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Literature summary for 6.1.1.4 extracted from

  • Hagiwara, Y.; Field, M.J.; Nureki, O.; Tateno, M.
    Editing mechanism of aminoacyl-tRNA synthetases operates by a hybrid ribozyme/protein catalyst (2010), J. Am. Chem. Soc., 132, 2751-2758.
    View publication on PubMed
Search for more literature for 6.1.1.4

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-leucine + tRNALeu Thermus thermophilus
-
 AMP + diphosphate + L-leucyl-tRNALeu
-
 ?

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-leucine + tRNALeu
-
 Thermus thermophilus AMP + diphosphate + L-leucyl-tRNALeu
-
 ?

Synonyms

Synonyms Comment Organism
Leucyl-tRNA synthetase
-
 Thermus thermophilus
LeuRS
-
 Thermus thermophilus
More the enzyme belongs to the class I aminoacyl-tRNA synthetases Thermus thermophilus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Thermus thermophilus

General Information

General Information Comment Organism
physiological function aminoacyl-tRNA synthetases are critical for the translational process, catalyzing the attachment of specific amino acids to their cognate tRNAs. To ensure formation of the correct aminoacyl-tRNA, and thereby enhance the reliability of translation, several aminoacyl-tRNA synthetases have an editing capability that hinders formation of misaminoacylated tRNAs, analysis of the mechanism of the editing reaction for class I enzyme leucyl-tRNA synthetase complexed with a misaminoacylated tRNALeu by initio hybrid quantum mechanical/molecular mechanical potentials in conjunction with molecular dynamics simulations, overview. Editing is a self-cleavage reaction of the tRNA and so it is the tRNA, and not the protein, that drives the reaction. The protein does, however, have an important stabilizing effect on some high-energy intermediates along the reaction path, which is more efficient than the ribozyme would be alone. This indicates that editing is achieved by a hybrid ribozyme/protein catalyst. The water molecule that acts as the nucleophile in the editing reaction is activated by a 3'-hydroxyl group at the 3'-end of tRNALeu and that the O2' atom of the leaving group of the substrate is capped by one of the water's hydrogen atoms Thermus thermophilus