Phenylalanine–tRNA ligase
In enzymology, a phenylalanine–tRNA ligase is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are ATP, -phenylalanine, and tRNA, whereas its 3 products are AMP, diphosphate, and -phenylalanyl-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 -phenylalanine:tRNA ligase . Other names in common use include phenylalanyl-tRNA synthetase, phenylalanyl-transfer ribonucleate synthetase, phenylalanine-tRNA synthetase, phenylalanyl-transfer RNA synthetase, phenylalanyl-tRNA ligase, phenylalanyl-transfer RNA ligase, -phenylalanyl-tRNA synthetase, and phenylalanine translase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and aminoacyl-tRNA biosynthesis.
Phenylalanine-tRNA synthetase is known to be among the most complex enzymes of the aaRS family. Bacterial and mitochondrial PheRSs share a ferredoxin-fold anticodon binding domain, which represents a canonical double split alpha+beta motif having no insertions. The FDX-ACB domain displays a typical RNA recognition fold formed by the four-stranded antiparallel beta sheet, with two helices packed against it.