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Information on EC 6.1.1.B3 - glutamyl-Q-tRNA(Asp) ligase and Organism(s) Escherichia coli and UniProt Accession P27305

for references in articles please use BRENDA:EC6.1.1.B3
preliminary BRENDA-supplied EC number
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Escherichia coli
UNIPROT: P27305 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
glutamyl-queuosine-trnaasp synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Glutamyl-Q tRNA(Asp) synthetase
-
glutamyl-queuosine-tRNAAsp synthetase
-
Glu-Q-RS
-
-
glutamyl-queuosine-tRNAAsp synthetase
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:tRNAAsp ligase (AMP-forming)
-
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 + tRNA
AMP + diphosphate + L-glutamyl-tRNA
show the reaction diagram
acceptor is unfractionated RNA
the activation step of L-glutamate is tRNA-independent
-
?
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
show the reaction diagram
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
show the reaction diagram
-
the enzyme glutamylates the queuosine Q34 nucleotide of the anticodon of tRNAAsp
-
-
?
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-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
show the reaction diagram
-
-
-
?
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
show the reaction diagram
-
the enzyme glutamylates the queuosine Q34 nucleotide of the anticodon of tRNAAsp
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutamol-adenosine monophosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17 - 0.5
ATP
0.5 - 6
L-glutamate
0.00015
tRNAAsp
pH 7.2, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2 - 18
L-glutamate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.73
L-glutamate
pH 7.2, 37°C
14700
tRNAAsp
pH 7.2, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0002 - 0.44
glutamol-adenosine monophosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
determination and comparisons of three-dimensional structures of free enzyme Glu-Q-RS and Glu-bound Glu-Q-RS
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene gluQ, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Rosetta II
expressed in Escherichia coli BL21(DE3) cells
-
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team