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Literature summary for 6.1.1.20 extracted from

  • Finarov, I.; Moor, N.; Kessler, N.; Safro, M.
    Crystallization and X-ray analysis of human cytoplasmic phenylalanyl-tRNA synthetase (2009), Acta Crystallogr. Sect. F, 65, 93-97.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
the two subunits of hcPheRS are cloned into two different plasmids, the alpha subunit, residues 1-508, into the vector pET21b+, the beta-subunit, residues 1-589, into pET28b+, for expression in Escherichia coli BLRDE3 cells, no affinity tag is used Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
the structure of human cytoplasmic phenylalanyl-tRNA synthetase is determined to a resolution of 3.3 A Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
247000
-
heterotetramer Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O95363
-
-

Purification (Commentary)

Purification (Comment) Organism
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 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-phenylalanine + tRNAPhe
-
Homo sapiens AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
?

Subunits

Subunits Comment Organism
heterotetramer two alpha and two beta subunits Homo sapiens

Synonyms

Synonyms Comment Organism
cytoplasmic phenylalanyl-tRNA synthetase
-
Homo sapiens
cytosolic phenylalanyl-tRNA synthetase
-
Homo sapiens
hcPheRS
-
Homo sapiens
Phenylalanyl-tRNA synthetase
-
Homo sapiens
PheRS
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
Homo sapiens