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Literature summary for 6.3.4.19 extracted from

  • Nakanishi, K.; Bonnefond, L.; Kimura, S.; Suzuki, T.; Ishitani, R.; Nureki, O.
    Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase (2009), Nature, 461, 1144-1148.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overepression in Escherichia coli Geobacillus kaustophilus

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of Geobacillus kaustophilus TilS complexed with Bacillus subtilis tRNAIle CAU at 3.65 A resolution, by the multiwavelength anomalous dispersion method. The asymmetric unit contains one TilS homodimer and two tRNAs, each tightly embedded in one monomer of TilS, with an overall interface of 2998 A. Each monomer consists of an amino-terminal catalytic domain, and two carboxy-terminal domains, connected by a long a-helical linker and a loop linker, respectively Geobacillus kaustophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00008
-
precursor [tRNAIle2]-cytidine34 pH 7.8, 60°C Geobacillus kaustophilus
0.00014
-
mature [tRNAIle2]-cytidine34 pH 7.8, 60°C Geobacillus kaustophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[tRNAIle2]-cytidine34 + L-lysine + ATP Geobacillus kaustophilus
-
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Geobacillus kaustophilus Q5L3T3
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Geobacillus kaustophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
mature [tRNAIle2]-cytidine34 + L-lysine + ATP TilS can modify both types of tRNA, pre-tRNAIle2 and mature tRNAIle2, with comparable efficiencies. TilS specifically recognizes the entire L-shape structure in pre-tRNAIle2 through extensive interactions coupled with sequential domain movements. TilS prevents the recognition of tRNAIle2 by methionyl-tRNA synthetase and achieves high specificity for its substrate Geobacillus kaustophilus mature [tRNAIle2]-2-lysylcytidine34 + AMP + diphosphate
-
?
precursor [tRNAIle2]-cytidine34 + L-lysine + ATP TilS can modify both types of tRNA, pre-tRNAIle2 and mature tRNAIle2, with comparable efficiencies. TilS specifically recognizes the entire L-shape structure in pre-tRNAIle2 through extensive interactions coupled with sequential domain movements. TilS prevents the recognition of tRNAIle2 by methionyl-tRNA synthetase and achieves high specificity for its substrate Geobacillus kaustophilus precursor [tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
-
Geobacillus kaustophilus [tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
?

Synonyms

Synonyms Comment Organism
TilS
-
Geobacillus kaustophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.025
-
precursor [tRNAIle2]-cytidine34 pH 7.8, 60°C Geobacillus kaustophilus
0.03
-
mature [tRNAIle2]-cytidine34 pH 7.8, 60°C Geobacillus kaustophilus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
21.4
-
mature [tRNAIle2]-cytidine34 pH 7.8, 60°C Geobacillus kaustophilus
31.2
-
precursor [tRNAIle2]-cytidine34 pH 7.8, 60°C Geobacillus kaustophilus