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Information on EC 6.1.1.B3 - glutamyl-Q-tRNA(Asp) ligase
for references in articles please use BRENDA:EC6.1.1.B3
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preliminary BRENDA-supplied EC number
EC Tree 6 Ligases
6.1 Forming carbon-oxygen bonds
6.1.1 Ligases forming aminoacyl-tRNA and related compounds
6.1.1.B3 glutamyl-Q-tRNA(Asp) ligase
The enzyme appears in viruses and cellular organisms
showSynonyms
glutamyl-queuosine-trnaasp synthetase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Glu-Q-RS
GluQ-RS
glutamyl queuosine-tRNAAsp synthetase
glutamyl-queuosine-tRNAAsp synthetase
YadB
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamate + tRNAAsp = AMP + diphosphate + L-glutamyl-tRNAAsp
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:tRNAAsp ligase (AMP-forming)
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamate + tRNA
AMP + diphosphate + L-glutamyl-tRNA
Substrates: acceptor is unfractionated RNA
Products: the activation step of L-glutamate is tRNA-independent
Products: the activation step of L-glutamate is tRNA-independent
?
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
Substrates: enzyme YadB activates glutamate in the absence of tRNA and transfers the activated glutamate not on tRNAGlu but instead on tRNAAsp. tRNAAsp is able to accept two amino acids: aspartate charged by aspartyl-tRNA synthetase and glutamate charged byYadB. YadB transfers the activated glutamate on the cyclopenthene-diol ring of the modified nucleoside queuosine posttranscriptionally inserted at the wobble position of the anticodon-loop to form glutamylqueuosine
Products: -
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ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
Substrates: -
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ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
-
Substrates: the enzyme glutamylates the queuosine Q34 nucleotide of the anticodon of tRNAAsp
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ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
-
Substrates: -
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?
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
Shigella flexneri 2457T / ATCC 700930
-
Substrates: -
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additional information
?
-
Substrates: among Escherichia coli tRNAs containing queuosine in the wobble position, only tRNAAsp is substrate ofYadB. No substrate: D-glutamate
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additional information
?
-
Substrates: enzyme does not catalyse attachment of the activated L-glutamate to Escherichia coli tRNAGlu
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additional information
?
-
Substrates: Glu-Q-RS glutamylates the Q34 residue of the anticodon of tRNAAsp, hence it is a tRNA hypermodifying enzyme
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additional information
?
-
-
Substrates: the enzyme cannot aminoacylate tRNAGlu in vitro
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
-
Substrates: the enzyme glutamylates the queuosine Q34 nucleotide of the anticodon of tRNAAsp
Products: -
Products: -
?
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
Shigella flexneri 2457T / ATCC 700930
-
Substrates: -
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
enzyme possesses a Zn2+ ion located in the putative tRNA acceptor stem-binding domain. The Zn2+ ion is coordinated by three cysteine and a tyrosine ligand
Zn2+
required, tetracoordinated to residues Cys101, Cys103, Cys119 and Tyr115. The zinc ion has a high impact on the enzyme structure and function. Enzyme Glu-Q-RS contain a single zinc-binding site in their putative tRNA acceptor stem-binding domain. Quantification by X-ray fluorescence spectrometry technique. Absence of saturating zinc in solution displays dramatic change in the solubility of the protein
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutamol-adenosine monophosphate
non-hydrolyzable analog of glutamyl-AMP, inhibits the ATP-diphosphate exchange competitively with respect to L-glutamate and ATP
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0002
glutamol-adenosine monophosphate
pH 7.2, 37°C, cosubstrate ATP
0.00044
glutamol-adenosine monophosphate
pH 7.2, 37°C, cosubstrate L-glutamate
