Literature summary for 6.1.1.4 extracted from

Liu, Y.; Liao, J.; Zhu, B.; Wang, E.; Ding, J.
Crystal structures of the editing domain of E. coli leucyl-tRNA synthetase and its complexes with methionine and isoleucine reveal a lock-and-key mechanism for amino acid discrimination (2006), Biochem. J., 394, 399-407.

Search for more literature for 6.1.1.4

Cloned(Commentary)

Cloned (Comment)	Organism
the gene fragment encoding the editing domain (residues 228-413) is subcloned into the pET3E-His expression plasmid. The plasmid is transformed into the Escherichia coli BL-21(DE3) strain	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of editing domain of Escherichia coli LeuRS in both apo form and complexes with methionine and isoleucine at 2.0 A, 2.4 A, and 3.2 A resolution, hanging drop vapour diffusion method	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P07813	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-leucine + tRNALeu	it is proposed that the enzyme uses a lock-and-key mechanism to recognize and discriminate the amino acids	Escherichia coli	AMP + diphosphate + L-leucyl-tRNALeu	-	?

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Release 2023.1 (January 2023)