In enzymology, a leucine—tRNA ligase (EC 6.1.1.4) is an enzyme that catalyzes the chemical reaction
ATP + L-leucine + tRNALeu formula_1 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 1WKB, 1WZ2, 2AJG, 2AJH, and 2AJI.
References.
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