Isoleucine–tRNA ligase
In enzymology, an isoleucine–tRNA ligase is an enzyme that catalyzes a two-step reaction in which isoleucine is attached to its corresponding tRNA molecule:
The 3 substrates of this enzyme are ATP, -isoleucine, and tRNA, whereas its 3 products are AMP, diphosphate, and -isoleucyl-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 -isoleucine:tRNA ligase . Other names in common use include isoleucyl-tRNA synthetase, isoleucyl-transfer ribonucleate synthetase, isoleucyl-transfer RNA synthetase, isoleucine-transfer RNA ligase, isoleucine-tRNA synthetase, and isoleucine translase. This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-tRNA biosynthesis.