Literature summary for 6.1.1.9 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.

Search for more literature for 6.1.1.9

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	P96142	-	-

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Release 2023.1 (January 2023)