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In enzymology, a glutamine-tRNA ligase () is an enzyme that catalyzes the chemical reaction :ATP + L-glutamine + tRNAGln 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 . 抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)』 ■ウィキペディアで「Glutamine—tRNA ligase」の詳細全文を読む スポンサード リンク
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