6.1.1.24: glutamate-tRNAGln ligase
This is an abbreviated version!
For detailed information about glutamate-tRNAGln ligase, go to the full flat file.
Word Map on EC 6.1.1.24
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6.1.1.24
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glutaminyl-trna
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aminoacylation
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gln-trnagln
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trnaglu
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aminoacyl-trnas
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synthetases
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amidotransferase
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glutamylates
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archaea
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transamidation
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gatcab
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anticodons
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thermautotrophicus
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glutaminylated
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methanothermobacter
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mischarged
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apicoplast
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isoacceptors
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glurss
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eukarya
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anticodon-binding
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berghei
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heterotrimeric
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arc1p
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lupinus
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luteus
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misaminoacylated
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noncognate
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drug development
- 6.1.1.24
- glutaminyl-trna
- aminoacylation
- gln-trnagln
- trnaglu
- aminoacyl-trnas
- synthetases
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amidotransferase
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glutamylates
- archaea
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transamidation
- gatcab
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anticodons
- thermautotrophicus
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glutaminylated
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methanothermobacter
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mischarged
- apicoplast
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isoacceptors
- glurss
- eukarya
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anticodon-binding
- berghei
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heterotrimeric
- arc1p
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lupinus
- luteus
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misaminoacylated
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noncognate
- drug development
Reaction
Synonyms
Glu-Q-RS, GluRS, GluRS1, GluRS2, GluRSND, glutamyl-queuosine tRNAAsp synthetase, Glutamyl-tRNA synthetase, GlxRS, ND-GluRS, non-discriminating GluRS, non-discriminating glutamyl-tRNA synthetase, nondiscriminating GluRS, nondiscriminating glutamyl-tRNA synthetase, Pf3D7_1357200, TM1875
ECTree
6.1.1.24 glutamate-tRNAGln ligaseAdvanced search results
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results (General Information
General Information on EC 6.1.1.24 - glutamate-tRNAGln ligase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
metabolism
the malaria parasite Plasmodium falciparum apicoplast indirect aminoacylation pathway utilizes a non-discriminating glutamyl-tRNA synthetase to synthesize Glu-tRNAGln and a glutaminyl-tRNA amidotransferase to convert Glu-tRNAGln to Gln-tRNAGln
physiological function
additional information
evolution
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evolution in the GlxRS family, overview. Two pathways exist for the formation of Gln-tRNAGln. The evolutionarily older indirect route utilizes a non-discriminating glutamyl-tRNA synthetase, ND-GluRS, that can form both Glu-tRNAGlu and Glu-tRNAGln. The Glu-tRNAGln is then converted to Gln-tRNAGln by an amidotransferase. ND-GluRS is the evolutionary predecessor of both the glutaminyl-tRNA synthetase, GlnRS, and the eukaryotic discriminating GluRS
evolution
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ND-GluRS is a class I aminoacyl-tRNA synthetase
physiological function
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for synthesis of Gln-tRNAGln, a two-step process is required: the non-discriminating glutamyl-tRNA synthetase, ND-GluRS, forms Glu-tRNAGln, while the heterodimeric amidotransferase GatDE converts this mischarged tRNA to Gln-tRNAGln. A similar complex for Gln-tRNAGln formation in Methanothermobacter thermautotrophicus that allows the mischarged Glu-tRNAGln made by the tRNA synthetase to be channeled to the amidotransferase. The association of archaeal ND-GluRS with GatDE sequesters the tRNA synthetase for Gln-tRNAGln formation, with GatDE reducing the affinity of ND-GluRS for tRNAGlu by at least 13fold. The archaeal complex does not require tRNA for its formation, is not stable through product (Gln-tRNAGln) formation, and has no major effect on the kinetics of tRNAGln glutamylation nor transamidation
physiological function
ND-GluRS produces the intermediate Glu-tRNAGln, which is converted to Gln-tRNAGln by Glu-tRNAGln amidotransferase. GluRS avoids competition with Glu-tRNAGln amidotransferase GatCAB and glutamylates tRNAGln
physiological function
Plasmodium apicoplast protein synthesis is essential for parasite survival, aminoacyl-tRNA formation is essential for protein synthesis. The malaria parasite Plasmodium falciparum apicoplast indirect aminoacylation pathway utilizes a non-discriminating glutamyl-tRNA synthetase to synthesize Glu-tRNAGln and a glutaminyl-tRNA amidotransferase to convert Glu-tRNAGln to Gln-tRNAGln. Formation of apicoplast Gln-tRNAGln proceeds via indirect aminoacylation. The nucleus-encoded non-discriminating GluRS is imported into the apicoplast is responsible for the formation of misacylated Glu-tRNAGln and is essential in the erythrocytic stages
additional information
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a hybrid enzyme, in which 23 amino acids from the catalytic domain of Escherichia coli glutaminyl-tRNA synthetase, GlnRS, are replaced with the corresponding residues of human glutamyl-tRNA synthetase, GluRS, synthesizes Glu-tRNAGln over 104fold more efficiently than GlnRS. Identification of residues involved in improving complementarity for glutamate and in communicating between amino acid and tRNA binding sites, overview
additional information
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ND-GluRS:GatDE complex formation and structure, detailed overview
