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Literature summary extracted from

  • Fukunaga, R.; Yokoyama, S.
    Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase (2006), J. Mol. Biol., 359, 901-912.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.5 expression of His-tagged wild-type and mutants enzymes in Escherichia coli Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.5 IleRS editing domain complexed with the substrate analogues in the pre and post-transfer modes, X-ray diffraction structure determination and analysis at 1.7 A resolution Thermus thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.5 H319A site-directed mutagenesis, Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain, but the mutant shows detectable editing activities against the cognate isoleucine, mechanism, overview Thermus thermophilus
6.1.1.5 T223A site-directed mutagenesis, Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain, but the mutant shows detectable editing activities against the cognate isoleucine, mechanism, overview Thermus thermophilus
6.1.1.5 W227A site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme Thermus thermophilus
6.1.1.5 W227F site-directed mutagenesis, the mutant shows editing activities which are unaltered compared to the wild-type enzyme Thermus thermophilus
6.1.1.5 W227H site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme Thermus thermophilus
6.1.1.5 W227L site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme Thermus thermophilus
6.1.1.5 W227V site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme Thermus thermophilus
6.1.1.5 W227Y site-directed mutagenesis, the mutant shows editing activities which are unaltered compared to the wild-type enzyme Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.5 Mg2+
-
 Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.5 ATP + L-isoleucine + tRNAIle Thermus thermophilus
-
 AMP + diphosphate + L-isoleucyl-tRNAIle
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.5 Thermus thermophilus P56690
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.5 recombinant His-tagged wild-type and mutants enzymes from Escherichia coli by nickel affinity chromatography Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.5 ATP + L-isoleucine + tRNAIle
-
 Thermus thermophilus AMP + diphosphate + L-isoleucyl-tRNAIle
-
 ?
6.1.1.5 ATP + L-isoleucine + tRNAIle substrate recognition mechanisms of IleRS are characterized by the active-site rearrangement between the two editing modes, overview, the editing domain contributes to accurate aminoacylation by hydrolyzing the mis-synthesized intermediate, valyl-adenylate, in the pre-transfer editing mode and the incorrect final product, valyl-tRNAIle, in the post-transfer editing mode, Trp227 with its aromatic ring is important Thermus thermophilus AMP + diphosphate + L-isoleucyl-tRNAIle
-
 ?
6.1.1.5 additional information Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain Thermus thermophilus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.5 IleRS
-
 Thermus thermophilus
6.1.1.5 Isoleucyl-tRNA synthetase
-
 Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.5 37
-
 assay at Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.5 7.5
-
 assay at Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.5 ATP
-
 Thermus thermophilus