Leucine–tRNA ligase


In enzymology, a leucine–tRNA ligase is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are ATP, -leucine, and tRNA, whereas its 3 products are AMP, diphosphate, and -leucyl-tRNA.
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 -leucine:tRNA ligase . 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.