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Literature summary extracted from

  • Bharatham, N.; Bharatham, K.; Lee, Y.; Woo Lee, K.
    Molecular dynamics simulation study of valyl-tRNA synthetase with its pre- and post-transfer editing substrates (2009), Biophys. Chem., 143, 34-43.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.9 expression in Escherichia coli Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.9 molecular dynamics simulation studies based on PDB structure ID 1wk9. Noncognate substrates Thr-AMP and Thr-A76, bind more strongly than the cognate substrates Val-AMP and Val-A76 in both pre- and post-transfer editing, respectivel Thermus thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.9 D279A editing site mutation, severely affects the binding ability of pre-transfer substrate Thr-AMP Thermus thermophilus
6.1.1.9 K270A editing site mutation, severely affects the binding ability of pre-transfer substrate Thr-AMP Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.9 Thermus thermophilus P96142
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