Phenylalanine—tRNA ligase explained

Phenylalanine—tRNA ligase
Ec Number:	6.1.1.20
Cas Number:	9055-66-7
Go Code:	0004826

Symbol:	FDX-ACB
Ferredoxin-fold anticodon binding domain
Pfam:	PF03147
Interpro:	IPR005121
Scop:	1pys

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

ATP + L-phenylalanine + tRNA^Phe

\rightleftharpoons AMP + diphosphate + L-phenylalanyl-tRNA^Phe

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, 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.

Phenylalanine-tRNA synthetase (PheRS) is known to be among the most complex enzymes of the aaRS (Aminoacyl-tRNA synthetase) family. Bacterial and mitochondrial PheRSs share a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents a canonical double split alpha+beta motif having no insertions. The FDX-ACB domain displays a typical RNA recognition fold (RRM) formed by the four-stranded antiparallel beta sheet, with two helices packed against it.^{[1] [2] [3] [4] [5]}

Structural studies

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

Further reading

• Stulberg MP . 1967 . The isolation and properties of phenylalanyl ribonucleic acid synthetase from Escherichia coli B . J. Biol. Chem. . 242 . 1060 - 4 . 5335910 . 5 .

Notes and References

1. Mosyak L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG . Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus . Nat. Struct. Biol. . 2 . 7 . 537–47 . July 1995 . 7664121 . 10.1038/nsb0795-537. 13042127 .
2. Goldgur Y, Mosyak L, Reshetnikova L, Ankilova V, Lavrik O, Khodyreva S, Safro M . The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe . Structure . 5 . 1 . 59–68 . January 1997 . 9016717 . 10.1016/s0969-2126(97)00166-4. free .
3. Rodova M, Ankilova V, Safro MG . Human phenylalanyl-tRNA synthetase: cloning, characterization of the deduced amino acid sequences in terms of the structural domains and coordinately regulated expression of the alpha and beta subunits in chronic myeloid leukemia cells . Biochem. Biophys. Res. Commun. . 255 . 3 . 765–73 . February 1999 . 10049785 . 10.1006/bbrc.1999.0141 .
4. Moor N, Lavrik O, Favre A, Safro M . Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA end . Biochemistry . 42 . 36 . 10697–708 . September 2003 . 12962494 . 10.1021/bi034732q .
5. Klipcan L, Levin I, Kessler N, Moor N, Finarov I, Safro M . The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase . Structure . 16 . 7 . 1095–104 . July 2008 . 18611382 . 10.1016/j.str.2008.03.020 . free .