Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

EC Number Activating Compound Comment Organism Structure
6.1.1.4 DTT
-
 Escherichia coli
6.1.1.4 DTT
-
 Saccharomyces cerevisiae

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

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.4 K809A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli
6.1.1.4 K846A site-directed mutagenesis, the mutant shows increased activity compared to the wild-typ enzyme Escherichia coli
6.1.1.4 K846A/K853A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli
6.1.1.4 K846E site-directed mutagenesis, the mutant shows similar activity compared to the wild-typ enzyme Escherichia coli
6.1.1.4 K846E/K853E site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli
6.1.1.4 K853A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-typ enzyme Escherichia coli
6.1.1.4 K853E site-directed mutagenesis, the mutant shows increased activity compared to the wild-typ enzyme Escherichia coli
6.1.1.4 L854A site-directed mutagenesis, the mutant shows increased activity compared to the wild-typ enzyme Escherichia coli
6.1.1.4 L855A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli
6.1.1.4 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
6.1.1.4 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
6.1.1.4 N807A site-directed mutagenesis, the mutant shows similar activity compared to the wild-typ enzyme Escherichia coli
6.1.1.4 N807A/N856A site-directed mutagenesis, the mutant shows similar activity compared to the wild-typ enzyme Escherichia coli
6.1.1.4 N856A site-directed mutagenesis, the mutant shows increased activity compared to the wild-typ enzyme Escherichia coli
6.1.1.4 Q805A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli
6.1.1.4 Q805A/N807A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli
6.1.1.4 Q805A/N807A/N856A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli
6.1.1.4 R811A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-typ enzyme Escherichia coli

KM Value [mM]

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

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+
-
 Escherichia coli
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 Escherichia coli two functions of the enzyme in splicing and aminoacylation in vivo, overview AMP + diphosphate + L-leucyl-tRNALeu
-
 ?
6.1.1.4 ATP + L-leucine + tRNALeu Saccharomyces cerevisiae two functions of the enzyme in splicing and aminoacylation in vivo, overview AMP + diphosphate + L-leucyl-tRNALeu
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.4 Escherichia coli
-
-
-
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 Escherichia coli
6.1.1.4 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography 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
-
 Escherichia coli AMP + diphosphate + L-leucyl-tRNALeu
-
 ?
6.1.1.4 ATP + L-leucine + tRNALeu
-
 Saccharomyces cerevisiae AMP + diphosphate + L-leucyl-tRNALeu
-
 ?
6.1.1.4 ATP + L-leucine + tRNALeu two functions of the enzyme in splicing and aminoacylation in vivo, overview Escherichia coli AMP + diphosphate + L-leucyl-tRNALeu
-
 ?
6.1.1.4 ATP + L-leucine + tRNALeu two functions of the enzyme in splicing and aminoacylation in vivo, overview Saccharomyces cerevisiae AMP + diphosphate + L-leucyl-tRNALeu
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.4 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
6.1.1.4 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

EC Number Synonyms Comment Organism
6.1.1.4 Leucyl-tRNA synthetase
-
 Escherichia coli
6.1.1.4 Leucyl-tRNA synthetase
-
 Saccharomyces cerevisiae
6.1.1.4 LeuRS
-
 Escherichia coli
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 Escherichia coli
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 Escherichia coli
6.1.1.4 7.5
-
 assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.4 ATP
-
 Escherichia coli
6.1.1.4 ATP
-
 Saccharomyces cerevisiae