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Literature summary for 6.1.1.4 extracted from

  • Xu, M.G.; Li, J.; Du, X.; Wang, E.D.
    Groups on the side chain of T252 in Escherichia coli leucyl-tRNA synthetase are important for discrimination of amino acids and cell viability (2004), Biochem. Biophys. Res. Commun., 318, 11-16.
    View publication on PubMed
Search for more literature for 6.1.1.4

Protein Variants

Protein Variants Comment Organism
T252D mutation results in isoleucylation of tRNALeu, editing activity is impaired, ATP hydrolysis in presence of norvaline is 27% of the wild-type value, ATP hydrolysis in presence of leucine is 98% of the wild-type value Escherichia coli
T252E mutation results in isoleucylation of tRNALeu, editing activity is impaired, ATP hydrolysis in presence of norvaline is 18% of the wild-type value, ATP hydrolysis in presence of leucine is 86% of the wild-type value Escherichia coli
T252G the mutant enzyme, like the native enzyme, does not mischarge tRNALeu with isoleucine, ATP hydrolysis in presence of norvaline is 2.1fold higher than wild-type value, ATP hydrolysis in presence of leucine is 60% of the wild-type value Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0025
-
 tRNALeu 37°C, pH 7.8, mutant enzyme T25D Escherichia coli
0.0026
-
 tRNALeu 37°C, pH 7.8, native enzyme Escherichia coli
0.0033
-
 tRNALeu 37°C, pH 7.8, mutant enzyme T252E Escherichia coli
0.019
-
 L-leucine 37°C, pH 7.8, mutant enzyme T252E Escherichia coli
0.019
-
 L-leucine 37°C, pH 7.8, mutant enzyme T25D Escherichia coli
0.02
-
 L-leucine 37°C, pH 7.8, native enzyme Escherichia coli
0.22
-
 ATP 37°C, pH 7.8, mutant enzyme T252E Escherichia coli
0.23
-
 ATP 37°C, pH 7.8, mutant enzyme T25D Escherichia coli
0.24
-
 ATP 37°C, pH 7.8, native enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-isoleucine + tRNALeu activity with mutant enzymes T252E and T252D, no activity with wild-type enzyme and with mutant enzyme T252G Escherichia coli AMP + diphosphate + L-isoleucyl-tRNALeu
-
 ?
ATP + L-leucine + tRNALeu
-
 Escherichia coli AMP + diphosphate + L-leucyl-tRNALeu
-
 ?

Synonyms

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.6
-
 L-leucine 37°C, pH 7.8, mutant enzyme T25D Escherichia coli
4.7
-
 tRNALeu 37°C, pH 7.8, mutant enzyme T25D Escherichia coli
4.8
-
 ATP 37°C, pH 7.8, mutant enzyme T25D Escherichia coli
4.9
-
 ATP 37°C, pH 7.8, mutant enzyme T252E Escherichia coli
4.9
-
 L-leucine 37°C, pH 7.8, mutant enzyme T252E Escherichia coli
5
-
 ATP 37°C, pH 7.8, native enzyme Escherichia coli
5.1
-
 tRNALeu 37°C, pH 7.8, mutant enzyme T252E Escherichia coli
5.1
-
 L-leucine 37°C, pH 7.8, native enzyme Escherichia coli
5.1
-
 tRNALeu 37°C, pH 7.8, native enzyme Escherichia coli