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Literature summary extracted from

  • Karkhanis, V.A.; Boniecki, M.T.; Poruri, K.; Martinis, S.A.
    A viable amino acid editing activity in the leucyl-tRNA synthetase CP1-splicing domain is not required in the yeast mitochondria (2006), J. Biol. Chem., 281, 33217-33225.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.4 expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), complementation abilities of wild-type and mutant enzymes of yeast null strain HM402 and Escherichia coli strain KL321, overview Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.4 D357A site-directed mutagenesis, the mutant shows reduced activity and abolished editing activity and misaminoacylated isoleucine to tRNALeu compared to the wild-type enzyme Saccharomyces cerevisiae
6.1.1.4 R265A site-directed mutagenesis, the mutant shows reduced activity and abolished post-transfer editing activity compared to the wild-type enzyme Saccharomyces cerevisiae
6.1.1.4 T263V/T264V site-directed mutagenesis, the mutant shows reduced activity and decreased post-transfer editing activity compared to the wild-type enzyme Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.1.1.4 mitochondrion
-
 Saccharomyces cerevisiae 5739
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.4 Mg2+
-
 Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.4 ATP + L-leucine + tRNALeu Saccharomyces cerevisiae possibly the yeast mitochondria have evolved to tolerate lower levels of fidelity in protein synthesis or have developed alternate mechanisms to enhance discrimination of leucine from non-cognate amino acids that can be misactivated by leucyl-tRNA synthetase AMP + diphosphate + L-leucyl-tRNALeu
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.4 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.4 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.4 ATP + L-leucine + tRNALeu possibly the yeast mitochondria have evolved to tolerate lower levels of fidelity in protein synthesis or have developed alternate mechanisms to enhance discrimination of leucine from non-cognate amino acids that can be misactivated by leucyl-tRNA synthetase Saccharomyces cerevisiae AMP + diphosphate + L-leucyl-tRNALeu
-
 ?
6.1.1.4 ATP + L-leucine + tRNALeu LeuRS has a hydrolytic active site that resides in a discrete amino acid editing domain called CP1, LeuRS misactivates many non-leucine amino acids, including isoleucine, valine, methionine, and also structurally similar metabolic cellular intermediate, but the enzyme has an editing active site that is competent for post-transfer editing of mischarged tRNA Saccharomyces cerevisiae AMP + diphosphate + L-leucyl-tRNALeu
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.4 Leucyl-tRNA synthetase
-
 Saccharomyces cerevisiae
6.1.1.4 LeuRS
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.4 37
-
 assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.4 7.5
-
 assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.4 ATP
-
 Saccharomyces cerevisiae