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・ Glutamic acid (data page)
・ Glutamic protease
・ Glutamin-(asparagin-)ase
・ Glutaminase
・ Glutamine
・ Glutamine (data page)
・ Glutamine amidotransferase
・ Glutamine N-acyltransferase
・ Glutamine N-phenylacetyltransferase
・ Glutamine oxoglutarate aminotransferase
・ Glutamine synthetase
・ Glutamine—fructose-6-phosphate transaminase (isomerizing)
・ Glutamine—phenylpyruvate transaminase
・ Glutamine—pyruvate transaminase
・ Glutamine—scyllo-inositol transaminase
Glutamine—tRNA ligase
・ Glutaminolysis
・ Glutaminyl-peptide cyclotransferase
・ Glutaminyl-tRNA synthase (glutamine-hydrolysing)
・ Glutamyl aminopeptidase
・ Glutamyl endopeptidase
・ Glutamyl endopeptidase II
・ Glutamyl-tRNA reductase
・ Glutaraldehyde
・ Glutarate-semialdehyde dehydrogenase
・ Glutarate—CoA ligase
・ Glutaredoxin
・ Glutaredoxin 2 (bacterial)
・ Glutaric acid
・ Glutaric acidemia type 2


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Glutamine—tRNA ligase : ウィキペディア英語版
Glutamine—tRNA ligase

In enzymology, a glutamine-tRNA ligase () is an enzyme that catalyzes the chemical reaction
:ATP + L-glutamine + tRNAGln \rightleftharpoons AMP + diphosphate + L-glutaminyl-tRNAGln
The 3 substrates of this enzyme are ATP, L-glutamine, and tRNA(Gln), whereas its 3 products are AMP, diphosphate, and L-glutaminyl-tRNA(Gln).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-glutamine:tRNAGln ligase (AMP-forming). Other names in common use include glutaminyl-tRNA synthetase, glutaminyl-transfer RNA synthetase, glutaminyl-transfer ribonucleate synthetase, glutamine-tRNA synthetase, glutamine translase, glutamate-tRNA ligase, glutaminyl ribonucleic acid, and GlnRS. This enzyme participates in glutamate metabolism and aminoacyl-trna biosynthesis.
==Structural studies==

As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , and .

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