Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.1.1.17 - glutamate-tRNA ligase and Organism(s) Thermus thermophilus and UniProt Accession P27000

for references in articles please use BRENDA:EC6.1.1.17
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Thermus thermophilus
UNIPROT: P27000 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Thermus thermophilus
The enzyme appears in selected viruses and cellular organisms
Synonyms
glurs, glutaminyl-trna synthetase, glutamyl-trna synthetase, glurs2, trna modifying enzyme, glurs1, glutamyl trna synthetase, discriminating glurs, glursat, d-glurs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Glutamyl-tRNA synthetase
-
GluRS
-
-
-
-
Glutamate--tRNA ligase
-
-
-
-
Glutamate-tRNA synthetase
-
-
-
-
Glutamic acid translase
-
-
-
-
Glutamic acid tRNA ligase
-
-
-
-
Glutamyl tRNA synthetase
-
-
-
-
Glutamyl-transfer ribonucleate synthetase
-
-
-
-
Glutamyl-transfer ribonucleic acid synthetase
-
-
-
-
Glutamyl-transfer RNA synthetase
-
-
-
-
Glutamyl-tRNA synthetase
-
-
-
-
P85
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
Aminoacylation
esterification
-
-
-
-
Aminoacylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:tRNAGlu ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9068-76-2
-
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-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
show the reaction diagram
ATP + L-glutamate + tRNAGlu mutant C36G
AMP + diphosphate + L-glutamyl-tRNAGlu mutant C36G
show the reaction diagram
mutant R358Q, low activity with the wild-type enzyme
-
?
ATP + L-glutamate + tRNAGlu wild-type
AMP + diphosphate + L-glutamyl-tRNAGlu wild-type
show the reaction diagram
enzyme is specific for tRNAGlu
-
?
ATP + L-glutamate + wild type tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
show the reaction diagram
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
show the reaction diagram
additional information
?
-
substrate and co-factor recognition and binding structures, GluRS and tRNAGlu collaborate to form a highly complementary L-glutamate-binding site, the collaborative site is functional, amino acid specificity is generated in the GluRS-tRNA complex, overview
-
-
?
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-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutamol-AMP
competitive inhibition
KCl
-
aminoacylation
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tRNA
GluRS is one of the aminoacyl-tRNA synthetases that require the cognate tRNA for specific amino acid recognition and activation, tRNA serves as the enzyme activator in the first step, and as the substrate in the second step of aminoacylation, overview, On the other hand, the main chain of the glutamate is immature glutamate-binding site in the absence of tRNA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043 - 0.055
tRNAGlu mutant C36G
-
0.0047 - 0.085
wild type tRNAGlu
-
0.023 - 0.23
ATP
0.07 - 0.12
L-Glu
0.0006 - 0.00273
tRNAGlu
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18 - 1.4
tRNAGlu mutant C36G
-
1.5 - 2.1
wild type tRNAGlu
-
additional information
additional information
-
turnover numbers of wild-type and mutant enzymes
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012
glutamol-AMP
pH 7.5, 65°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
-
aminoacylation
8 - 9
-
aminoacylation, in presence of 5 mM Mg2+
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
aminoacylation
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 80
-
about 25% of maximal activity at 50°C and 80°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53901
-
x * 53901, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 53901, calculation from nucleotide sequence
additional information
the pretransition-state quaternary complex, crystal structure analysis, in the GluRS-tRNAGlu-Glu structure, GluRS and tRNAGlu collaborate to form a highly complementary L-glutamate-binding site
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of complexes: 1. GluRS and L-Glu, 2. GluRS, tRNAGlu, and L-Glu, 3. GluRS, tRNAGlu, ATP, and L-glutamol, 4. GluRS, tRNAGlu, and L-glutamyl-sulfamoyl adenosine, by hanging drop vapour diffusion method, 5.0 mg/ml enzyme in 10 mM MOPS-Na buffer, pH 6.5, MgCl2, 5 mM 2-mercaptoethanol, 1% PEG 6000, and 2 mM L-glutamate, equilibration against a 1 ml reservoir solution containing 10% PEG at 4°C, ERS/tRNA/Glu and ERS/tRNA/ESA crystals are prepared by diffusing 1 mM L-glutamate and 0.5 mM glutamyl-sulfamoyl adenosine, i.e. ESA, respectively, into the ERS/tRNA binary complex crystals, ERS/tRNA/ATP/Eol crystals are obtained by adding both 1 mM ATP and 1 mM L-glutamol, i.e. Eol, to drops containing the ERS/tRNA binary complex, X-ray diffraction structure determination and analysis at 1.98 A, 2.4 A, 2.2 A, and 2.69 A resolution, respectively
