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Information on EC 6.1.1.24 - glutamate-tRNAGln ligase and Organism(s) Helicobacter pylori and UniProt Accession O25360

for references in articles please use BRENDA:EC6.1.1.24
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EC Tree
IUBMB Comments
When this enzyme acts on tRNAGlu, it catalyses the same reaction as EC 6.1.1.17, glutamate---tRNA ligase. It has, however, diminished discrimination, so that it can also form glutamyl-tRNAGln. This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon . This accounts for the ability of this enzyme in, for example, Bacillus subtilis, to recognize both tRNA1Gln (UUG anticodon) and tRNAGlu (UUC anticodon) but not tRNA2Gln (CUG anticodon). The ability of this enzyme to recognize both tRNAGlu and one of the tRNAGln isoacceptors derives from their sharing a major identity element, a hypermodified derivative of U34 (5-methylaminomethyl-2-thiouridine). The glutamyl-tRNAGln is not used in protein synthesis until it is converted by EC 6.3.5.7, glutaminyl-tRNA synthase (glutamine-hydrolysing), into glutaminyl-tRNAGln.
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This record set is specific for:
Helicobacter pylori
UNIPROT: O25360
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Word Map
The taxonomic range for the selected organisms is: Helicobacter pylori
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
glu-q-rs, nd-glurs, non-discriminating glutamyl-trna synthetase, glxrs, nondiscriminating glurs, tm1875, non-discriminating glurs, nondiscriminating glutamyl-trna synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GluRS
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-
-
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nondiscriminating glutamyl-tRNA synthetase
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminoacylation
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-
-
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:tRNAGlx ligase (AMP-forming)
When this enzyme acts on tRNAGlu, it catalyses the same reaction as EC 6.1.1.17, glutamate---tRNA ligase. It has, however, diminished discrimination, so that it can also form glutamyl-tRNAGln. This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon [1]. This accounts for the ability of this enzyme in, for example, Bacillus subtilis, to recognize both tRNA1Gln (UUG anticodon) and tRNAGlu (UUC anticodon) but not tRNA2Gln (CUG anticodon). The ability of this enzyme to recognize both tRNAGlu and one of the tRNAGln isoacceptors derives from their sharing a major identity element, a hypermodified derivative of U34 (5-methylaminomethyl-2-thiouridine). The glutamyl-tRNAGln is not used in protein synthesis until it is converted by EC 6.3.5.7, glutaminyl-tRNA synthase (glutamine-hydrolysing), into glutaminyl-tRNAGln.
CAS REGISTRY NUMBER
COMMENTARY hide
9068-76-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
show the reaction diagram
GluRS2
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-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GluRS2
Uniprot
Manually annotated by BRENDA team
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E334R/G417T/
mutant of GluRS2 specifically and more robustly aminoacylates tRNAGlu1 instead of tRNAGln
G417T
mutant GluRS2 shows weak activity towards tRNAGlu1
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nunez, H.; Lefimil, C.; Min, B.; Soll, D.; Orellana, O.
In vivo formation of glutamyl-tRNA(Gln) in Escherichia coli by heterologous glutamyl-tRNA synthetases
FEBS Lett.
557
133-135
2004
Acidithiobacillus ferrooxidans, Helicobacter pylori
Manually annotated by BRENDA team
Lee, J.; Hendrickson, T.L.
Divergent anticodon recognition in contrasting glutamyl-tRNA synthetases
J. Mol. Biol.
344
1167-1174
2004
Helicobacter pylori (O25360), Helicobacter pylori ATCC 700392 (O25360)
Manually annotated by BRENDA team
Salazar, J.C.; Ahel, I.; Orellana, O.; Tumbula-Hansen, D.; Krieger, R.; Daniels, L.; Soll, D.
Coevolution of an aminoacyl-tRNA synthetase with its tRNA substrates
Proc. Natl. Acad. Sci. USA
100
13863-13868
2003
Acidithiobacillus ferrooxidans, Helicobacter pylori, Acidithiobacillus ferrooxidans GluRS1, Helicobacter pylori GluRS2, Acidithiobacillus ferrooxidans GluRS2
Manually annotated by BRENDA team