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6.1.1.20: phenylalanine-tRNA ligase

This is an abbreviated version!
For detailed information about phenylalanine-tRNA ligase, go to the full flat file.

Word Map on EC 6.1.1.20

Reaction

ATP
+
L-phenylalanine
+
tRNAPhe
=
AMP
+
diphosphate
+
L-phenylalanyl-tRNAPhe

Synonyms

CML33, ctPheRS, cytoplasmic phenylalanyl-tRNA synthetase, cytosolic phenylalanyl-tRNA synthetase, cytosolic PheRS, EcPheRS, FARS2, FRS, hcPheRS, HSPC173, L-Phenylalanyl-tRNA synthetase, mitochondrial phenylalanyl-tRNA synthetase, mitochondrial PheRS, mitPheRS, More, mtPheRS, p-azido-phenylalanyl-tRNA synthetase, pAzFRS, Phe-RS, Phenylalanine translase, phenylalanine tRNA synthetase, Phenylalanine--tRNA ligase, Phenylalanine-tRNA synthetase, Phenylalanyl transfer ribonucleic acid synthetase, Phenylalanyl-transfer ribonucleate synthetase, Phenylalanyl-transfer RNA ligase, Phenylalanyl-transfer RNA synthetase, Phenylalanyl-tRNA ligase, Phenylalanyl-tRNA synthetase, PheRS, PheRS-alpha, Synthetase, phenylalanyl-transfer ribonucleate

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.20 phenylalanine-tRNA ligase

General Information

General Information on EC 6.1.1.20 - phenylalanine-tRNA ligase

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
architecture of four helix-bundle interface, characteristic of class IIc heterotetrameric aaRSs, is changed, each of the two long helices belonging to CLM transformed into the coil-short helix structural fragments. The N-terminal domain of the alpha-subunit in EcPheRS forms compact triple helix domain
malfunction
physiological function
cytosolic phenylalanyl-tRNA synthetase exerts control over the translation accuracy, hydrolyzing misacylated products, while the monomeric mitochondrial enzyme lacks the editing activity