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In enzymology, a leucine-tRNA ligase () is an enzyme that catalyzes the chemical reaction :ATP + L-leucine + tRNALeu AMP + diphosphate + L-leucyl-tRNALeu The 3 substrates of this enzyme are ATP, L-leucine, and tRNA(Leu), whereas its 3 products are AMP, diphosphate, and L-leucyl-tRNA(Leu). 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-leucine:tRNALeu ligase (AMP-forming). Other names in common use include leucyl-tRNA synthetase, leucyl-transfer ribonucleate synthetase, leucyl-transfer RNA synthetase, leucyl-transfer ribonucleic acid synthetase, leucine-tRNA synthetase, and leucine translase. This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-trna biosynthesis. ==Structural studies== As of late 2007, 5 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「Leucine—tRNA ligase」の詳細全文を読む スポンサード リンク
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