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Literature summary 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)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.4 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

EC Number Protein Variants Comment Organism
6.1.1.4 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
6.1.1.4 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
6.1.1.4 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
6.1.1.4 T252A decreased activity with L-leucine, mutant shows altered editing specificity, it edits correctly formed leucyl-tRNALeu Escherichia coli

Inhibitors

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

Localization

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.4 ATP + L-leucine + tRNALeu Escherichia coli
-
 AMP + diphosphate + L-leucyl-tRNALeu
-
 r
6.1.1.4 ATP + L-leucine + tRNALeu Saccharomyces cerevisiae
-
 AMP + diphosphate + L-leucyl-tRNALeu
-
 r
6.1.1.4 ATP + L-leucine + tRNALeu Thermus thermophilus
-
 AMP + diphosphate + L-leucyl-tRNALeu
-
 r

Organism

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

Purification (Commentary)

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

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.4 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
a
6.1.1.4 ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu Asp345 is involved in the editing process, mechanism of hydrolysis Escherichia coli
a
6.1.1.4 ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu Asp419 is involved in the editing process, mechanism of hydrolysis Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.4 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
6.1.1.4 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
6.1.1.4 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
6.1.1.4 ATP + L-leucine + tRNALeu
-
 Escherichia coli AMP + diphosphate + L-leucyl-tRNALeu
-
 r
6.1.1.4 ATP + L-leucine + tRNALeu
-
 Saccharomyces cerevisiae AMP + diphosphate + L-leucyl-tRNALeu
-
 r
6.1.1.4 ATP + L-leucine + tRNALeu
-
 Thermus thermophilus AMP + diphosphate + L-leucyl-tRNALeu
-
 r
6.1.1.4 ATP + L-leucine + tRNALeu mutant T252A edits correctly charged Leu-tRNALeu Escherichia coli AMP + diphosphate + L-leucyl-tRNALeu
-
 r
6.1.1.4 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
6.1.1.4 ATP + L-methionine + tRNALeu mutant D345A, not the wild-type enzyme Escherichia coli AMP + diphosphate + L-methionyl-tRNALeu
-
 r
6.1.1.4 ATP + L-methionine + tRNALeu mutant D419A, not the wild-type enzyme Saccharomyces cerevisiae AMP + diphosphate + L-methionyl-tRNALeu
-
 r

Synonyms

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.4 7.5
-
 assay at Escherichia coli
6.1.1.4 7.5
-
 assay at Saccharomyces cerevisiae
6.1.1.4 7.5
-
 assay at Thermus thermophilus

Cofactor

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