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Words near each other
・ Glutamate receptor-interacting protein
・ Glutamate synthase (ferredoxin)
・ Glutamate synthase (NADH)
・ Glutamate synthase (NADPH)
・ Glutamate-1-semialdehyde
・ Glutamate-1-semialdehyde 2,1-aminomutase
・ Glutamate-5-semialdehyde
・ Glutamate-5-semialdehyde dehydrogenase
・ Glutamate-glutamine cycle
・ Glutamatergic
・ Glutamate–cysteine ligase
・ Glutamate—ethylamine ligase
・ Glutamate—methylamine ligase
・ Glutamate—prephenate aminotransferase
・ Glutamate—putrescine ligase
Glutamate—tRNA ligase
・ Glutamate—tRNA(Gln) ligase
・ Glutamic acid
・ 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)


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

In enzymology, a glutamate-tRNA ligase () is an enzyme that catalyzes the chemical reaction
:ATP + L-glutamate + tRNAGlu \rightleftharpoons AMP + diphosphate + L-glutamyl-tRNAGlu
The 3 substrates of this enzyme are ATP, L-glutamate, and tRNA(Glu), whereas its 3 products are AMP, diphosphate, and L-glutamyl-tRNA(Glu).
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-glutamate:tRNAGlu ligase (AMP-forming). Other names in common use include glutamyl-tRNA synthetase, glutamyl-transfer ribonucleate synthetase, glutamyl-transfer RNA synthetase, glutamyl-transfer ribonucleic acid synthetase, glutamate-tRNA synthetase, and glutamic acid translase. This enzyme participates in 3 metabolic pathways: glutamate metabolism, porphyrin and chlorophyll metabolism, and aminoacyl-trna biosynthesis.
==Structural studies==

As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , and .

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