Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Turner, J.M.; Graziano, J.; Spraggon, G.; Schultz, P.G.
    Structural plasticity of an aminoacyl-tRNA synthetase active site (2006), Proc. Natl. Acad. Sci. USA, 103, 6483-6488.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.1 DNA and amino acid sequence determination and analysis of two enzymes types, expression of tyrosyl aminoacyl-tRNA synthetase as C-terminally His6-tagged enzyme in Escherichia coli Methanocaldococcus jannaschii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.1 purified recombinant C-terminally His6-tagged tyrosyl aminoacyl-tRNA synthetase, sitting-drop vapor diffusion technique, 15 mg/ml protein in 20 mM Tris, pH 8.5, 50 mM NaCl, 10 mM 2-mercaptoethanol, crystals are grown either in the presence of 2 mM 4-bromophenylalanine or 3-(2-naphthyl)alanine at 20°C or 4°C, against a mother liquor composed of 16-20% PEG 300, 3-5% PEG 8000, 100 mM Tris, pH 8.8-pH 8.2, and 10% glycerol by mixing of equla volumes, X-ray diffraction structure determination and analysis at 1.9 A resolution Methanocaldococcus jannaschii

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.1 additional information structural comparison of wild-type enzyme and naturally occuring mutant variant p-BrPhe TyrRSs, the latter shows an altered substrate specificity charging 4-bromophenylalanine, 3-(2-naphthyl)alanine, or 4-acetylphenylalanine, overview Methanocaldococcus jannaschii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.1 Mg2+
-
 Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.1 ATP + 3-(2-naphthyl)alanine + tRNATyr Methanocaldococcus jannaschii activity of a natural mutant enzyme, NpAla TyrRS activity AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
-
 ?
6.1.1.1 ATP + 4-acetylphenylalanine + tRNATyr Methanocaldococcus jannaschii activity of a natural mutant enzyme AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
-
 ?
6.1.1.1 ATP + 4-bromophenylalanine + tRNATyr Methanocaldococcus jannaschii activity of a natural mutant enzyme, p-BrPhe TyrRS activity AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
-
 ?
6.1.1.1 ATP + L-tyrosine + tRNATyr Methanocaldococcus jannaschii wild-type activity AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.1 Methanocaldococcus jannaschii Q57834
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.1 recombinant C-terminally His6-tagged tyrosyl aminoacyl-tRNA synthetase from Escherichia coli by nickel affinity and ion exchange chromatography to homogeneity Methanocaldococcus jannaschii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.1 ATP + 3-(2-naphthyl)alanine + tRNATyr activity of a natural mutant enzyme, NpAla TyrRS activity Methanocaldococcus jannaschii AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
-
 ?
6.1.1.1 ATP + 3-(2-naphthyl)alanine + tRNATyr activity of a natural mutant enzyme, NpAla TyrRS activity, altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site Methanocaldococcus jannaschii AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
-
 ?
6.1.1.1 ATP + 4-acetylphenylalanine + tRNATyr activity of a natural mutant enzyme Methanocaldococcus jannaschii AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
-
 ?
6.1.1.1 ATP + 4-acetylphenylalanine + tRNATyr activity of a natural mutant enzyme, altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site Methanocaldococcus jannaschii AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
-
 ?
6.1.1.1 ATP + 4-bromophenylalanine + tRNATyr activity of a natural mutant enzyme, p-BrPhe TyrRS activity Methanocaldococcus jannaschii AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
-
 ?
6.1.1.1 ATP + 4-bromophenylalanine + tRNATyr activity of a natural mutant enzyme, p-BrPhe TyrRS activity, altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site Methanocaldococcus jannaschii AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
-
 ?
6.1.1.1 ATP + L-tyrosine + tRNATyr wild-type activity Methanocaldococcus jannaschii AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?
6.1.1.1 additional information high degree of structural plasticity that is observed in these aminoacyl-tRNA synthetases, overview Methanocaldococcus jannaschii ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.1 NpAla TyrRS
-
 Methanocaldococcus jannaschii
6.1.1.1 p-BrPhe TyrRS
-
 Methanocaldococcus jannaschii
6.1.1.1 tyrosyl aminoacyl-tRNA synthetase
-
 Methanocaldococcus jannaschii
6.1.1.1 TyrRS
-
 Methanocaldococcus jannaschii

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.1 ATP
-
 Methanocaldococcus jannaschii