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Literature summary for 6.1.1.4 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)

Cloned (Comment) Organism
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

Protein Variants Comment Organism
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
R265A site-directed mutagenesis, the mutant shows reduced activity and abolished post-transfer editing activity compared to the wild-type enzyme Saccharomyces cerevisiae
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

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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

Synonyms Comment Organism
Leucyl-tRNA synthetase
-
Saccharomyces cerevisiae
LeuRS
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
Saccharomyces cerevisiae