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Literature summary for 6.1.1.20 extracted from

  • Yadavalli, S.S.; Klipcan, L.; Zozulya, A.; Banerjee, R.; Svergun, D.; Safro, M.; Ibba, M.
    Large-scale movement of functional domains facilitates aminoacylation by human mitochondrial phenylalanyl-tRNA synthetase (2009), FEBS Lett., 583, 3204-3208.
    View publication on PubMed
Search for more literature for 6.1.1.20

Cloned(Commentary)

Cloned (Comment) Organism
Escherichia coli strain BL21(pArgU218)/pET21c-PheRS expresses C-terminal His6-tagged mtPheRS, RosettaDE3 cells containing pRARE plasmids encoding tRNAs for rare codons are transformed with the mutant mtPheRS plasmid constructs Homo sapiens

Protein Variants

Protein Variants Comment Organism
K33C/T351C mutant, crosslinked catalytic and RNA-binding domains, results in a closed form of mtPheRS that still catalyses ATP-dependent Phe activation, but is no longer able to transfer Phe to tRNA and complete the aminoacylation reaction Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
48000
-
 monomer, determined by SDS-PAGE Homo sapiens
96000
-
 dimer, mutant, crosslinked subunits Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O95363
-
-

Purification (Commentary)

Purification (Comment) Organism
a TALON metal affinity resin column is applied 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
dimer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
mitochondrial phenylalanyl-tRNA synthetase
-
 Homo sapiens
mtPheRS
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens