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In enzymology, a threonine-tRNA ligase () is an enzyme that catalyzes the chemical reaction :ATP + L-threonine + tRNAThr AMP + diphosphate + L-threonyl-tRNAThr The 3 substrates of this enzyme are ATP, L-threonine, and tRNA(Thr), whereas its 3 products are AMP, diphosphate, and L-threonyl-tRNA(Thr). 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-threonine:tRNAThr ligase (AMP-forming). Other names in common use include threonyl-tRNA synthetase, threonyl-transfer ribonucleate synthetase, threonyl-transfer RNA synthetase, threonyl-transfer ribonucleic acid synthetase, threonyl ribonucleic synthetase, threonine-transfer ribonucleate synthetase, threonine translase, threonyl-tRNA synthetase, and TRS. This enzyme participates in glycine, serine and threonine metabolism and aminoacyl-trna biosynthesis. ==Structural studies== As of late 2007, 17 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「Threonine—tRNA ligase」の詳細全文を読む スポンサード リンク
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