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Literature summary for 6.1.1.20 extracted from

  • Kast, P.; Hennecke, H.
    Amino acid substrate specificity of Escherichia coli phenylalanyl-tRNA synthetase altered by distinct mutations (1991), J. Mol. Biol., 222, 99-124.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
mutant genes Escherichia coli

Protein Variants

Protein Variants Comment Organism
A293X p-fluorophenylalanine-resistant strain with Ala294Ser, Ala293X or Ala295X mutation. Phe293 and Phe295 are not directly involved in substrate binding, but replacements of these residues affect PheRS stability. Exchanges at position 294 alter the binding of Phe, and certain mutants show pronounced changes in specificity towards Phe analogues Escherichia coli
A294S p-fluorophenylalanine-resistant strain with Ala294Ser, Ala293X or Ala295X mutation. Phe293 and Phe295 are not directly involved in substrate binding, but replacements of these residues affect PheRS stability. Exchanges at position 294 alter the binding of Phe, and certain mutants show pronounced changes in specificity towards Phe analogues Escherichia coli
A295X p-fluorophenylalanine-resistant strain with Ala294Ser, Ala293X or Ala295X mutation. Phe293 and Phe295 are not directly involved in substrate binding, but replacements of these residues affect PheRS stability. Exchanges at position 294 alter the binding of Phe, and certain mutants show pronounced changes in specificity towards Phe analogues Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
p-fluorophenylalanine-resistant strain with Ala294Ser mutation
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-phenylalanine + tRNAPhe
-
Escherichia coli AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
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