Literature summary for 6.1.1.4 extracted from

Fukunaga, R.; Yokoyama, S.
The C-terminal domain of the archaeal leucyl-tRNA synthetase prevents misediting of isoleucyl-tRNA(Ile) (2007), Biochemistry, 46, 4985-4996.

Search for more literature for 6.1.1.4

Protein Variants

Protein Variants	Comment	Organism
additional information	the deletion mutant lacking the C-terminal domain, LeuRSDELTA811-967, retains normal editing activity, but has severely reduced aminoacylation activity, deletion of amino acid residues 911-913 of LeuRS enhances the Ile-tRNAIle deacylation activity, without affecting the Ile-tRNALeu deacylation activity, a C-terminally truncated LeuRS can catalyze the first step of the aminoacylation reaction, Leu-AMP formation, but cannot catalyze the second step, transfer of Leu from Leu-AMP to tRNALeu, overview	Pyrococcus horikoshii

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.00167	-	tRNALeu	full-length enzyme, pH 7.5, 37°C	Pyrococcus horikoshii
0.00179	-	tRNALeu	truncation mutant DELTA911-913, pH 7.5, 37°C	Pyrococcus horikoshii

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	-	-	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	activity and specificity of several truncation and deletion mutants, overview	Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-leucine + tRNALeu	-	Pyrococcus horikoshii	AMP + diphosphate + L-leucyl-tRNALeu	-	?
ATP + L-leucine + tRNALeu	a two step reaction, the C-terminal domain recognizes the long variable arm of tRNALeu for aminoacylation, and the so-called editing domain deacylates incorrectly formed Ile-tRNALeu, structural superposition of tRNAIle onto the LeuRS-tRNALeu complex indicated that Ile911, Lys912, and Glu913 of the LeuRS C-terminal domain clash with U20 of tRNAIle, which is bulged out as compared to the corresponding nucleotide of tRNALeu, mechanism for prevention of misediting, overview	Pyrococcus horikoshii	AMP + diphosphate + L-leucyl-tRNALeu	-	?

Subunits

Subunits	Comment	Organism
More	enzyme structure and tRNA binding site, the requirement of the C-terminal domain for misediting prevention is unique to LeuR, overview	Pyrococcus horikoshii

Synonyms

Synonyms	Comment	Organism
Leucyl-tRNA synthetase	-	Pyrococcus horikoshii
LeuRS	-	Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Pyrococcus horikoshii
65	-	misformation assay at	Pyrococcus horikoshii

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
37	65	-	Pyrococcus horikoshii

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.177	-	tRNALeu	truncation mutant DELTA911-913, pH 7.5, 37°C	Pyrococcus horikoshii
0.331	-	tRNALeu	full-length enzyme, pH 7.5, 37°C	Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Pyrococcus horikoshii

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Pyrococcus horikoshii

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Release 2023.1 (January 2023)