Phenylalanine-tRNA ligase

In enzymology, a phenylalanine-tRNA ligase is an enzyme that catalyzes the chemical reaction


 * ATP + L-phenylalanine + tRNAPhe $$\rightleftharpoons$$ AMP + diphosphate + L-phenylalanyl-tRNAPhe

The 3 substrates of this enzyme are ATP, L-phenylalanine, and tRNA(Phe), whereas its 3 products are AMP, diphosphate, and L-phenylalanyl-tRNA(Phe).

This enzyme belongs to the family of ligases, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-phenylalanine:tRNAPhe ligase (AMP-forming). 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, L-phenylalanyl-tRNA synthetase, and phenylalanine translase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and aminoacyl-trna biosynthesis.

Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , and.