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In enzymology, an aspartate-tRNA ligase () is an enzyme that catalyzes the chemical reaction :ATP + L-aspartate + tRNAAsp AMP + diphosphate + L-aspartyl-tRNAAsp The 3 substrates of this enzyme are ATP, L-aspartate, and tRNA(Asp), whereas its 3 products are AMP, diphosphate, and L-aspartyl-tRNA(Asp). 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-aspartate:tRNAAsp ligase (AMP-forming). Other names in common use include aspartyl-tRNA synthetase, aspartyl ribonucleic synthetase, aspartyl-transfer RNA synthetase, aspartic acid translase, aspartyl-transfer ribonucleic acid synthetase, and aspartyl ribonucleate synthetase. This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis. ==Structural studies== As of late 2007, 10 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「Aspartate—tRNA ligase」の詳細全文を読む スポンサード リンク
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