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-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.
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^Moor N, Lavrik O, Favre A, Safro M (September 2003). "Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA end". Biochemistry. 42 (36): 10697–708. doi:10.1021/bi034732q. PMID12962494.
^Klipcan L, Levin I, Kessler N, Moor N, Finarov I, Safro M (July 2008). "The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase". Structure. 16 (7): 1095–104. doi:10.1016/j.str.2008.03.020. PMID18611382.