Literature summary for 6.1.1.4 extracted from

Tan, M.; Zhu, B.; Zhou, X.L.; He, R.; Chen, X.; Eriani, G.; Wang, E.D.
tRNA-dependent pre-transfer editing by prokaryotic leucyl-tRNA synthetase (2010), J. Biol. Chem., 285, 3235-3244.

Search for more literature for 6.1.1.4

Activating Compound

Activating Compound	Comment	Organism	Structure
tRNALeu	presence of tRNALeu robustly stimulates editing activity	Escherichia coli
tRNALeu	presence of tRNALeu robustly stimulates editing activity	Aquifex aeolicus

Protein Variants

Protein Variants	Comment	Organism
T272R	no change in aminoacylation activity, but the deacylation of Ile-tRNALeu is strongly impaired. Mutant still exhibits 45% of wild-type AMP formation	Escherichia coli
T273R	no change in aminoacylation activity, but the deacylation of Ile-tRNALeu is strongly impaired. Mutant still exhibits 70% of wild-type AMP formation	Aquifex aeolicus

Inhibitors

Inhibitors	Comment	Organism	Structure
5-fluoro-1,3-dihydro-1-hydroxy-2,1-benzoxaborole	i.e. AN2690, 0.1 mM, 5fold decrease in aminoacylation activity	Escherichia coli
additional information	aminoacylation and editing reaction are resistant to inactivation by compound AN2690	Aquifex aeolicus

Organism

Organism	UniProt	Comment	Textmining
Aquifex aeolicus	-	-	-
Escherichia coli	-	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)