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Literature summary for 6.1.1.4 extracted from

  • Hsu, J.L.; Rho, S.B.; Vannella, K.M.; Martinis, S.A.
    Functional divergence of a unique C-terminal domain of leucyl-tRNA synthetase to accommodate its splicing and aminoacylation roles (2006), J. Biol. Chem., 281, 23075-23082.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
DTT
-
Escherichia coli
DTT
-
Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Escherichia coli
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
K809A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli
K846A site-directed mutagenesis, the mutant shows increased activity compared to the wild-typ enzyme Escherichia coli
K846A/K853A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli
K846E site-directed mutagenesis, the mutant shows similar activity compared to the wild-typ enzyme Escherichia coli
K846E/K853E site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli
K853A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-typ enzyme Escherichia coli
K853E site-directed mutagenesis, the mutant shows increased activity compared to the wild-typ enzyme Escherichia coli
L854A site-directed mutagenesis, the mutant shows increased activity compared to the wild-typ enzyme Escherichia coli
L855A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli
additional information deletions of the C terminus differentially impact the two functions of the enzyme in splicing and aminoacylation in vivo, overview, a five-amino acid C-terminal deletion of LeuRS, which does not complement a null strain, can form a ternary complex with the bI4 intron and its maturase splicing partner, however, the complex fails to stimulate splicing activity, deletion of the C-terminal domain of LeuRS abolishes aminoacylation of tRNALeu and also amino acid editing of mischarged tRNA molecules, overview Escherichia coli
additional information deletions of the C terminus differentially impact the two functions of the enzyme in splicing and aminoacylation in vivo, overview, a five-amino acid C-terminal deletion of LeuRS, which does not complement a null strain, can form a ternary complex with the bI4 intron and its maturase splicing partner, however, the complex fails to stimulate splicing activity, deletion of the entire yeast mitochondrial LeuRS C-terminal domain enhances its aminoacylation and amino acid editing activities Saccharomyces cerevisiae
N807A site-directed mutagenesis, the mutant shows similar activity compared to the wild-typ enzyme Escherichia coli
N807A/N856A site-directed mutagenesis, the mutant shows similar activity compared to the wild-typ enzyme Escherichia coli
N856A site-directed mutagenesis, the mutant shows increased activity compared to the wild-typ enzyme Escherichia coli
Q805A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli
Q805A/N807A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli
Q805A/N807A/N856A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli
R811A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of wild-type and mutant enzymes, overview Escherichia coli

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Escherichia coli
Mg2+
-
Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-leucine + tRNALeu Escherichia coli two functions of the enzyme in splicing and aminoacylation in vivo, overview AMP + diphosphate + L-leucyl-tRNALeu
-
?
ATP + L-leucine + tRNALeu Saccharomyces cerevisiae two functions of the enzyme in splicing and aminoacylation in vivo, overview AMP + diphosphate + L-leucyl-tRNALeu
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
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 Escherichia coli
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-leucine + tRNALeu
-
Escherichia coli AMP + diphosphate + L-leucyl-tRNALeu
-
?
ATP + L-leucine + tRNALeu
-
Saccharomyces cerevisiae AMP + diphosphate + L-leucyl-tRNALeu
-
?
ATP + L-leucine + tRNALeu two functions of the enzyme in splicing and aminoacylation in vivo, overview Escherichia coli AMP + diphosphate + L-leucyl-tRNALeu
-
?
ATP + L-leucine + tRNALeu two functions of the enzyme in splicing and aminoacylation in vivo, overview Saccharomyces cerevisiae AMP + diphosphate + L-leucyl-tRNALeu
-
?

Subunits

Subunits Comment Organism
More primary and tertiary structures of the LeuRS unique C-terminal domain, overview, the C-terminal extension of about 60 amino acids forms a discrete domain, which is unique among the LeuRSs and interacts with the corner of the L-shaped tRNALeu, overview Escherichia coli
More primary and tertiary structures of the LeuRS unique C-terminal domain, overview, the C-terminal extension of about 60 amino acids forms a discrete domain, which is unique among the LeuRSs and interacts with the corner of the L-shaped tRNALeu, overview Saccharomyces cerevisiae

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli
ATP
-
Saccharomyces cerevisiae