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Literature summary for 6.1.1.4 extracted from

  • Chen, J.F.; Guo, N.N.; Li, T.; Wang, E.D.; Wang, Y.L.
    CP1 domain in Escherichia coli leucyl-tRNA synthetase is crucial for its editing function (2000), Biochemistry, 39, 6726-6731.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of the His-tagged CP1 domain mutant and isolated CP1 domain in Escherichia coli strain JM109(DE3) Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information construction of an enzyme mutant with a duplication of the peptide fragment from Met238 to Pro368 within the CP1 domain which shows an activity reduced by 59% compared to the wild-type enzyme, and catalyzes the mischarging of tRNALeu by methionine or isoleucine due to impaired ability to edit incorrect products Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0015
-
tRNALeu aminoacylation reaction, wild-type enzyme, pH 7.8, 37°C Escherichia coli
0.0024
-
tRNALeu aminoacylation reaction, mutant enzyme, pH 7.8, 37°C Escherichia coli
0.015
-
L-leucine aminoacylation reaction, wild-type and mutant enzyme, pH 7.8, 37°C Escherichia coli
0.052
-
L-leucine ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.8, 37°C Escherichia coli
0.069
-
L-leucine ATP-diphosphate exchange reaction, mutant enzyme, pH 7.8, 37°C Escherichia coli
0.25
-
ATP aminoacylation reaction, mutant enzyme, pH 7.8, 37°C Escherichia coli
0.28
-
ATP aminoacylation reaction, wild-type enzyme, pH 7.8, 37°C Escherichia coli
2.8
-
L-isoleucine ATP-diphosphate exchange reaction, mutant enzyme, pH 7.8, 37°C Escherichia coli
3.5
-
L-isoleucine ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.8, 37°C Escherichia coli
6.2
-
L-methionine ATP-diphosphate exchange reaction, mutant enzyme, pH 7.8, 37°C Escherichia coli
7.5
-
L-methionine ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.8, 37°C Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-leucine + tRNALeu Escherichia coli
-
AMP + diphosphate + L-leucyl-tRNALeu
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged mutant and His-tagged CP1 domain expressed in Escherichia coli strain Jm109(DE3), to electrophoretic homogeneity Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.79
-
recombinant CP1 domain mutant Escherichia coli
1.5
-
about, wild-type enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-isoleucine + tRNALeu wild-type and CP1 domain mutant enzyme, the mischarged product can be edited by the wild-type enzyme, but not by a recombinant isolated CP1 domain Escherichia coli AMP + diphosphate + L-isoleucyl-tRNALeu
-
?
ATP + L-leucine + tRNALeu
-
Escherichia coli AMP + diphosphate + L-leucyl-tRNALeu
-
?
ATP + L-leucine + tRNALeu two-step reaction, the connecting peptide CP1 domain is crucial for the editing function Escherichia coli AMP + diphosphate + L-leucyl-tRNALeu
-
?
ATP + L-methionine + tRNALeu wild-type and CP1 domain mutant enzyme, the mischarged product can be edited by the wild-type enzyme, but not by a recombinant isolated CP1 domain Escherichia coli AMP + diphosphate + L-methionyl-tRNALeu
-
?
additional information the enzyme also performs the ATP-diphosphate exchange reaction Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
More determination of secondary structure elements in the wild-type and mutant enzyme Escherichia coli

Synonyms

Synonyms Comment Organism
Leucine translase
-
Escherichia coli
Leucine--tRNA ligase
-
Escherichia coli
Leucyl-transfer ribonucleate synthetase
-
Escherichia coli
Leucyl-transfer ribonucleic acid synthetase
-
Escherichia coli
Leucyl-transfer RNA synthetase
-
Escherichia coli
Leucyl-tRNA synthetase
-
Escherichia coli
LeuRS
-
Escherichia coli
Synthetase, leucyl-transfer ribonucleate
-
Escherichia coli

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3
-
tRNALeu mutant enzyme, pH 7.8, 37°C Escherichia coli
1.5
-
L-leucine mutant enzyme, pH 7.8, 37°C Escherichia coli
1.6
-
ATP mutant enzyme, pH 7.8, 37°C Escherichia coli
2.9
-
tRNALeu wild-type enzyme, pH 7.8, 37°C Escherichia coli
3
-
L-leucine wild-type enzyme, pH 7.8, 37°C Escherichia coli
3.6
-
ATP wild-type enzyme, pH 7.8, 37°C Escherichia coli
6.9
-
L-isoleucine ATP-diphosphate exchange reaction, mutant enzyme, pH 7.8, 37°C Escherichia coli
7.6
-
L-methionine ATP-diphosphate exchange reaction, mutant enzyme, pH 7.8, 37°C Escherichia coli
18
-
L-isoleucine ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.8, 37°C Escherichia coli
19
-
L-methionine ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.8, 37°C Escherichia coli
101
-
L-leucine ATP-diphosphate exchange reaction, mutant enzyme, pH 7.8, 37°C Escherichia coli
171
-
L-leucine ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.8, 37°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli