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Literature summary for 2.3.2.22 extracted from

  • Bonnefond, L.; Arai, T.; Sakaguchi, Y.; Suzuki, T.; Ishitani, R.; Nureki, O.
    Structural basis for nonribosomal peptide synthesis by an aminoacyl-tRNA synthetase paralog (2011), Proc. Natl. Acad. Sci. USA, 108, 3912-3917.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
in the apo form and complexed with substrate mimics, at 1.7-2.4 A resolutions. Data show the presence of an aminoacyl-enzyme reaction intermediate, but not a dipeptide tRNA intermediate. Reaction follows a sequential catalytic mechanism, with the successive attachment of two leucine residues on the enzyme via a conserved serine residue Bacillus licheniformis

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis Q65EX3
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Bacillus licheniformis ATCC 14580 Q65EX3
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Reaction

Reaction Comment Organism Reaction ID
2 L-leucyl-tRNALeu = 2 tRNALeu + cyclo(L-leucyl-L-leucyl) sequential catalytic mechanism, with the successive attachment of two leucine residues on the enzyme via a conserved serine residue Bacillus licheniformis

Synonyms

Synonyms Comment Organism
YvmC
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Bacillus licheniformis