0.2
glutamol-adenosine monophosphate
pH 7.2, 37°C, substrate ATP, activation of L-glutamate
0.44
glutamol-adenosine monophosphate
pH 7.2, 37°C, substrate L-glutamate, activation of L-glutamate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
glutamyl-QtRNA Asp synthetase (Glu-Q-RS) from Escherichia coli is a paralogue of glutamyl-tRNA synthetase, GluRS, both containing one zinc ion
malfunction
Absence of saturating zinc in solution displays dramatic change in the solubility of the protein
physiological function
physiological function
-
the enzyme play a role in some stress responses but is not essential for invasion or intracellular growth of Shigella flexneri
physiological function
Shigella flexneri 2457T / ATCC 700930
-
the enzyme play a role in some stress responses but is not essential for invasion or intracellular growth of Shigella flexneri
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GLUQ_ECOLI
Escherichia coli (strain K12)
308
0
34868
Swiss-Prot
other Location (Reliability: 5)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
determination and comparisons of three-dimensional structures of free enzyme Glu-Q-RS and Glu-bound Glu-Q-RS
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
determination of strucure by molecular replacement, to 1.5 A resolution. Enzyme possesses a Zn2+ located in the putative tRNA acceptor stem-binding domain. The Zn2+ ion is coordinated by three cysteine and a tyrosine ligand
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C101S/C103S
site-directed mutagenesis, in the mutant the zinc ion still remains coordinated but the variant becomes structurally labile and acquires aggregation capacity. The extent of aggregation of the protein is significantly decreased in presence of the small substrates and more particularly by adenosine triphosphate. Addition of zinc increases significantly the solubility of the variant. The aminoacylation assay reveals a decrease in activity of the mutant even after addition of zinc as compared to the wild-type, although the secondary structure of the protein is not altered. Unlike wild type Glu-Q-RS, the mutant shows a strong tendency to aggregate in solution at room temperature, addition of a saturating concentration of the small substrate ATP and/or L-Glu decreases the rate of aggregation of C101S/C103S Glu-Q-RS, ATP has the most efficient effect
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
gene gluQ, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Rosetta II
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dubois, D.Y.; Blaise, M.; Becker, H.D.; Campanacci, V.; Keith, G.; Giege, R.; Cambillau, C.; Lapointe, J.; Kern, D.
An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli yadB gene glutamylates specifically tRNAAsp
Proc. Natl. Acad. Sci. USA
101
7530-7535
2004
Escherichia coli (P27305)
brenda
Blaise, M.; Becker, H.; Lapointe, J.; Cambillau, C.; Giege, R.; Kern, D.
Glu-Q-tRNAAsp synthetase coded by the yadB gene, a new paralog of aminoacyl-tRNA synthetase that glutamylates tRNAAsp anticodon
Biochimie
87
847-861
2005
Escherichia coli (P27305)
brenda
Campanacci, V.; Dubois, D.Y.; Becker, H.D.; Kern, D.; Spinelli, S.; Valencia, C.; Pagot, F.; Salomoni, A.; Grisel, S.; Vincentelli, R.; Bignon, C.; Lapointe, J.; Giege, R.; Cambillau, C.
The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA synthetase like activity
J. Mol. Biol.
337
273-283
2004
Escherichia coli (P27305)
brenda
Caballero, V.C.; Toledo, V.P.; Maturana, C.; Fisher, C.R.; Payne, S.M.; Salazar, J.C.
Expression of Shigella flexneri gluQ-rs gene is linked to dksA and controlled by a transcriptional terminator
BMC Microbiol.
12
226
2012
Shigella flexneri, Shigella flexneri 2457T / ATCC 700930
brenda
Ray, S.; Banerjee, V.; Blaise, M.; Banerjee, B.; Das, K.P.; Kern, D.; Banerjee, R.
Critical role of zinc ion on E. coli glutamyl-queuosine-tRNA(Asp) synthetase (Glu-Q-RS) structure and function
Protein J.
33
143-149
2014
Escherichia coli (P27305)
brenda
Ray, S.; Blaise, M.; Roy, B.; Ghosh, S.; Kern, D.; Banerjee, R.
Fusion with anticodon binding domain of GluRS is not sufficient to alter the substrate specificity of a chimeric Glu-Q-RS
Protein J.
33
48-60
2014
Escherichia coli
brenda
EXTERNAL LINKS (specific for EC-Number 6.1.1.B3)
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