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Literature summary extracted from

  • Nawaz, M.H.; Pang, Y.L.; Martinis, S.A.
    Molecular and functional dissection of a putative RNA-binding region in yeast mitochondrial leucyl-tRNA synthetase (2007), J. Mol. Biol., 367, 384-394.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.4 R449A site-directed mutagenesis, nearly inactive mutant Saccharomyces cerevisiae
6.1.1.4 R449E site-directed mutagenesis, mutation within the RDW peptide, no complementation of the null mutant strain QBY320 Saccharomyces cerevisiae
6.1.1.4 R449K site-directed mutagenesis, mutation within the RDW peptide, no complementation of the null mutant strain QBY320, 30fold reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
6.1.1.4 R451A site-directed mutagenesis, nearly inactive mutant Saccharomyces cerevisiae
6.1.1.4 R451E site-directed mutagenesis, mutation within the RDW peptide, no complementation of the null mutant strain QBY320 Saccharomyces cerevisiae
6.1.1.4 R451K site-directed mutagenesis, mutation within the RDW peptide, complementation of the null mutant strain QBY320, 11fold reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
6.1.1.4 W445A site-directed mutagenesis, nearly inactive mutant Saccharomyces cerevisiae
6.1.1.4 W445F site-directed mutagenesis, mutation within the RDW peptide, no complementation of the null mutant strain QBY320 Saccharomyces cerevisiae
6.1.1.4 W445H site-directed mutagenesis, mutation within the RDW peptide, no complementation of the null mutant strain QBY320 Saccharomyces cerevisiae
6.1.1.4 W445K site-directed mutagenesis, mutation within the RDW peptide, no complementation of the null mutant strain QBY320 Saccharomyces cerevisiae
6.1.1.4 W445Y site-directed mutagenesis, mutation within the RDW peptide, weak complementation of the null mutant strain QBY320, 30fold reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae

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 recombinant wild-type and mutant enzymes Saccharomyces cerevisiae
6.1.1.4 0.0002
-
 tRNALeu mutant R449K Saccharomyces cerevisiae
6.1.1.4 0.0005
-
 tRNALeu mutant W445Y Saccharomyces cerevisiae
6.1.1.4 0.0006
-
 tRNALeu wild-type enzyme Saccharomyces cerevisiae
6.1.1.4 0.0007
-
 tRNALeu mutant R451K 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
-
 AMP + diphosphate + L-leucyl-tRNALeu
-
 ?

Organism

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.1.1.4 additional information
-
-
 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
-
 Saccharomyces cerevisiae AMP + diphosphate + L-leucyl-tRNALeu
-
 ?
6.1.1.4 ATP + L-leucine + tRNALeu a two step reaction, the first of which is reversible, aminoacylation and editing by LeuRS require migration of the tRNA acceptor stem end between the canonical aminoacylation core and a separate domain called CP1 that is responsible for amino acid editing, post-transfer editing mechanism., overview Saccharomyces cerevisiae AMP + diphosphate + L-leucyl-tRNALeu
-
 ?
6.1.1.4 additional information the LeuRS CP1 domain can also support group I intron RNA splicing in the yeast mitochondria, overview, the RDW peptide, a highly conserved peptide within an RDW-containing motif, is important for enzyme interactions, the RDW peptide is dynamic and forms unique sets of interactions with the aminoacylation and editing complexes, overview Saccharomyces cerevisiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.4 More primary and tertiary structure, overview, the RDW peptide, a highly conserved peptide within an RDW-containing motif, is important for enzyme interactions, overview Saccharomyces cerevisiae

Synonyms

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.4 0.05
-
 tRNALeu mutant R449K Saccharomyces cerevisiae
6.1.1.4 0.2
-
 tRNALeu mutant W445Y Saccharomyces cerevisiae
6.1.1.4 0.6
-
 tRNALeu mutant R451K Saccharomyces cerevisiae
6.1.1.4 5
-
 tRNALeu wild-type enzyme Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.4 ATP
-
 Saccharomyces cerevisiae