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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

Purification

Purification on EC 6.1.1.20 - phenylalanine-tRNA ligase

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a TALON metal affinity resin column is applied
ammonium sulfate fractionation is followed by four chromatography columns, anion exchange on a DEAE-Sepharose column, a heparin-Sepharose column, concentrating the protein on a TSK hydrophobic interaction column and finally gel filtration on a column of superfine Sephadex G-200
glutathione Sepharose column chromatography
-
His6-tagged proteins are purified on nickel-nitrilotriacetic acid-agarose
HiTrap Ni2+ chelating column chromatography, Ni-NTA column chromatography and Sephacryl S300 gel filtration
mature mitPheRS in Escherichia coli by streptomycin precipitation, ultrafiltration, anion exchange chromatography and heparin affinity chromatography, followed by ammonium sulfate fractionation, hydrophobic interaction chromatography, and gel filtration, to homogeneity
-
native enzyme from Oxford strain, 50% purity, recombinant enzyme overexpressed in Escherichia coli, over 90% purity
-
Ni-NTA column chromatography
recombinant alpha- and beta-subunit both expressed in Escherichia coli
recombinant His-tagged heterodimers and nontagged subunits from Escherichia coli, over 200fold
-
recombinant His-tagged PheRs from Escherichia coli
recombinant His-tagged proteins from Escherichia coli strain M15 by nickel affinity chromatography, complex formation of the two subunits during purification
-
recombinant N-terminal fragment of the PheRS beta-subunit from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant selenomethionine-labeled N-terminal fragment of the PheRS beta-subunit from Escherichia coli strain B834(DE3) by anion exchange chromatography, adsorption chromatography, and gel filtration
to homogeneity
Methanobacterium thermoautotrophicus
-