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Information on EC 6.1.1.18 - glutamine-tRNA ligase and Organism(s) Homo sapiens

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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cytosolic glutaminyl-tRNA synthetase
-
GlnRS
Glutamine translase
-
-
-
-
Glutamine--tRNA ligase
-
-
-
-
Glutamine-tRNA synthetase
-
-
-
-
Glutaminyl-transfer ribonucleate synthetase
-
-
-
-
Glutaminyl-transfer RNA synthetase
-
-
-
-
Glutaminyl-tRNA synthetase
glutamyl/glutaminyl-tRNA synthetase
-
-
Synthetase, glutaminyl-transfer ribonucleate
-
-
-
-
Vegetative specific protein H4
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminoacylation
esterification
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamine:tRNAGln ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9075-59-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
show the reaction diagram
additional information
?
-
-
the enzyme interacts with the apoptosis signal-regulating kinase ASK1, which involves the active sites of the enzymes and inhibits AKS1, the association is mediated and enhanced by glutamine, it is inhibited by Fas ligation, the enzyme inhibits ASK1-induced apoptosis
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00053 - 0.0017
tRNAGln
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 0.203
tRNAGln
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.118 - 302.99
tRNAGln
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00024 - 0.00033
recombinant mutant Y57H/R515W enzyme in crude cell extract, pH 7.5, 37°C
0.00028
recombinant mutant G45V/R403W enzyme in crude cell extract, pH 7.5, 37°C
0.00041
recombinant mutant G45V enzyme in crude cell extract, pH 7.5, 37°C
0.00051
recombinant mutant R515W enzyme in crude cell extract, pH 7.5, 37°C
0.00058
recombinant mutant Y57H enzyme in crude cell extract, pH 7.5, 37°C
0.00079 - 0.00083
recombinant wild-type enzyme in crude cell extract, pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
QARS is highly expressed in the developing fetal human cerebral cortex in many cell types
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
human GlnRS is a monomeric class I aminoacyl-tRNA synthetase family member
malfunction
physiological function
cytosolic glutaminyl-tRNA synthetase (GlnRS) is the singular enzyme responsible for translation of glutamine codons
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SYQ_HUMAN
775
0
87799
Swiss-Prot
other Location (Reliability: 4)
B4DDN1_HUMAN
630
0
71738
TrEMBL
other Location (Reliability: 2)
Q53HS0_HUMAN
775
0
87711
TrEMBL
other Location (Reliability: 4)
A0A1B0GVU9_HUMAN
736
0
83783
TrEMBL
Mitochondrion (Reliability: 2)
A8K3A8_HUMAN
775
0
87809
TrEMBL
other Location (Reliability: 4)
Q9BUZ3_HUMAN
618
0
70496
TrEMBL
other Location (Reliability: 1)
B4DNN3_HUMAN
725
0
82246
TrEMBL
other Location (Reliability: 4)
Q96AW5_HUMAN
717
0
81706
TrEMBL
Mitochondrion (Reliability: 2)
Q9H3A5_HUMAN
608
0
69344
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
primary structure
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
the enzyme adopts a boomerang-like shaped structure built of 5 domains, domain organization of the intact enzyme and structure of the functionally important N-terminal domain, modeling of overall structure and domain organization of wild-type, full-length enzyme, structure-function analysis, overview
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified multisynthetase complex (MSC) subcomplex comprising ArgRS, glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)/p43, X-ray diffraction structure determination and analysis
purified recombinant His-tagged wild-type and mutant enzymes, sitting drop vapour diffusion method, apo wild-type GlnRS crystallizes from 0.1 M calcium acetate, 0.1 M Tris, pH 6.0, 12.5% w/v PEG 3350, and 60 mM Gly-Gly-Gly, the Y57H mutant crystallizes from 0.1 M ammonium acetate, 0.1 M Bis-Tris, pH 5.5, and 17% w/v PEG 10 000, and the G45V mutant crystallizes from 0.15 M ammonium acetate, 0.1 M Bis-Tris, pH 5.5, 3% w/v PEG 20 000, and 10 mM EDTA, 16°C, X-ray diffraction strutcure determination and analysis at 2.4 A, 3.3 A, and 2.7 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G45V/R403W
naturally occuring mutation involved in progressive microcephaly, severe seizures in infancy, atrophy of the cerebral cortex and cerebellar vermis, and mild atrophy of the cerebellar hemispheres, the mutant shows a highly reduced aminoacylation activity, heterozygous mutations
H175A
the mutant shows reduced activity compared to the wild-type
K496stop
naturally occuring mutation involved in early-onset epileptic encephalopathy (EOEE), heterozygous mutation leading to a deletion of part of the catalytic domain and the entire anticodon-binding domain, a loss-of-function mutant
R403W
R515W
Y57H/R515W
occuring mutation involved in progressive microcephaly, severe seizures in infancy, atrophy of the cerebral cortex and cerebellar vermis, and mild atrophy of the cerebellar hemispheres, the mutant shows a highly reduced aminoacylation activity, heterozygous mutations
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47.5
melting temperature of the recombinant wild-type enzyme
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography and dialysis
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain Rosetta (DE3)pLysS by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene QARS, genotyping, recombinant expression of codon-optimized His-tagged wild-type and mutant enzymes in Escherichia coli
gene QARS, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta (DE3)pLysS
overexpression of various Myc-tagged enzyme mutants in human embryonic kidney 293 cells
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recombinant expression of the enzyme in Escherichia coli
transient expression of the p.Lys496stop mutant in neuroblastoma 2A cells reveals diminished and aberrantly aggregated expression
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fett, R.; Knippers, R.
The primary structure of human glutaminyl-tRNA synthetase
J. Biol. Chem.
266
1448-1455
1991
Homo sapiens
Manually annotated by BRENDA team
Kim, T.; Park, S.G.; Kim, J.E.; Seol, W.; Ko, Y.G.; Kim, S.
Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex
J. Biol. Chem.
275
21768-21772
2000
Homo sapiens
Manually annotated by BRENDA team
Ko, Y.G.; Kim, E.Y.; Kim, T.; Park, H.; Park, H.S.; Choi, E.J.; Kim, S.
Glutamine-dependent antiapoptotic interaction of human glutaminyl-tRNA synthetase with apoptosis signal-regulating kinase 1
J. Biol. Chem.
276
6030-6036
2001
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Zhang, X.; Ling, J.; Barcia, G.; Jing, L.; Wu, J.; Barry, B.J.; Mochida, G.H.; Hill, R.S.; Weimer, J.M.; Stein, Q.; Poduri, A.; Partlow, J.N.; Ville, D.; Dulac, O.; Yu, T.W.; Lam, A.T.; Servattalab, S.; Rodriguez, J.; Boddaert, N.; Munnich, A.; Colleaux, L.; Zon, L.I.; Soell, D.; Walsh, C.A.; Nabbout, R.
Mutations in QARS, encoding glutaminyl-tRNA synthetase, cause progressive microcephaly, cerebral-cerebellar atrophy, and intractable seizures
Am. J. Hum. Genet.
94
547-558
2014
Homo sapiens (P47897)
Manually annotated by BRENDA team
Kodera, H.; Osaka, H.; Iai, M.; Aida, N.; Yamashita, A.; Tsurusaki, Y.; Nakashima, M.; Miyake, N.; Saitsu, H.; Matsumoto, N.
Mutations in the glutaminyl-tRNA synthetase gene cause early-onset epileptic encephalopathy
J. Hum. Genet.
60
97-101
2015
Homo sapiens (P47897)
Manually annotated by BRENDA team
Ognjenovic, J.; Wu, J.; Matthies, D.; Baxa, U.; Subramaniam, S.; Ling, J.; Simonovic, M.
The crystal structure of human GlnRS provides basis for the development of neurological disorders
Nucleic Acids Res.
44
3420-3431
2016
Homo sapiens (P47897), Homo sapiens
Manually annotated by BRENDA team
Fu, Y.; Kim, Y.; Jin, K.S.; Kim, H.S.; Kim, J.H.; Wang, D.; Park, M.; Jo, C.H.; Kwon, N.H.; Kim, D.; Kim, M.H.; Jeon, Y.H.; Hwang, K.Y.; Kim, S.; Cho, Y.
Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation
Proc. Natl. Acad. Sci. USA
111
15084-15089
2014
Homo sapiens (P47897)
Manually annotated by BRENDA team