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Literature summary for 6.1.1.4 extracted from

  • Lincecum, T.L., Jr.; Tukalo, M.; Yaremchuk, A.; Mursinna, R.S.; Williams, A.M.; Sproat, B.S.; Van Den Eynde, W.; Link, A.; Van Calenbergh, S.; Grotli, M.; Martinis, S.A.; Cusack, S.
    Structural and mechanistic basis of pre- and posttransfer editing by leucyl-tRNA synthetase (2003), Mol. Cell, 11, 951-963.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene CDC60, expression of wild-type and mutants in an Escherichia coli BL21 strain Saccharomyces cerevisiae
gene leuS, expression in a BL21 strain Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal growth in presence of mercuric chloride, soaking of the crystals in solution containing 0.6 mM of the non-hydrolyzable substrate analogue norvaline-AMS for 1 month, or cocrystallization of enzyme and norvaline-AMS, X-ray diffraction structure determinationat 2.0-2.2 A resolution and analysis Thermus thermophilus

Protein Variants

Protein Variants Comment Organism
D345A mutation of the highly conserved Asp residue, located in the CP1 domain, is responsible for editing mechanism, slightly reduced activity with L-leucine, mutant mischarges tRNALeu with isoleucine Escherichia coli
D347A mutation of the highly conserved Asp residue, located in the CP1 domain, is responsible for editing mechanism, slightly reduced activity with L-leucine, mutant mischarges tRNALeu with isoleucine Thermus thermophilus
D419A mutation of the highly conserved Asp residue, located in the CP1 domain, is responsible for editing mechanism, slightly reduced activity with L-leucine, mutant mischarges tRNALeu with isoleucine Saccharomyces cerevisiae
T252A decreased activity with L-leucine, mutant shows altered editing specificity, it edits correctly formed leucyl-tRNALeu Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
O-[N-(L-norvalyl)sulfamoyl]adenosine analogue to the reaction intermediate, non-hydrolyzable Thermus thermophilus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Saccharomyces cerevisiae 5737
-

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
-
r
ATP + L-leucine + tRNALeu Saccharomyces cerevisiae
-
AMP + diphosphate + L-leucyl-tRNALeu
-
r
ATP + L-leucine + tRNALeu Thermus thermophilus
-
AMP + diphosphate + L-leucyl-tRNALeu
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Saccharomyces cerevisiae
-
-
-
Thermus thermophilus Q72GM3 purified recombinant enzyme
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Escherichia coli
recombinant from Escherichia coli Saccharomyces cerevisiae

Reaction

Reaction Comment Organism Reaction ID
ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu active site structure and mechanism, the editing active site binds the two different substrates using a single amino acid discriminatory pocket while preserving he same mode of adenine recognition, Asp347 is involved in the editing process, mechanism of hydrolysis Thermus thermophilus
ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu Asp345 is involved in the editing process, mechanism of hydrolysis Escherichia coli
ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu Asp419 is involved in the editing process, mechanism of hydrolysis Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-isoleucine + tRNALeu mutant D345A, not the wild-type which performs only the misacetylation with isoleucine, but eliminates the incorrect isoleucyl-AMP Escherichia coli AMP + diphosphate + L-isoleucyl-tRNALeu
-
r
ATP + L-isoleucine + tRNALeu mutant D345A, not the wild-type which performs only the misacetylation with isoleucine, but eliminates the incorrect isoleucyl-AMP Thermus thermophilus AMP + diphosphate + L-isoleucyl-tRNALeu
-
r
ATP + L-isoleucine + tRNALeu mutant D419A, not the wild-type, which performs only the misacetylation with isoleucine, but eliminates the incorrect isoleucyl-AMP Saccharomyces cerevisiae AMP + diphosphate + L-isoleucyl-tRNALeu
-
r
ATP + L-leucine + tRNALeu
-
Escherichia coli AMP + diphosphate + L-leucyl-tRNALeu
-
r
ATP + L-leucine + tRNALeu
-
Saccharomyces cerevisiae AMP + diphosphate + L-leucyl-tRNALeu
-
r
ATP + L-leucine + tRNALeu
-
Thermus thermophilus AMP + diphosphate + L-leucyl-tRNALeu
-
r
ATP + L-leucine + tRNALeu mutant T252A edits correctly charged Leu-tRNALeu Escherichia coli AMP + diphosphate + L-leucyl-tRNALeu
-
r
ATP + L-leucine + tRNALeu the editing active site hydrolytically cleaves the misactivated aminoacyl-adenylate, called pre-transfer editing, or the mischarged tRNA, called post-transfer editing Thermus thermophilus AMP + diphosphate + L-leucyl-tRNALeu
-
r
ATP + L-methionine + tRNALeu mutant D345A, not the wild-type enzyme Escherichia coli AMP + diphosphate + L-methionyl-tRNALeu
-
r
ATP + L-methionine + tRNALeu mutant D419A, not the wild-type enzyme Saccharomyces cerevisiae AMP + diphosphate + L-methionyl-tRNALeu
-
r

Synonyms

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli
ATP
-
Saccharomyces cerevisiae
ATP
-
Thermus thermophilus