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Literature summary for 6.1.1.4 extracted from

  • Mascarenhas, A.P.; Martinis, S.A.
    A glycine hinge for tRNA-dependent translocation of editing substrates to prevent errors by leucyl-tRNA synthetase (2009), FEBS Lett., 583, 3443-3447.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
G225P abolishes tRNA leucylation due to a defect in leucine activation, decrease in deacylation of Ile-tRNALeu Escherichia coli
G229P increased aminoacylation activity compared to the wild-type, mutant deacylates Ile-tRNALeu similar to wild-type Escherichia coli
G229P/T252A double mutant rescues leucylation activity to levels comparable to wild-type and retains deacylation activity of LeutRNALeu that is characteristic of the T252A mutation Escherichia coli
G407P aminoacylates tRNALeu and decylates Ile-tRNALeu as well as wild-type Escherichia coli
G409P increased aminoacylation activity compared to the wild-type, mutant deacylates Ile-tRNALeu similar to wild-type Escherichia coli
G409P/T252A double mutant fails to rescue the T252A mutation in LeuRS Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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