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Literature summary for 6.1.1.20 extracted from

  • Ling, J.; Yadavalli, S.S.; Ibba, M.
    Phenylalanyl-tRNA synthetase editing defects result in efficient mistranslation of phenylalanine codons as tyrosine (2007), RNA, 13, 1881-1886.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.20

Protein Variants

Protein Variants Comment Organism
additional information editing-defective PheRS variants display significantly increased tyrosylation levels in the presence of EF-Tu, likely through elongation factor Tu, EF-Tu, protection of synthesized Tyr-tRNAPhe from hydrolysis, overview Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information aminoacylation kinetics with Phe and Tyr Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-phenylalanine + tRNAPhe Escherichia coli cognate amino acid charging AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?
ATP + L-tyrosine + tRNAPhe Escherichia coli PheRS misactivates Tyr but is able to correct the mistake using a proofreading editing activity, overview, after evading editing by PheRS, Tyr-tRNAPhe is recognized by elongation factor Tu EF-Tu, involved in translational quality control including substrate selection by aminoacyl-tRNA synthetases, as efficiently as the cognate Phe-tRNAPhe, overview AMP + diphosphate + L-tyrosinyl-tRNAPhe
-
 ?
additional information Escherichia coli PheRS editing is the major proofreading step that prevents infiltration of Tyr into Phe codons during translation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-phenylalanine + tRNAPhe cognate amino acid charging Escherichia coli AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?
ATP + L-phenylalanine + tRNAPhe cognate amino acid charging onto tRNAPheUUU and tRNAPheUUC Escherichia coli AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?
ATP + L-tyrosine + tRNAPhe PheRS misactivates Tyr but is able to correct the mistake using a proofreading editing activity, overview, after evading editing by PheRS, Tyr-tRNAPhe is recognized by elongation factor Tu EF-Tu, involved in translational quality control including substrate selection by aminoacyl-tRNA synthetases, as efficiently as the cognate Phe-tRNAPhe, overview Escherichia coli AMP + diphosphate + L-tyrosinyl-tRNAPhe
-
 ?
additional information PheRS editing is the major proofreading step that prevents infiltration of Tyr into Phe codons during translation Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
Phenylalanyl-tRNA synthetase
-
 Escherichia coli
PheRS
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at, aminoaclyation Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at, aminoaclyation Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli