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Literature summary for 6.1.1.4 extracted from

  • Yao, P.; Zhu, B.; Jaeger, S.; Eriani, G.; Wang, E.D.
    Recognition of tRNALeu by Aquifex aeolicus leucyl-tRNA synthetase during the aminoacylation and editing steps (2008), Nucleic Acids Res., 36, 2728-2738.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0011
-
L-leucine
-
Aquifex aeolicus

Organism

Organism UniProt Comment Textmining
Aquifex aeolicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-leucine + tRNALeu recognition of tRNALeu by the leucyl-tRNA synthetase (LeuRS) is studied by RNA probing and mutagenesis. Results show that the base A73, the core structure of tRNA formed by the tertiary interactions U8-A14, G18-U55 and G19-C56, and the orientation of the variable arm are critical elements for tRNALeu aminoacylation. Although dispensable for aminoacylation, the anticodon arm carries discrete editing determinants that are required for stabilizing the conformation of the post-transfer editing state and for promoting translocation of the tRNA acceptor arm from the synthetic to the editing site Aquifex aeolicus AMP + diphosphate + L-leucyl-tRNALeu
-
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Synonyms

Synonyms Comment Organism
AaLeuRS
-
Aquifex aeolicus
Leucyl-tRNA synthetase
-
Aquifex aeolicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
assay at Aquifex aeolicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.28
-
L-leucine
-
Aquifex aeolicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Aquifex aeolicus