzyme
additional information
additional information
analysis of the contributions to aminoacylation efficiency made by the N-terminal Yqey domain of Saccharomyces cerevisiae GlnRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview
additional information
-
analysis of the contributions to aminoacylation efficiency made by the N-terminal Yqey domain of Saccharomyces cerevisiae GlnRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Saccharomyces cerevisiae GlnRS contains an N-terminal domain that is conserved in eukaryotic enzymes and is not present in bacterial homologues, The N-terminal domain consists of 187 amino acids organized in two helical subdomains and is followed by an unstructured 26-residue linker that links it with the main catalytic portion of the enzyme, the C-terminal domain, computational modeling
additional information
-
Saccharomyces cerevisiae GlnRS contains an N-terminal domain that is conserved in eukaryotic enzymes and is not present in bacterial homologues, The N-terminal domain consists of 187 amino acids organized in two helical subdomains and is followed by an unstructured 26-residue linker that links it with the main catalytic portion of the enzyme, the C-terminal domain, computational modeling
additional information
-
determination of glutamyl/glutaminyl-tRNA synthetase domain sequences in the proteosome of the organism, classification of proteins into homologous groups by determination and validation of Markov clusters of homologous subsequences, MACHOS, for structure-function analysis, method evaluation, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
microbatch-under-oil method, using 50 mM NH4Br, 50 mM KC2H3O2, 100 mM HEPES (pH 7.5), and 20% (w/v) polyethylene glycol 20000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
truncated enzyme form lacking the NH2-terminal domain, with modest increase in Km value for glutamine and ATP and no difference in kcat for aminoacylation or Km for tRNA
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
IgG Sepharose column chromatography and Superdex HiLoad 16/60 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ludmerer, S.W.; Wright, D.J.; Schimmel, P.
Purification of glutamine tRNA synthetase from Saccharomyces cerevisiae
J. Biol. Chem.
268
5519-5523
1993
Saccharomyces cerevisiae
Mitchell, A.P.; Ludmerer, S.W.
Identification of a glutaminyl-tRNA synthetase mutation in Saccharomyces cerevisiae
J. Bacteriol.
158
530-534
1984
Saccharomyces cerevisiae
Ludmerer, S.W.; Schimmel, P.
Cloning of GLN4: an essential gene that encodes glutaminyl-tRNA synthetase in Saccharomyces cerevisiae
J. Bacteriol.
163
763-768
1985
Saccharomyces cerevisiae
Rinehart, J.; Krett, B.; Rubio, M.A.; Alfonzo, J.D.; Soll, D.
Saccharomyces cerevisiae imports the cytosolic pathway for Gln-tRNA synthesis into the mitochondrion
Genes Dev.
19
583-592
2005
Saccharomyces cerevisiae
Wong, S.; Ragan, M.A.
MACHOS: Markov clusters of homologous subsequences
Bioinformatics
24
i77-i85
2008
Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus
Grant, T.D.; Luft, J.R.; Wolfley, J.R.; Snell, M.E.; Tsuruta, H.; Corretore, S.; Quartley, E.; Phizicky, E.M.; Grayhack, E.J.; Snell, E.H.
The structure of yeast glutaminyl-tRNA synthetase and modeling of its interaction with tRNA
J. Mol. Biol.
425
2480-2493
2013
Saccharomyces cerevisiae (P13188), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P13188)
EXTERNAL LINKS (specific for EC-Number 6.1.1.18)
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