Literature summary for 6.1.1.4 extracted from

Hsu, J.L.; Martinis, S.A.
A flexible peptide tether controls accessibility of a unique C-terminal RNA-binding domain in Leucyl-tRNA synthetases (2008), J. Mol. Biol., 376, 482-491.

Search for more literature for 6.1.1.4

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli as a His-tagged fusion protein	Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
DELTA788-798	partial deletion of the C-terminal domain peptide linker shows that as the length of the peptide linker decreases, aminoacylation activity decreases. This mutant shows almost no aminoacylation activity. Mutant shows reduced deacylation activity against mischarged Ile-tRNALeu	Escherichia coli
DELTA790-798	partial deletion of the C-terminal domain peptide linker shows that as the length of the peptide linker decreases, aminoacylation activity decreases. Mutant shows reduced deacylation activity against mischarged Ile-tRNALeu	Escherichia coli
DELTA792-798	partial deletion of the C-terminal domain peptide linker shows that as the length of the peptide linker decreases, aminoacylation activity decreases. Mutant retains significant deacylation activity against mischarged Ile-tRNALeu	Escherichia coli
DELTA793	single-site deletion at the more flexible end of the peptide linker: no significant change in aminoacylation activity	Escherichia coli
DELTA794	single-site deletion at the more flexible end of the peptide linker: no significant change in aminoacylation activity	Escherichia coli
DELTA794-798	partial deletion of the C-terminal domain peptide linker shows that as the length of the peptide linker decreases, aminoacylation activity decreases. Mutant retains significant deacylation activity against mischarged Ile-tRNALeu	Escherichia coli
DELTA795	single-site deletion at the more flexible end of the peptide linker: no significant change in aminoacylation activity	Escherichia coli
DELTA795-796	two-site deletion at the more flexible end of the peptide linker: no significant change in aminoacylation activity	Escherichia coli
DELTA795-798	partial deletion of the C-terminal domain peptide linker shows that as the length of the peptide linker decreases, aminoacylation activity decreases. Mutant retains significant deacylation activity against mischarged Ile-tRNALeu	Escherichia coli
DELTA796	single-site deletion at the more flexible end of the peptide linker: no significant change in aminoacylation activity	Escherichia coli
DELTA796-798	partial deletion of the C-terminal domain peptide linker shows that as the length of the peptide linker decreases, aminoacylation activity decreases. Mutant retains significant deacylation activity against mischarged Ile-tRNALeu	Escherichia coli
DELTA796-798	two-site deletion at the more flexible end of the peptide linker: mutant exhibits lower aminoacylation activity compared to wild-type	Escherichia coli
DELTA797	single-site deletion at the more flexible end of the peptide linker: no significant change in aminoacylation activity	Escherichia coli
DELTA797-798	two-site deletion at the more flexible end of the peptide linker: mutant exhibits lower aminoacylation activity compared to wild-type	Escherichia coli
DELTA819-828	deletion of the C-terminal domain peptide linker stimulates aminoacylation and editing activity shows that as the length of the peptide linker decreases, aminoacylation activity decreases. Mutant retains significant deacylation activity against mischarged Ile-tRNALeu	Saccharomyces cerevisiae
E797GGG	mutant shows no altered aminoacylation activity compared to wild-type	Escherichia coli
E797PPP	mutant shows no altered aminoacylation activity compared to wild-type	Escherichia coli
additional information	a series of deletions and chimeric variations in the peptide linker of the yeast mitochondrial LeuRS chimeric mutant that is fused to the Escherichia coli LeuRS C-terminal domain extension are created: a four residue deletion mutant of the yeast mitochondrial LeuRS chimera (Ym EcCTD Delta4) stimulates aminoacylation activity significantly compared to that of the chimera enzyme with no deletion within the linker peptide	Saccharomyces cerevisiae
additional information	an eight residue peptide linker deletion mutant that contains three (Ym EcCTD DELTA8/+3), six (Ym EcCTD DELTA8/+6), or nine (Ym EcCTD DELTA8/+9) residues from the Escherichia coli LeuRS linker peptide restors protein stability and activity. Within these three chimeric peptide linker swaps, successive increases in the length of the Escherichia coli chimeric peptide linker decreases aminoacylation activity progressively	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Saccharomyces cerevisiae	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
purified by affinity chromatography using His-select resin	Escherichia coli
purified by affinity chromatography using His-select resin	Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-leucine + tRNALeu	-	Escherichia coli	AMP + diphosphate + L-leucyl-tRNALeu	-	?
ATP + L-leucine + tRNALeu	-	Saccharomyces cerevisiae	AMP + diphosphate + L-leucyl-tRNALeu	-	?

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
additional information	-	assay carried out at room temperature	Escherichia coli
additional information	-	assay carried out at room temperature	Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Escherichia coli
7.5	-	assay at	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)