crystallization of the enzyme in different complexes: 1. non-productively complexed with ATP and L-glutamate, 2. with ATP, 3. with tRNAGlu and ATP, 4. with tRNAGlu and the glutamyl-AMP analogue glutamol-AMP, hanging-drop method, 0.008 ml of 5.0 mg/ml protein in 10 mM Na-MOPS, pH 6.5, 5 mM MgCl2, 2.5 mM 2-mercaptoethanol, 1% PEG 6000, 1-2 mM ATP and/or 2 mM glutamate and/or 0.5 mM glutamol-AMP, plus 1 ml reservoir solution containing 10% PEG 6000 at 4 or 20°C, 3 days or more, X-ray diffraction structure determination at 1.8 A resolution, molecular replacement, and analysis
molecular modeling, internal pKa calculations, and molecular dynamics simulations for consideration of distinct, mechanistically relevant post-transfer states with charged tRNA bound to glutamyl-tRNA synthetase. The transfer of amino acid to tRNA is accompanied by the protonation of AMP to H-AMP. Subsequent migration of proton to water reduces the stability of the complex and loosens the interface both in the presence and in the absence of AMP. The subsequent undocking of AMP or tRNA then proceeds along thermodynamically competitive pathways. Release of the tRNA acceptor stem is further accelerated by the deprotonation of the alpha-ammonium group on the charging amino acid. The proposed general base is Glu41
purified recombinant enzyme in complex with tRNAGlu, hanging-drop vapour diffusion method, precipitant solution contains 37 mM Na-MOPS, pH 6.7, 22% PEG 1500, 37 mM ammonium sulfate, 1% 2-methyl-2,4-pentanediol, 10 mM MgCl2, 5 mM 2-mercaptoethanol, X-ray diffraction structure determination at 2.4 A resolution, and analysis
architectures of class-defining and specific domains
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R358Q
site-directed mutagenesis, exchange of the Arg residue results in a mutant that no longer discriminates between tRNAGlu and tRNAGln anticodons YUC and YUG, respectively
additional information
-
mutant enzymes with higher Km and lower turnover numbers
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nureki, O.; Suzuki, K.; Hara-Yokoyama, M.; Kohno, T.; Matsuzawa, H.; Ohta, T.; Shimizu, T.; Morikawa, K.; Miyazawa, T.; Yokoyama, S.
Glutamyl-tRNA synthetase from Thermus thermophilus HB8. Molecular cloning of the gltX gene and crystallization of the overproducing protein
Eur. J. Biochem.
204
465-472
1992
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Manually annotated by BRENDA team
Tateno, M.; Nureki, O.; Sekine, S.i.; Kaneda, K.; Go, M.; Yokoyama, S.
A three-dimensional structure model of the complex of glutamyl-tRNA synthetase and its cognate tRNA
FEBS Lett.
377
77-81
1995
Thermus thermophilus
Manually annotated by BRENDA team
Nureki, O.; Vassylyev, D.G.; Katayanagi, K.; Shimizu, T.; Sekine, S.i.; Kigawa, T.; Miyazawa, T.; Yokoyama, S.; Morikawa, K.
Architectures of class-defining and specific domains of glutamyl-tRNA synthetase
Science
267
1958-1965
1995
Thermus thermophilus
Manually annotated by BRENDA team
Liu, J.; Lin, S.X.; Blochet, J.E.; Pezolet, M.; Lapointe, J.
The glutamyl-tRNA synthetase of Escherichia coli contains one atom of zinc essential for its native conformation and its catalytic activity
Biochemistry
32
11390-11396
1993
Bacillus subtilis, Escherichia coli, Thermus thermophilus
Manually annotated by BRENDA team
Kohda, D.; Hara, M.; Yokoyama, S.; Miyazawa, T.
Aminoacyl-tRNA synthetases from an extreme thermophile, Thermus thermophilus HB8
Nucleic Acids Symp. Ser.
12
153-154
1983
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Manually annotated by BRENDA team
Hara-Yokoyama, M.; Yokoyama, S.; Miyazawa, T.
Purification and characterization of glutamyl-tRNA synthetase from an extreme thermophile, Thermus thermophilus HB8
J. Biochem.
96
1599-1607
1984
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Manually annotated by BRENDA team
Hara-Yokoyama, M.; Yokoyama, S.; Miyazawa, T.
Conformation change of tRNAGlu in the complex with glutamyl-tRNA synthetase is required for specific binding of L-glutamate
Biochemistry
25
7031-7036
1986
Thermus thermophilus
Manually annotated by BRENDA team
Sekine, S.; Nureki, O.; Dubois, D.Y.; Bernier, S.; Chenevert, R.; Lapointe, J.; Vassylyev, D.G.; Yokoyama, S.
ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding
EMBO J.
22
676-688
2003
Thermus thermophilus (P27000), Thermus thermophilus
Manually annotated by BRENDA team
Sekine, S.; Nureki, O.; Shimada, A.; Vassylyev, D.G.; Yokoyama, S.
Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase
Nat. Struct. Biol.
8
203-206
2001
Thermus thermophilus (P27000), Thermus thermophilus
Manually annotated by BRENDA team
Sekine, S.; Shichiri, M.; Bernier, S.; Chenevert, R.; Lapointe, J.; Yokoyama, S.
Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase
Structure
14
1791-1799
2006
Thermus thermophilus (P27000)
Manually annotated by BRENDA team
Black Pyrkosz, A.; Eargle, J.; Sethi, A.; Luthey-Schulten, Z.
Exit strategies for charged tRNA from GluRS
J. Mol. Biol.
397
1350-1371
2010
Thermus thermophilus (P27000), Thermus thermophilus
Manually annotated by BRENDA team